DESCRIPTION

PROTEINS AND ENZYMES

A0018 a1-acid glycoprotein (orosomucoid) from bovine plasma. Molecular weight 38-40 kDa. Isoelectric point 2.7, E1%280 nm= 8.1. The preparation is homogeneous by electrophoresis in 8.0 % PAAG conducted according to Davis. The protein may be useful for affinity purification of some lectins and also for separation of chiral compounds by chromatography.
Hermansson J et al Separation of chiral compounds with a1-acid glycoprotein as selector Chem Anal NY 1989, v. 98 (HPLC) 337-374
A0019 a1-acid glycoprotein (orosomucoid) human plasma. Acute phase protein. Molecular weight 38-40 kDa. Isoelectric point 2.7, E1%280 nm= 8.1. The preparation is homogeneous by electrophoresis in 8.0 % PAAG conducted according to Davis. The protein has diagnostic significance and its concentration is changed during various pathologies (inflammation, trauma, contraceptives, drugs etc. By request monospecific antibodies can be developed.
1.Baumann H Gauldie J The acute phase response Immunol. Rev. 1994, v. 15, N 2 74-81
2.Routledge PA, Clinical relevance of a1-acid glycoprotein in health and disease Prog Clin. Biol.Res 1988 (Publ 1989) 300 (a1-acid glycoprotein) 185-198
A0013 Albumin from bovine plasma. Major plasma protein, Cohn V fractionate. Molecular weight of protein is 67 kDa. E 1%280 nm=5.8. Isoelectric point is 4.7. The preparation is homogeneous by electrophoresis in 7.5% PAAG conducted according to Davis. The preparation can be applied as blocking agent in blotting procedures (Western blotting), in latex agglutination immunoassays in colloidal gold immunoassays etc.
A0014 Albumin from human plasma. The preparation is homogeneous by electrophoresis in 7.5% PAAG conducted according to Davis. Preparation can be applied as standard in kits for determination of HSA
A0041 Albumin from hen egg white. Preparation can be applied as the blocking agent for blotting, latex agglutination etc
A0079 Albumin acetylated. Prepared from albumin by acetylation with acetic anhydride. The procedure and consequent treatment provides acetylation only lysine free amino groups.The preparation can be applied in blotting procedures when neutralization of charges is necessary.
A0015 Albumin fatty acid free from bovine plasma,. Prepared from native albumin
Chen RF Removal of fatty acids from serum albumin by charcoal treatment JBC 1967, v. 242, 173-181
A0078 Albumin glycated from bovine plasma. Prepared from native albumin by in vitro glycation. The preparation contains 1-2 mol fructosamine per mol albumin. . The preparation is useful as standard in diagnostic kits for determination of fructosamine.
A0035 Albumin methylated from bovine plasma. Prepared from native albumin by in vitro methylation. The preparation is useful in procedures where separation of DNA from RNA is necessary.
A0023 Amine oxidase from bovine plasma (copper containing). Molecular weight of protein is 170-200 kDa. The preferential substrates are monoamines however some di and polyamines are oxidized also. Activity of preparation is about 60-100 U/g protein. One unit will oxidize 1mcmol benzylamine to benzaldehyde per minute at pH 7.4 at 25 0 C. The proteins are considered as useful for synthesis of drugs effective for cancer treatment.
1.Colloquium Amine oxidases Biochem Soc Trans 1991, v. 19, N 1, 199-228

2.Kunimoto S et al Cytotoxicity of spergualin and AO activity in medium J. Antibiot 1985, v. 38, N 7, 899-903
A0024 Amine oxidase from bovine liver (flavin-containing). Molecular weight of preparation is about 60 kDa. The protein consists from one subunit and from FAD as cofactor. Molar extinction at 450 nm is 9800 Mol-1cm-1. Spectral ratio A280/A450 is about 10. The protein has typical flavin spectrum with two peaks in visible region at 360 and 450 nm. The protein participates in reutilization of polyamines and its preferential substrates are acetyl spermine and acetyl spermidine. These polyamine oxidases are considered as prospective targets for cancer therapy.PAO-PA system has antifungal and antiparasitic activity.
1.Holtta E Oxidation of spermidine and spermine in liver: purification and properties of PAO Biochemistry 1977, v. 16, N 1, 91-100
2. Levitz SN et al Inhibition and killing of fungi by PAO-PA system. Antifungal activity of the PAO-PA system Antonie van Leeuwanhoek 1990, v. 58, N 2, 107-114

3.Hessels J et al Inhibition of PAO in rats improves the sensitivity of urinary PAO as marker for cell death Biochem J. 1990, v. 266, N 3, 843-851
A0095 Annexin –V from human placenta (placental anticoagulant protein). Molecular weight of protein is 30-35 kDa. The preparation is homogeneous by electrophoresis in 10% PAAG conducted according to Davis. Annexins are group of Ca-dependent phospholipid binding proteins. Assay of preparation is conducted by inhibition of plasma coagulation by thromboplastin and Ca+2. Annexin V conjugated with appropriate labels (fluorescein isothiocyanate, colloidal gold etc) is applied widely for apoptosis (programmed cell death) detection.
Geison MJ Annexins-new family of ca-regulated phospholipids binding protein Biosci Rep 1987, v. 7, N 4, 289-298
A0096 Annexin-gold conjugate. Annexin –gold conjugate (15 nm) may be used for apoptosis detection, process where translocation of phosphotidylserine from inner part of membrane to outer takes place. This translocation may be detected by binding with annexin-V gold conjugate. The preparation is supplied as solution of red color with adsorption at 520 nm about 2-3.
1. Dachary PJ et al Annexin V as a probe of aminophospholipid exposure and platelet membrane vesiculation: A flow cytometry study showing a role free sulphydryl groups Blood 1993, v. 81, 2555-2565

2.Koopman G et al Annexin V for flow cytometric detection of phosphatidylserine expression on B-cells undergoing apoptosis Blood 1994, v. 84, 1415-1420
A0099 Avidin from egg white. It is a protein that binds biotin with high affinity. This property permits its application in various types of EIA for binding with biotinylated antibodies. Preparation is chromatografically pure.
Methods in Enzymology (Avidin Biotin Technology) 1990,v.184
A0100 Avidin-gold conjugate. The preparation can be used in immunochromatographic formats for detection of various antigens.
A0101 Avidin-peroxidase conjugate. Preparation can be applied in EIA for binding to biotinylated antibodies.
C0020 Calmodulin (phosphodiesterase 3’5’-cyclic nucleotide activator) Ca-binding protein. Molecular weight of protein is about 17 kDa. Activity of preparation is about 40000u/mg protein. The preparation is homogeneous by electrophoresis in 10 % PAAG conducted according to Davis. The protein has diverse functions that have to be elucidated
1.Takuwa N, Zhou W, Takuwa Y Ca, calmodulin and cell cycle progression Cell Signalling 1995, v. 7, N 2, 93-104
2.Horvath L et al Calmodulin is a potent target for new hypothalamic neuropeptides FEBS Lett 1990, v. 276, N 1,2, 197-201
C0011 Carbonic anhydrase from bovine erythrocytes. The enzyme catalyzes the following reaction Carbonic anhydrase CO2+ H2O ? H2CO3 Molecular weight of protein is about 30 kDa. Isoelectric point of protein 5.65. Molar extinction at 280 nm is 5700 Mol-1cm-1. Activity is about 2500 W-A U/mg protein. Assay: Reaction mixture contains 2 ml 0.025 M veronal pH 8.2, bromthymol blue 1mg/ 100 ml. Enzyme solution 1 ml is added to 2 ml of CO2 saturated buffer solution and time is registered until color of indicator is changed from blue to yellow. Activity is calculated from the following equation U = 10 (Tb/Tc-1)/mg of protein Where Tb- time of noncatalyzed reaction Tc- time of enzyme catalyzed reaction.

1.Brian C. et al Carbonic Anhydrase: New Insights for an Ancient Enzyme J. Biol. Chem. 2001 276: 48615-48618

2.Giacobini E Carbonic anhydrase: the first marker of glial development Curr Top Dev Biol 1987, v. 21, (Neurol Dev Pt 4) 207-215
C005 Catalase from bovine liver. Fe- containing hemoprotein. Molecular weight of enzyme 225-250 kDa. E1%405=13.5. Activity of preparation is about 50000 U/mg of protein. One unit will decompose 1 ?mol H202 per minute at pH 7.0 at 250 C while concentration of hydrogen peroxide falls from 10.3 to 9.2 mM. The rate of disappearance of hydrogen peroxide is followed by observing the rate of decrease in absorbance at 240 nm (Sigma assay procedure).The enzyme can be applied in systems where effective removal of hydrogen peroxide is necessary. Moreover recent data show its role in processes of apoptosis.
1.Brown MR et al Overexpression of human catalase inhibits proliferation and promotes apoptosis in vascular smooth muscle cells Circ Res 1999, v. 85, 524-533

2.Tome ME et al Catalase-overexpressing Thymocytes Are Resistant to Glucocorticoid-induced Apoptosis and Exhibit Increased Net Tumor Growth Cancer Res 2001 61: 2766-2773
C0021 Ceruloplasmin- copper containing, antioxidant, blue protein from bovine plasma. Molecular weight of protein is 150-160 kDa. Spectral ratio A280/A610 =25-28. Ceruloplasmin is oxidase and it oxidizes some polyphenols. Activity of preparation is 20-50 U/mg of protein.
Shosinsky K et al Measurement of ceruloplasmin from its oxidase activity. Clin Chem 1974, v.20, 1556
C0022 Ceruloplasmin- copper containing, antioxidant, blue protein from human plasma. Spectral ratio A280/A610 =25-28. The protein has diagnostic significance and its concentration is changed during some pathologies (Wilson disease, Menkes syndrome)
1.Holtzman NA et al Ceruloplasmin in Wilson disease J.Clin Invest 1967, v. 46, N 6, 993-1002
2.Gutteridge JMC, Stocks J Ceruloplasmin : Physiological and pathological perspectives CRC Clin Lab Sci 1981, v. 14, 257-329
C0082 Chorionic gonadotropin from urine of pregnancy women. Molecular weight of the protein is 50-60 kDa when it is determined by various methods. E1%280nm= 3.88. The preparation has follicle stimulating and luteinizing activity. Activity of preparation is about 15000 U/mg of protein. Activity was estimated by biotest by its effects on ovaries. The protein has diagnostic significance. In normal plasma it absent, but it appear during various tumors and in pregnancy. Recent data demonstrate that the protein has apoptosis inducing activity.
1.Srivastava P, Russu J, Russo IU CG inhibits rat mammary carcinogenesis through activation of PCD Carcinogenesis 1997, v. 18, n 9, 1799-1808
2.Bidart JM, Bellet Dl HCG. Molecular forms and clinical application Trends Endocrinol Met 1993, v. 4, N 9, 285-291
C0048 C-Reactive protein from human pleural fluid. Acute phase protein. Molecular weight of protein is 120 kDa. E1%280 nm= 20. The preparation is homogeneous by electrophoresis in 6% PAAG conducted according to Davis. Immunization by the protein produces antibodies that do not cross-react with any other plasma protein as assayed by double immunodiffusion according to Ouchterlony. The protein has diagnostic significance. The elevated concentrations of the protein are risk for development of coronary diseases.
1.Westhuyren J, Healy H Review: biology and relevance of CRP in cardiovascular and renal disease Ann Clin Lab Sci 2000, v. 30, N 2, 145-159
2.Griselli M, Herbert J, Hutchinson WL, taylor KM, Sohail M, Krautz T, Pepys MB CRP and complement are important mediators of tissue damage in acute myocardial infarction J.Expl Med 1999, v. 190, N 12, 1733-1741
C0016 Cytochrome C from bovine heart. The protein is purified by chromatography without TCA. The preparation is homogeneous by electrophoresis in 12% PAAG conducted in non denaturated conditions. The protein are applied in reactions for determination of superoxide dismutase activity in xantine-xantine oxidase system. Its role in apoptosis induction supposes that it can be applied as therapeutic agent for cancer treatment.
Zhivotovsky B, Orrenius S, Brustugun OT, Doskeland SO Injected cytochrome c induces apoptosis Nature 1998, v. 391, 449-450
C0017 Cytochrome c from human heart. The protein is purified by chromatography without TCA.The preparation is homogeneous by electrophoresis in 12% PAAG conducted in non denaturated conditions. The protein can be applied for development of antibodies. Moreover it can be applied for affinity purification of appropriate antibodies.
F0001 Ferritin from bovine spleen (holo form). Iron containing protein. Mol weight of the protein is about 430-480 kDa. The preparation contains about 3000 g.atom iron/mol of protein. E1%280 nm =9 for apoferritin. The protein can be applied in electron microscopy as electron dense marker in conjugation with various ligands. Ferritin in spefic form can be applied as targeting of cancer cells
M. Uchida et al Targeting of Cancer Cells with Ferrimagnetic Ferritin Cage Nanoparticles JACS 2006, v128, N 51, pp 16626 - 16633
F0002 Ferritin from bovine spleen (apo-form). It is prepared from F0001
F0003 Ferritin from human spleen (holo form). Iron containing protein.The protein has diagnostic significance and its concentration reflects various pathologic conditions (anemia, hemochromatosis, some types of tumors). Preparation can be applied for antibody preparaion.
1.Scholefield JH et al Serum ferritin: screening test for colorectal cancer Dis Colon Rectum 1998, v. 41, N 8, 1029-1031
2. Sun-Ah You Ferritin in atherosclerosis Clin Chim Acta 2005, v. 357, N1-2, 1-16
3.Joshi JG et al Ferritin –a general metal detoxicant Biol Trace Elem Res 1988, Publ 1989, v. 21, 105-110
F0004 Ferritin from human spleen. (apo form). It is prepared from F003
F0073 Fibrinogen from bovine plasma. About 65-75% of the protein is clottable.
F0123 Fibrinogen from porcine plasma. About 65-75% of the protein is clottable.
F0025 a1-Fetoprotein from human fetal plasma. Fetal albumin. Molecular weight of the protein is 74 kDa . E1%280 nm =5.3 .The preparation is homogeneous by electrophoresis in 8% PAAG conducted according to Davis. The protein has diagnostic significance. It is absents practically in normal plasma, but appear during some tumors. Recent data demonstrate that the protein has apoptosis inducing activity.
1.Um SH et alAFP impairs APC function and induces their apoptosis J.Immunol 2004, v. 173, N 3, 1772-1778
2.Semenkova LN et al AFP induced apoptosis in human hepatoma cells Tumor Biology 1998, v. 19, 261-274
3. Uriel J The physiological role of AFP in cell growth and differentiation J.natl Med Allied Sci 1989, v. 33, 12-17
H0008 Hemoglobin from bovine erythrocytes (ferrous) The preparation is homogeneous by electrophoresis in 8% PAAG conducted according to Davis. E1%530 nm =9. The preparation is supplied in solution to prevent its conversion to methemoglobin
H0009 Hemoglobin from human erythrocytes (ferrous) The preparation is homogeneous by electrophoresis in 8% PAAG conducted according to Davis. The preparation after its conversion to cyanmethemoglobin can be applied as standard in diagnostic kits for determination of Hb
H0010 Hemoglobin F from human erythrocytes. It is alkaline resistant fraction of total hemoglobin The preparation is homogeneous by electrophoresis in 8% PAAG conducted according to Davis.
H0012 Hemopexin from bovine plasma. The protein has high affinity to heme. E1%280 nm = 19.2 for heme-hemopexin and for apoprotein E1%280 nm = 19.7. Physiological role of protein is removal of heme, and porphirins from circulation. Purity more than 90%. Recently its protective role in lung oxidative stress.
Barnard ML, Muller-Eberhardt U Turrens JF Protective role of hemopexin on heme dependent lung oxidative stress BBRC 1993, v. 192, N 1, 82-88
L0039 Lactate dehydrogenase from bovine liver. Activity of preparation is about 500 U/mg of protein. One unit will reduce 1 ?mol of pyruvate to l-lactate per minute at pH 7.5 at 37 0 C. The protein is applied widely in diagnostic test kits for determination of alanine and aspartate amine transferases.

Lectins

lectins are group of carbohydrate binding proteins with diverse functions.They have spcificity to various carbohydrates and these proteins participate in various biological processes (induction of proliferation, apoptosis, defense functions etc). They can be applied for study of carbohydrate composition in plasma membranes, for diagnosis, for purification of glycoproteins etc
1. S. Saevarsdottir et al Mannan binding lectin as an adjunct to risk assessment for myocardial infarction in individuals with enhanced risk J. Exp. Med. 2005 201: 117-125
2. Miyagi T et al Concanavalin A injection activates intrahepatic innate immune cells to provoke an antitumor effect in murine liver Hepatology 2004, v. 40, N 5, 1190-1196
3. Gastman B et al A novel apoptotic pathway as defined by lectin cellular initiative BBRC 2004, v. 316, N 1, 263-271
4.Nangia-Makker P et al Carbohydrate binding proteins in cancer and their ligands as therapeutic agents Trends Mol Med 2002, v. 8, 187-192
5. Gabius HJ, The sugar code: functional lectinomics BBA 2002, v. 1572, 165-177
6.Singh RS et al Lectins: sources, activities and applications Crit Rev Biotechnol 1999, v. 19, N 2, 145-178
L0086 Lectin from soy bean (glycine max). The preparation is homogeneous by electrophoresis in 8% PAAG. It is not blood group specific and it has specificity for N-acetyl galactosamine. Preparation after immobilization on various carriers can be applied for purification of appropriate glycoproteins
L0087 Lectin from soy bean (glycine max) conjugated with colloidal gold. The preparation can be used in SEM for study of membrane dynamics.
0088 Lectin from soy bean . (glycine max), peroxidase labeled. The preparation can be used for study of membrane dynamics by EIA like analysis.
L0089 Lectin from lentils (lens culinaris) The preparation is homogeneous by electrophoresis in 8% PAAG. It is not blood group specific and it has specificity for terminal d-mannosyl and d-glycosyl residues. Preparation after immobilization on various carriers can be applied for purification of appropriate glycoproteins
L0090 Lectin from lentils (lens culinaris) conjugated with colloidal gold. The preparation can be used in SEM for study of membrane dynamics
L0091 Lectin from lentils (lens culinaris) conjugated with peroxidase. The preparation can be used for study of membrane dynamics by EIA like analysis
L0097 Lectin from wheat germ (triticum vulgaris). Preparation is homogeneous by electrophoresis in 10 % PAAG conducted at pH 4.5. The protein has activity to N-acetyl glucosamine. Preparation after immobilization on various carriers can be applied for purification of appropriate glycoproteins.Some tumors have N-acetyl glucosamine residues on surface of their plasma membranes. This lectin immobilized on magnetic nanobeads can be applied for separation of tumor cells.
L0098 Lectin from wheat germ(triticum vulgaris) conjugated with colloidal gold. The preparation can be used in SEM for study of membrane dynamics
L0104 Lectin from wheat germ(triticum vulgaris) conjugated with peroxidase. The preparation can be used for study of membrane dynamics by EIA analysis
L0074 Lysozyme from egg white, crystallized, dialyzed, lyophilized. The protein is useful for preparation of protoplasts.
L0115 Lysozyme from human milk. The preparation is homogeneous by electrophoresis in 10% PAAG. The preparation is suitable for preparation of monospecific antibodies.
M0057 Myoglobin from human heart (muscle hemoglobin). The preparation is homogeneous by electrophoresis in 10% PAAG conducted according to Davis. Protein has diagnostic significance. Its concentration in plasma is increased during infarction, (early marker), uremia, trauma etc. When injected to experimental animals the monospecific antibodies are developed that do not cross-react with any other plasma proteins.Preparation can be applied for development of antibodies.
P0085 Prostate specific antigen from human seminal plasma. The preparation is homogeneous by electrophoresis in 10% PAAG conducted according to Davis. The protein was assayed by its proteolytic activity. Substrate – myoglobin of 1mg/ml was dissolved in 0.05 M tris HCl buffer of pH 7.8 Then enzyme solution was added (substrate/enzyme ratio is about 20/1). After incubation and precipitation by TCA soluble fragments were analyzed by spectrophotometry at 280 nm. The protein has diagnostic significance and its determination is applied widely for detection of prostate cancer.
1. Nadji M et alPSA an immunohistologic marker for prostatic neoplasms Cancer 1981, v. 48, 1229.

2.Stamey TA et al PSA as a serum marker for adenocarcinoma of the prostate N.Engl J. Med 1987, v. 317, 909-916
T0045 Thromboplastin from rabbit brain or lung. Highly active lyophilized powder. Reconstitution by calcium chloride gives normal range for plasma coagulation 13-16 sec
1.Nature 1954, v. 174, N 4436 880-881

2.Blood 1964, v. 23, 657
Thromboplastin from bovine lung. Highly active lyophilized powder. Reconstitution by calcium chloride gives normal range for plasma coagulation 14-17 sec
T0006 Transferrin holo form from human plasma. Iron- transport protein. E1%280 nm = 11.4. The preparation is homogeneous by electrophoresis in 7% PAAG conducted according to Davis. Spectral ratio A460/A410 is about 1.3 and more. Transferrin is an acute phase protein and therefore it has diagnostic significance.
DeJong G et al The biology of transferrin Clin Chim Acta 1990, 1-2, 1-46
T0007 Transferrin apo form from human plasma. Iron- transport protein. Prepared from T0006. The preparation can be appled as carrier for other metals.
Aisen P et al The Cr, Mn and Co complexes of transferrin JBC 1969, v. 244, 4628
T0102 Troponin from human heart. Troponin is a complex of proteins (C,T,I) those can be separated by electrophoresis in presence of 8 M urea. Preparation can be applied for consequent separation of these troponins
T0093 Troponin C from human heart. The preparation is homogeneous by electrophoresis in 10 % PAAG
T0094 Troponin C from bovine muscle attached to to Sepharose CL 4B. Protein immobilized 1-3 mg/ ml of gel. This matrix is suitable for affinity purification of human troponin I
T0103 Troponin B from human heart.The protein consists of troponin I and troponin T
U0030 Urease from soy bean. Partially purified powder. Activity 10-20 U/mg. The preparation is suitable in diagnostic kits for determination of urea.
U0063 Uricase from porcine liver. The enzyme catalyzes oxidation of uric acid to allantoin. Activity of preparation is about 40-100 U/g of protein. One unit will convert 1 micromol uric acid to allantoin per minute, pH 8.5 at 25 0 C. The preparation is useful in diagnostic kits for determination of uric acid

ANTIBODIES
- Monospecific polyclonal antibodies were developed in experimental animals (rabbits) by injection of pure antigen. Sera of immunized animals were fractionated for preparation of IgG fraction. Antibodies were tested by double immunodiffusion assay according to Ouchterlony. They do not cross-react with any other plasma proteins.Antibodies are supplied as solution containing 0.01 M phosphate buffer pH 7.1, 0.15 M NaCl and 0.1% NaN3 as preservative. The antibodies preserve their antigen binding properties at least 2-3 years. We can produce monospecific antibodies to all our proteins by your request. Moreover we can produce antibodies to your antigens.
- A0112 Antibodies to human annexin V. They can be used for immobilization to various chromatografic media for consequent affinity purification of annexin V. The preparation can be applied also for immobilization to polymeric microparticles for immune detection of annexin V, for immobilization to quantum dots for study physiological role of the annexin V.
  A0113 Antibodies to human annexin V conjugated with peroxidase. The preparation may be aplied in EIA analysis as a second antibody for quantitative determination of annexin V
  A0114 Antibodies to human annexin V conjugated with colloidal gold. The preparation may be applied in electron microscopy for determination of localization of annexin V
  A0083 Antibodies to human chorionic gonadotropin (whole molecule). They can be used for immobilization to various chromatografic media for consequent affinity purification of CG and LH. In conjugation with various labels the antibodies can be applied in various types of immunoassay for detection of CG.
  A0084 Antibodies to human chorionic gonadotropin-conjugated with peroxidase The preparation may be applied in EIA analysis as a second antibody for quantitative determination of HCG.
  A0049 Antibodies to human C-Reactive protein. They can be applied in immunoassays for determination of CRP (radial immunodiffusion, immunoprecipitation, immunoelectrophoresis). In conjugation with polystyrene latex beads the antibodies can be applied for determination of CRP by agglutination assay
  A0068 Antibodies to human C-Reactive protein-conjugated with colloidal gold. The preparation can be applied in immunochromatographic strips for rapid detection of CRP.
  A0053 Antibodies to human C-Reactive protein-conjugated with peroxidase Conjugation was conducted by using or Na periodate or glutaric dialdehyde as cross-linking agents. The preparation may be applied in EIA analysis as a second antibody for quantitative determination of CRP.
  A0110 Antibodies to human ferritin. The preparation can be applied for affinity purification of human ferritin.
  A0111 Antibodies to human ferritin conjugated with peroxidase. The preparation can be useful as the second antibody in EIA for quantitative determination of ferritin in human sera
  A0080 Antibodies to human Immunoglobulin G (whole molecule) IgG fraction (rabbit). 2.5 mg/ml. The preparation can be applied for quantitative determination of IgG by reaction of radial immunodiffusion.
  A0081 Antibodies to human Immunoglobulin G (whole molecule) IgG fraction (rabbit). conjugated with peroxidase Conjugation was conducted by using or Na periodate or glutaric dialdehyde as cross-linking agents. The preparation can be useful as the second antibody in various EIA for quantitative determination of IgG in human sera during various autoimmune conditions. (A)
  A0119 Antibodies to human lysozyme. Concentration of lysozyme is increased during some diseases, in particlular during multiple myeloma, and these antibodies can be applied for diagnosis of this disease.
  A0120 Antibodies to human lysozyme conjugated with peroxidase.Conjugation was conducted by using or Na periodate or glutaric dialdehyde as cross-linking agents. The preparation can be useful as the second antibody in various EIA for quantitative determination of lysozyme in human sera.
  A0058 Antibodies to human myoglobin. The preparation can be applied for preparation of affinity columns for purification of the myoglobin
  A0069 Antibodies to human myoglobin conjugated with colloidal gold. The preparation can be applied for detection of myoglobin in various tissues. Moreover it can be applied for determination of myoglobin in immunochromatographic formats.
  A0060 Antibodies to human myoglobin-conjugated with peroxidase Conjugation was conducted by using or Na periodate or glutaric dialdehyde as cross-linking agents. The preparation may be applied in EIA analysis as a second antibody for quantitative determination of myoglobin.
  A0107 Antibodies to human prostate specific antigen
  A0109 Antibodies to human prostate specific antigen conjugated with peroxidase The preparation may be applied in EIA analysis as a second antibody for quantitative determination of PSA.
  
  DIAGNOSTIC KITS
  
  DK0028 ALANINE AMINOTRANSFERASE
  
  Method: ultraviolet, kinetic
  Principle:
  
  l-alanine +a-ketoglutarate +ALT = pyruvate +l- glutamate
  pyruvate + NADH+ LDH = l-lactate +NAD
  The rate of decrease in absorbance at 340 nm due to formation of NAD is directly proportional to ALT activity.
  Diagnostic significance: Increased levels of enzyme is associated with liver diseases.
  1. Bergmeyer HU, Scheide P, Wilhelm A, Wahlfeld Optimization of methods for AST and ALT Clin Chem 1978, v. 24, N 1, 58-73
  
  2. Hafkenscheid JCM, Diggt CCM Determination of serum aminotransferases: activation by pyridoxal-5 phosphate in relation to substrate concentration Clin Chem 1979, v. 25, N 3, 353-362
  
  DK0075 ALANINE AMINOTRANSFERASE
  
  Method: colorimetric, endpoint
  Principle:
  l-alanine +a-ketoglutarate +ALT = pyruvate +l- glutamate
  The pyruvate then reacts with 2,4 dinitrophenylhydrazine producing highly colored complex with absorbance at 490-520 nm . Intensity of absorbance is proportional to ALT activity.
  Diagnostic significance: Increased levels of enzyme is associated with liver diseases.
  DK0034 ALBUMIN
  
  Method: colorimetric, endpoint
  Principle:
  Bromcresol purple binds with HSA forming colored complex with absorbance at 600 nm. Intensity of absorbance is proportional to albumin concentration in serum.
  Diagnostic significance: Low levels associated with liver diseases, nephrotic syndrome.
  Henry JB Clinical Chemistry 1967
  
  DK0052 ALCOHOL
  
  Method: ultraviolet, endpoint
  Principle:
  Ethanol+NAD+ADH= acetaldehyde+ NADH
  Formation of NADH during this reaction brings to increase of absorbtion at 340nm, and it is proportional to ethanol concentration
  Diagnostic significance: Established circulating levels of ethanol in cases of suspected intoxication
  DK0036 AMYLASE
  
  Method: colorimetric, end point
  Principle:
  Soluble starch is incubated with sample and then reducing substances determine in protein free filtrate. The difference in reducing substances, expressed as glucose before and after incubation is taken as the units of amylase activity
  Diagnostic significance: Increased levels associated with acute pancreatitis, pancreatic duct obstruction, bacterial parotitis
  DK0070 ANTIBODIES TO ds DNA
  
  Method: latex agglutination
  Principle:
  Polystyrene latex beads coated with ds DNA in the presence of antibodies to it in human serum form visible agglutination. The rate of agglutination correlates with antibodies concentration in serum.
  Diagnostic significance: Antibodies to dsDNA are characteristics of the autoimmune diseases, SLE
  DK0071 ANTIBODIES TO DNP
  
  Method: latex agglutination
  Principle:
  Polystyrene latex beads coated with DNP in the presence of antibodies to it in human serum form visible agglutination. The rate of agglutination correlates with antibodies concentration in serum.
  Diagnostic significance: Antibodies to DNP are characteristics of the autoimmune diseases
  1. Hall AP et al Latex agglutination and inhibition reactions: clinical experience in diagnosis of rheumatoid arthritis New Engl J. Med 1958, v. 258, 731
  
  2. Dubois EL et al A latex nucleoprotein test for diagnosis of SLE: comparative evaluation JAMA 1961, v. 177, 141-143
  
  DK0072 ANTIBODIES TO RNP
  
  Method: latex agglutination
  Principle:
  Polystyrene latex beads coated with RNP in the presence of antibodies to it in human serum form visible agglutination. The rate of agglutination correlates with antibodies concentration in serum.
  Diagnostic significance: Antibodies to RNP are characteristics of the autoimmune diseases
  DK0029 ASPARTATE AMINOTRANSFERASE
  
  Method: utraviolet, kinetic
  Principle:
  Aspartate +a-ketoglutarate +AST = pyruvate +l- glutamate
  Pyruvate + NADH +MDH l-malate +NAD
  The rate of decrease in absorbance at 340 nm due to formation of NAD is directly proportional to AST activity.
  Diagnostic significance: Increased levels associated with myocardial infarction, liver diseases muscular dystrophy
  1. Bergmeyer HU, Scheide P, Wilhelm A, Wahlfeld Optimization of methods for AST and ALT Clin Chem 1978, v. 24, N 1, 58-73
  
  2. Hafkenscheid JCM, Diggt CCM Determination of serum aminotransferases: activation by pyridoxal-5 phosphate in relation to substrate concentration Clin Chem 1979, v. 25, N 3, 353-362
  
  DK0076 ASPARTATE AMINOTRANSFERASE
  
  Method: colorimetric, endpoint
  Principle
  aspartate +a-ketoglutarate +AST = pyruvate +l- glutamate
  The oxalacetate then reacts with 2,4 dinitrophenylhydrazine producing highly colored complex with absorbance at 490-520 nm Intensity of absorbance is proportional to AST activity.
  Diagnostic significance: Increased levels associated with myocardial infarction, liver diseases muscular dystrophy
  DK0077 BACTERINURIA
  
  Screening test
  Principle:
  paper strips are coated by reagents that become purple by action of nitrite . Many types of bacteria are producing nitrite and thus they can be detected by these strips
  Diagnostic significance: Cystitis, pyelonephritis
  DK0038 BILIRUBIN (direct/total)
  
  Method: colorimetric, endpoint (Walters Gerarde)
  Principle:
  In the presence of dimethylsulfoxide both conjugated and nonconjugated bilirubin react with diazotized sulfanilic acid to yield azobilirubin with absorbance at 560 nm. Conjugated (direct) bilirubin reacts directly with diazotized sulfanilic acid to yield azobilirubin with absorbance at 560nm
  Diagnostic significance: Increased levels associated with biliary obstruction and hepatocellular diseases
  Walters M et al An ultramicromethod for the determination of conjugated and total bilirubin in serum and plasma Microchem J. 1970, v.15, 231-243
  
  DK0044 CERULOPLASMIN
  
  Method: colorimetric, endpoint
  Principle:
  Serum ceruloplasmin oxidizes some substrates producing highly colored compounds in acid media. The intensity of color is proportional to ceruloplasmin activity.
  Diagnostic significance: Decreased levels associated with Wilson disease and Menkes syndrome.
  Shrifrine M, Fisher G Ceruloplasmin levels in sera from human patients with osteosarcoma Cancer 1976, v. 39, 244-248
  
  DK0051 C-REACTIVE PROTEIN
  
  Method: latex agglutination
  Principle:
  Polystyrene latex beads coated with antibodies to human C-Reactive protein in the presence of CRP in human serum form visible agglutination. The rate of agglutination correlates with CRP concentration in serum.
  Diagnostic significance: Increased concentration of CRP have been found during virtually all diseases associated with active inflammatory or tissue destruction
  1. Wadsworth C et al Efficacy of latex agglutination and quantitation methods for determination of CRP in pediatric sera Clin Chim Acta 1984, v. 138, N 2, 309-319
  
  2. Volanakis JE et al Human CRP and host defences UCLA Symp Mol Cell Biol New Ser 1990, v121 161-175
  
  3.Griselli M et al CRP and complement are important mediators of tissue damage in acute myocardial infarction J.Expl Med 1999, v. 190, N 12, 1733-1741
  
  DK0033 CREATININE
  
  Method: colorimetric endpoint (Jaffe, Slot modification)
  Principle:
  Creatinine reacts with picric acid under alkaline conditions forming yellow-orange complex derived from creatinine as well as some nonspecific substances. Upon addition of acid the color contributed by creatinine is destroyed while that produced by non- specific substances remains. The difference in color intensity before and after acidification is proportional to the creatinine concentration
  Diagnostic significance: Increased levels associated with impaired renal function.
  Grafnetter D et al Note on Slot method for the specific determination of creatinine Clin Chim Acta 1967, v.17, 493-498
  
  DK0042 FRUCTOSAMINE
  
  Method: colorimetric, endpoint
  
  Principle: fructosamine (glycated serum protein) reduces nitroblue tetrazolium under appropriate conditions forming a purple colored formazan. Intensity of absorbance is proportional to fructosamine concentration.
  Diagnostic significance: Fructosamine is the index of the average glycemic state during previous 2-3 weeks. The test is useful short term diabetic control
  1. Baker J et al Clinical usefulness of estimation of serum fructosamine concentration as a screening test for diabetes melititus Br.Med J. 1983, v. 287, N 6396 863-867
  
  2. Johnson RN et alFructosamine: a new approach to the estimation of serum glycoprotein. An index of diabetic control Clin Chim Acta 1983, v. 127, 87-95
  
  3. Johnson RH et al The alkaline reducing activity of glycated serum proteins and its relevance to diabetic mellitus Clin Chem 1986, v. 32, 368-370
  
  DK0043 FRUCTOSE
  
  Method: colorimetric, endpoint
  
  Principle: Heating of samples under appropriate conditions with specific reagents brings to selective coloring of fructose. Intensity of the color is proportional to fructose concentration
  Diagnostic significance: Decreased levels of fructose in sperm may be the cause of infertility.
  Davis J, Gander J A reevaluation of the Roe procedure for the determination of fructose Anal Biochem 1967, v. 19, 72
  
  DK0027 GLUCOSE
  
  Method: Colorimetric , endpoint
  Principle:
  Glucose +H20+02+GO=gluconic acid + H202
  PO+ 2H202+ 4- amino antipyrine+phenol+peroxidase= dyed complex
  Intensity of absorbance is proportional to glucose concentration.
  Diagnostic significance: Increased levels associated with diabetes mellitus, hyperactivity of thyroid, feochromocytoma, pancreas diseases.
  Henry JB (ed) Clinical diagnosis and management by laboratory methods 18 th Ed WB Saunders Co 1991
  
  DK0046 HEMOGLOBIN
  
  Method: colorimetric, endpoint
  
  Principle: hemoglobin reacts with acetoncyanhydrine in appropriate medium. All forms of hemoglobin in blood are converted to cyanmethemoglobin. The absorbance at 530-550 nm is proportional to the hemoglobin concentration in blood.
  Diagnostic significance: Decreased levels associated with anemia and increased levels with polycitemia and dehydration
  Rice E Rapid determination of total Hb as hemoglobin cyanide in blood containing carboxy hemoglobin Clin Chim Acta 1967, v. 18, N 1, 89-91
  
  DK0040 LACTATE DEHYDROGENASE
  
  Method: ultraviolet, kinetic
  Principle: Pyruvate + NADH+LDH=Lactate+NAD
  The rate of decrease in absorbance at 340 nm due to formation of NAD is directly proportional to LDH activity.
  Diagnostic significance: Increased levels of enzyme takes place after 8-12 hours after myocardial infarction. Moderate increases also observed in cases of liver diseases.
  Vassault A. Lactate dehydrogenase. UV method with pyruvate and NADH in Bergmeyer HU Ed Methods of Enzymatic Analysis 1983, v3
  DK0059 MYOGLOBIN
  
  Method: latex agglutination
  Principle:
  Polystyrene latex beads coated with antibodies to human myoglobin in the presence of myoglobin in human serum form visible agglutination. The rate of agglutination correlates with myoglobin concentration in serum.
  Diagnostic significance: Increased levels associated with heart diseases. Myoglobin is the first marker of infarction
  1.Mair J Myoglobin Dev Cardiovasc Med 1998, v. 205 (myocardial Damage) 53-59
  
  2.Ohman EM et al Early detection of acute myocardial infarction . Additional diagnostic information from serum concentration of myoglobin in patients without ST elevation Br.Heart J 1990, v. 63, N 6, 335-338
  
  3. Chapell JP et al Semi-quantitative estimation of serum myoglobin by a rapid latex agglutination method: an emergency screening test for acute myocardial infarction Clin Chim Acta 1985, v. 145, 143-150
  
  DK0026 PROTEIN
  
  Method: colorimetric, endpoint
  Principle:
  The copper ions in alkaline biuret reagent react with peptide bonds of serum proteins to form a purple color. The intensity of the color is proportional to the total protein concentration
  Diagnostic significance: Increased levels observed in cases of dehydration.
  Tietz N (ed) Fundamentals of Clinical Chemistry 3rd ed Philadelphia 1987
  
  DK0065 PROTEIN MICRO
  
  Method: colorimetric endpoint.
  Principle:
  brilliant blue G reacts with protein in acid alcohol medium to form a blue colored complex. The intensity of color is proportional to protein concentration.
  Diagnostic significance: Increased level of protein in urine is observed during impaired kidney function
  Macart M, Gerbaut L Evaluation of an improved Coomassie dye binding method for urinary protein assay Clin Chim Acta 1984, v. 141, N 1, 77-85
  
  DK0108 PROTHROMBIN TIME
  
  Method: clotting assay
  Principle:
  thromboplastin in presence of Ca enhances clotting citrated plasma.
  Diagnostic significance: monitoring of patients on oral anticoagulant therapy
  Miale JB Laboratory medicine: Hematology 1982
  
  DK0055 RHEUMATOID FACTOR
  
  Method: Latex Agglutination
  Principle:
  Polystyrene latex beads coated with denaturated human IgG in the presence of rhematoid factors in human serum form visible agglutination. The rate of agglutination correlates with rheumatoid factor concentration in serum.
  Diagnostic significance: Rheumatoid factor has been associated with some bacterial and viral infections, some chronic infections. Its determination is applied for differentiating rheumatoid arthritis from other inflammatory diseases]
  1.Singer JM et al Latex fixation test I. Application to the serologic diagnosis of rheumatoid arthritis Am. J. Med 1956, v. 21, 888
  2. Rheins ML et al Effect of animal sera and serum albumin on latex fixation test for rheumatoid arthritis Proc Soc Expl Biol Med 1957, v. 96, 67,
  
  DK0031 UREA
  
  Method : colorimetric, endpoint
  Principle:
  Urea + H20+urease= NH3+ C02 nitroprusside
  NH3 + salicilate-hypochlorite = colored complex
  Diagnostic significance: Increased levels associated with renal diseases as well as dehydration, diabetic coma.
  Tobacco A, Meiattini F, Moda E, tarli P Simplified enzymic/colorimetric serum urea nitrogen determination Clin Chem 1979, v. 25, N 2, 336-337
  
  DK0062 URIC ACID
  
  Method: ultraviolet, endpoint
  Principle
  Uric acid + H2O +O2 +uricase= allantoin + CO2 +H2O2
  Absorbance at 293 nm is measured before and after reaction. Differences in absorbances show concentration of uric acid.
  Diagnostic significance: Increased levels associated with gout, leukemia, severe renal impairment.
  DK0047 URIC ACID
  
  Method: colorimetric, endpoint
  Principle:
  Uric acid + H2O +O2 +uricase = allantoin + CO2 +
  H2O2 + peroxidase + phenol +4-aminoantipyrine= dyed complex
  Diagnostic significance: Increased levels associated with gout, leukemia, severe renal impairment.
  1.Domagk GF, Schlicke HH A colorimetric method using uricase and peroxidase for the determination of uric acid Anal Biochem 1968, v. 22, 219-224
  
  2. Sanders GTB, Pasma AJ,Hock FJ Determination of uric acid with uricase and peroxidase Clin Chim Acta 1980, v. 100, N 2-3, 299-305
  
  REAGENTS
  
  B0037 Bilirubin standard 20 mg/dl in a bovine albumin base. The preparation can be used in kits for determination of bilirubin.
  C0092 Chitin from crawfish shells, purified powder. The preparation is suitable for analysis chitinase
  C0106 Chitosan from crawfish shells (powder). Preparation is suitable for immobilization of biomolecules. Prepared from C0092
  C0064 Chitosan from crawfish shells (films). Preparation is suitable for immobilization of various biomoleciles and may be applied in biosensors.
  C0066 Colloidal gold nonconjugated It is electron dense marker and has a wide application in electron microscopy, light microscopy, blotting procedures. Recently conjugates of antibodies with colloidal gold were applied for quantitative photometric determination of appropriate antigens. Colloidal gold conjugated with antibodies are applied widely also for qualitative determination of appropriate antigens in strips. Recently new ways for application of colloidal god also were presented. Modified colloidal gold is able to bind DNA and to detect hybridization. Colloidal gold for various purposes is prepared with various sizes. We can supply the following sizes 3-5 nm, 13-15 nm, and 20 nm, 40 nm 50 nm that can be used in various research areas. Concentration: approximately 0.01% A520 =approximately 0.75.
  1. Gheorghean WD et al Passive gold agglutination : an alternative to passive hemagglutination JIM 1980, v. 34, 11-21
  
  2. Leuvering JHW Sol particle immunoassay J.Immunoassay 1980, v. 1, N 1, 77-91
  
  3.Goodman SL et al Colloidal gold markers and probes for routine application in microscopy J.Microscopy 1981, v. 123, N 2, 201-213
  
  4.Brada D et al Golden blot detection of polyclonal and monoclonal antibodies bound to antigen on nitrocellulose by protein A-gold complexes Anal Biochem 1984, v. 142, N 1, 79-83
  
  5. Moeremans M et al Sensitive colloid metal (gold or silver)staining of protein blots on nitrocellulose membranes Anal Biochem 1985, v. 145, 315-321
  
  6.Tomlinson S Detection of biotinilated nucleic acid hybrids by antibody-coated gold colloid Anal Biochem 1988, v. 171, N 1, 217-222
  
  7. Bain CD et al Formation of monolayers by the coadsorption of thiol on gold: variation in the head,group, tail group and solvent JACS 1989, v. 111, 7155
  
  C0116 Colloidal gold, functionalized with amino groups for consequent binding of various ligands
  C0117 Colloidal gold, functionalized with carboxy groups for consequent binding of various ligands
  C0118 Colloidal gold, functionalized with hydroxy groups for consequent binding of various ligands
  C0122 Colloidal silver The preparation can be applied in immunoagglutination assays for detection of various antigens
  C0032 Creatinine standard 20 mg/dl. The preparation can be used in kits for determination of creatinine
  G0121 Glass functionalized. It may be applied as the matrix for covalent immobilization of biomolecules. It is suitable for appropriate sensor preparation.
  G0054 Glycogen from bovine liver or rabbit muscle
  M0125 L-malic acid, Purity more than 95% (enzymatic assay). The preparation can be applied in food industry, medical preparations,cosmetics etc,
  P0056 Pectin from appple or citrus fruits. The preparation can be used as the matrix for affinity purification of some lectins
  P0050 Polystyrene latex beads nonsensitized, for agglutination reactions. Size of particles is about 1 ?m. Concentration of solid particles 1%. This suspension after conjugation with appropriate antibodies may be used in latex slide tests for determination of appropriate antigens. We offer also latex beads with smaller size for application in turbidimetric and nephelometric assays
  S0105 Silica gel blue indicating.
  S0067 Starch soluble (Lintner) The preparation can be used as substrate for amylases
  U0061 Uric acid standard 20 mg/dl. The preparation can be used in kits for determination of uric acid and also in reactions of organic synthesis

DESCRIPTION

PROTEINS AND ENZYMES

Hermansson J et al Separation of chiral compounds with a1-acid glycoprotein as selector Chem Anal NY 1989, v. 98 (HPLC) 337-374

1.Baumann H Gauldie J The acute phase response Immunol. Rev. 1994, v. 15, N 2 74-81

2.Routledge PA, Clinical relevance of a1-acid glycoprotein in health and disease Prog Clin. Biol.Res 1988 (Publ 1989) 300 (a1-acid glycoprotein) 185-198

A0014 Albumin from human plasma. The preparation is homogeneous by electrophoresis in 7.5% PAAG conducted according to Davis. Preparation can be applied as standard in kits for determination of HSA

A0041 Albumin from hen egg white. Preparation can be applied as the blocking agent for blotting, latex agglutination etc

A0079 Albumin acetylated. Prepared from albumin by acetylation with acetic anhydride. The procedure and consequent treatment provides acetylation only lysine free amino groups.The preparation can be applied in blotting procedures when neutralization of charges is necessary.

A0015 Albumin fatty acid free from bovine plasma,. Prepared from native albumin

Chen RF Removal of fatty acids from serum albumin by charcoal treatment JBC 1967, v. 242, 173-181

A0078 Albumin glycated from bovine plasma. Prepared from native albumin by in vitro glycation. The preparation contains 1-2 mol fructosamine per mol albumin. . The preparation is useful as standard in diagnostic kits for determination of fructosamine.

A0035 Albumin methylated from bovine plasma. Prepared from native albumin by in vitro methylation. The preparation is useful in procedures where separation of DNA from RNA is necessary.

1.Colloquium Amine oxidases Biochem Soc Trans 1991, v. 19, N 1, 199-228

2.Kunimoto S et al Cytotoxicity of spergualin and AO activity in medium J. Antibiot 1985, v. 38, N 7, 899-903

1.Holtta E Oxidation of spermidine and spermine in liver: purification and properties of PAO Biochemistry 1977, v. 16, N 1, 91-100

2. Levitz SN et al Inhibition and killing of fungi by PAO-PA system. Antifungal activity of the PAO-PA system Antonie van Leeuwanhoek 1990, v. 58, N 2, 107-114

3.Hessels J et al Inhibition of PAO in rats improves the sensitivity of urinary PAO as marker for cell death Biochem J. 1990, v. 266, N 3, 843-851

Geison MJ Annexins-new family of ca-regulated phospholipids binding protein Biosci Rep 1987, v. 7, N 4, 289-298

1. Dachary PJ et al Annexin V as a probe of aminophospholipid exposure and platelet membrane vesiculation: A flow cytometry study showing a role free sulphydryl groups Blood 1993, v. 81, 2555-2565

2.Koopman G et al Annexin V for flow cytometric detection of phosphatidylserine expression on B-cells undergoing apoptosis Blood 1994, v. 84, 1415-1420

A0099 Avidin from egg white. It is a protein that binds biotin with high affinity. This property permits its application in various types of EIA for binding with biotinylated antibodies. Preparation is chromatografically pure.

Methods in Enzymology (Avidin Biotin Technology) 1990,v.184

A0100 Avidin-gold conjugate. The preparation can be used in immunochromatographic formats for detection of various antigens.

A0101 Avidin-peroxidase conjugate. Preparation can be applied in EIA for binding to biotinylated antibodies.

1.Takuwa N, Zhou W, Takuwa Y Ca, calmodulin and cell cycle progression Cell Signalling 1995, v. 7, N 2, 93-104

2.Horvath L et al Calmodulin is a potent target for new hypothalamic neuropeptides FEBS Lett 1990, v. 276, N 1,2, 197-201

1.Brian C. et al Carbonic Anhydrase: New Insights for an Ancient Enzyme J. Biol. Chem. 2001 276: 48615-48618

2.Giacobini E Carbonic anhydrase: the first marker of glial development Curr Top Dev Biol 1987, v. 21, (Neurol Dev Pt 4) 207-215

1.Brown MR et al Overexpression of human catalase inhibits proliferation and promotes apoptosis in vascular smooth muscle cells Circ Res 1999, v. 85, 524-533

2.Tome ME et al Catalase-overexpressing Thymocytes Are Resistant to Glucocorticoid-induced Apoptosis and Exhibit Increased Net Tumor Growth Cancer Res 2001 61: 2766-2773

C0021 Ceruloplasmin- copper containing, antioxidant, blue protein from bovine plasma. Molecular weight of protein is 150-160 kDa. Spectral ratio A280/A610 =25-28. Ceruloplasmin is oxidase and it oxidizes some polyphenols. Activity of preparation is 20-50 U/mg of protein.

Shosinsky K et al Measurement of ceruloplasmin from its oxidase activity. Clin Chem 1974, v.20, 1556

C0022 Ceruloplasmin- copper containing, antioxidant, blue protein from human plasma. Spectral ratio A280/A610 =25-28. The protein has diagnostic significance and its concentration is changed during some pathologies (Wilson disease, Menkes syndrome)

1.Holtzman NA et al Ceruloplasmin in Wilson disease J.Clin Invest 1967, v. 46, N 6, 993-1002

2.Gutteridge JMC, Stocks J Ceruloplasmin : Physiological and pathological perspectives CRC Clin Lab Sci 1981, v. 14, 257-329

1.Srivastava P, Russu J, Russo IU CG inhibits rat mammary carcinogenesis through activation of PCD Carcinogenesis 1997, v. 18, n 9, 1799-1808

2.Bidart JM, Bellet Dl HCG. Molecular forms and clinical application Trends Endocrinol Met 1993, v. 4, N 9, 285-291

1.Westhuyren J, Healy H Review: biology and relevance of CRP in cardiovascular and renal disease Ann Clin Lab Sci 2000, v. 30, N 2, 145-159

2.Griselli M, Herbert J, Hutchinson WL, taylor KM, Sohail M, Krautz T, Pepys MB CRP and complement are important mediators of tissue damage in acute myocardial infarction J.Expl Med 1999, v. 190, N 12, 1733-1741

Zhivotovsky B, Orrenius S, Brustugun OT, Doskeland SO Injected cytochrome c induces apoptosis Nature 1998, v. 391, 449-450

M. Uchida et al Targeting of Cancer Cells with Ferrimagnetic Ferritin Cage Nanoparticles JACS 2006, v128, N 51, pp 16626 - 16633

F0002 Ferritin from bovine spleen (apo-form). It is prepared from F0001

F0003 Ferritin from human spleen (holo form). Iron containing protein.The protein has diagnostic significance and its concentration reflects various pathologic conditions (anemia, hemochromatosis, some types of tumors). Preparation can be applied for antibody preparaion.

1.Scholefield JH et al Serum ferritin: screening test for colorectal cancer Dis Colon Rectum 1998, v. 41, N 8, 1029-1031

2. Sun-Ah You Ferritin in atherosclerosis Clin Chim Acta 2005, v. 357, N1-2, 1-16

3.Joshi JG et al Ferritin –a general metal detoxicant Biol Trace Elem Res 1988, Publ 1989, v. 21, 105-110

F0004 Ferritin from human spleen. (apo form). It is prepared from F003

F0073 Fibrinogen from bovine plasma. About 65-75% of the protein is clottable.

F0123 Fibrinogen from porcine plasma. About 65-75% of the protein is clottable.

1.Um SH et alAFP impairs APC function and induces their apoptosis J.Immunol 2004, v. 173, N 3, 1772-1778

2.Semenkova LN et al AFP induced apoptosis in human hepatoma cells Tumor Biology 1998, v. 19, 261-274

3. Uriel J The physiological role of AFP in cell growth and differentiation J.natl Med Allied Sci 1989, v. 33, 12-17

H0008 Hemoglobin from bovine erythrocytes (ferrous) The preparation is homogeneous by electrophoresis in 8% PAAG conducted according to Davis. E1%530 nm =9. The preparation is supplied in solution to prevent its conversion to methemoglobin

H0009 Hemoglobin from human erythrocytes (ferrous) The preparation is homogeneous by electrophoresis in 8% PAAG conducted according to Davis. The preparation after its conversion to cyanmethemoglobin can be applied as standard in diagnostic kits for determination of Hb

H0010 Hemoglobin F from human erythrocytes. It is alkaline resistant fraction of total hemoglobin The preparation is homogeneous by electrophoresis in 8% PAAG conducted according to Davis.

Barnard ML, Muller-Eberhardt U Turrens JF Protective role of hemopexin on heme dependent lung oxidative stress BBRC 1993, v. 192, N 1, 82-88

Lectins

1. S. Saevarsdottir et al Mannan binding lectin as an adjunct to risk assessment for myocardial infarction in individuals with enhanced risk J. Exp. Med. 2005 201: 117-125

2. Miyagi T et al Concanavalin A injection activates intrahepatic innate immune cells to provoke an antitumor effect in murine liver Hepatology 2004, v. 40, N 5, 1190-1196

3. Gastman B et al A novel apoptotic pathway as defined by lectin cellular initiative BBRC 2004, v. 316, N 1, 263-271

4.Nangia-Makker P et al Carbohydrate binding proteins in cancer and their ligands as therapeutic agents Trends Mol Med 2002, v. 8, 187-192

5. Gabius HJ, The sugar code: functional lectinomics BBA 2002, v. 1572, 165-177

6.Singh RS et al Lectins: sources, activities and applications Crit Rev Biotechnol 1999, v. 19, N 2, 145-178

L0086 Lectin from soy bean (glycine max). The preparation is homogeneous by electrophoresis in 8% PAAG. It is not blood group specific and it has specificity for N-acetyl galactosamine. Preparation after immobilization on various carriers can be applied for purification of appropriate glycoproteins

L0087 Lectin from soy bean (glycine max) conjugated with colloidal gold. The preparation can be used in SEM for study of membrane dynamics.

0088 Lectin from soy bean . (glycine max), peroxidase labeled. The preparation can be used for study of membrane dynamics by EIA like analysis.

L0090 Lectin from lentils (lens culinaris) conjugated with colloidal gold. The preparation can be used in SEM for study of membrane dynamics

L0091 Lectin from lentils (lens culinaris) conjugated with peroxidase. The preparation can be used for study of membrane dynamics by EIA like analysis

L0098 Lectin from wheat germ(triticum vulgaris) conjugated with colloidal gold. The preparation can be used in SEM for study of membrane dynamics

L0104 Lectin from wheat germ(triticum vulgaris) conjugated with peroxidase. The preparation can be used for study of membrane dynamics by EIA analysis

L0074 Lysozyme from egg white, crystallized, dialyzed, lyophilized. The protein is useful for preparation of protoplasts.

L0115 Lysozyme from human milk. The preparation is homogeneous by electrophoresis in 10% PAAG. The preparation is suitable for preparation of monospecific antibodies.

1. Nadji M et alPSA an immunohistologic marker for prostatic neoplasms Cancer 1981, v. 48, 1229.

2.Stamey TA et al PSA as a serum marker for adenocarcinoma of the prostate N.Engl J. Med 1987, v. 317, 909-916

T0045 Thromboplastin from rabbit brain or lung. Highly active lyophilized powder. Reconstitution by calcium chloride gives normal range for plasma coagulation 13-16 sec

1.Nature 1954, v. 174, N 4436 880-881

2.Blood 1964, v. 23, 657

Thromboplastin from bovine lung. Highly active lyophilized powder. Reconstitution by calcium chloride gives normal range for plasma coagulation 14-17 sec

DeJong G et al The biology of transferrin Clin Chim Acta 1990, 1-2, 1-46

T0007 Transferrin apo form from human plasma. Iron- transport protein. Prepared from T0006. The preparation can be appled as carrier for other metals.