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

The preparation after immobilization to Sepharose can be useful for affinity purification of some lectins.

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

Preparation can be applied as the blocking agent for blotting, latex agglutination etc

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.

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.

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

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

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

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.

A0138 Annexin-V from human placenta (placental anticoagulant protein) conjugared with FITC. The preparation can be applied in fluorescent microscopy for detection of early stages of apoptosis.

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

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

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

The preparation can be used in immunochromatographic formats for detection of various antigens.

Preparation can be applied in EIA for binding to biotinylated antibodies.

Ca-binding protein. Molecular weight of protein is about 17 kDa. Activity of preparation is 25000- 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

Product can be applied as blocking reagent in various blotting procedures

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

Activity of preparation is about 4000U/mg 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.

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

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

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

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

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.

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 can be applied as vehicle for selective delivery of drugs to tumor cells

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

M. Truffi et al Ferritin nanocages: A biological platform for drug delivery, imaging and theranostics in cancer. Pharmacological Research (2016) 107 57–65

It is prepared from F0001

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

It is prepared from F003

About 65-75% of the protein is clottable.

About 65-75% of the protein is clottable.

The protein was purified by affinity chromatography on hemoglobin-Sepharose. The preparation contains all three isoforms of the protein.

Spectral ration A280/A540 is about 60. The protein can be used as a carrier protein for production of antibodies to small molecules

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

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

It is alkaline resistant fraction of total hemoglobin The preparation is homogeneous by electrophoresis in 8% PAAG conducted according to Davis.

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

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.

It is a major component of the calcified egg shells. It was found to bind bacterial polysaccharides and has bacteriocidal activity. The preparation is homogeneous by electrophoresis in non denaturing conditions in 15% PAAG

The preparation can be used in SEM for study of membrane dynamics in various physiological processes

The preparation can be used in SEM for study of membrane dynamics in various physiological processes

A Ca-dependent collagenous serum lectin involved in innate immunity. It is recognition molecule which binds to mannose and N-acetyl glucosamine residues

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

The preparation can be used in SEM for study of membrane dynamics

The preparation can be used for study of membrane dynamics by EIA like analysis

The preparation can be used for study of membrane dynamics in various physiological conditions by EIA like analysis

The preparation can be applied for affinity purification of some glycoproteins

The lectin agglutinates human erythrocytes irrespective of their blood group (A, B or 0). The agglutination is inhibited by galactose and its derivatives. The lectin has specificity to N-Acetyl-n-galactosamine, lactose, galactose methyl-D-galacfopyranoside, galactosamine rafhnose

The preparation can be used for study of membrane dynamics by EIA like analysis

The preparation can be used for study of membrane dynamics in various physiological conditions by EIA like analysis

Partially purified. The preparation agglutinates the trypsinized erythrocytes and has affinity for some bacteria

The preparation can be used in SEM for study of membrane dynamics

The preparation can be used in various types of enzyme immune analysis

The preparation can be used for study of membrane dynamics by fluorescent assays under various physiological conditions

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

The preparation can be used in SEM for study of membrane dynamics.

The preparation can be used for study of membrane dynamics by EIA like analysis.

FITC labeled. The preparation can be used for study of membrane dynamics by EIA like analysis.

Soy bean lectin conjugated with Sepharose. The preparation can be applied for purification of some glycoproteins

The preparation is homogeneous by electrophoresis in 8% PAAG. LEA is not blood group specific, but has an affinity for N-acetyl-β-D-glucosamine oligomers.

The preparation can be used for study of membrane dynamics by EIA like analysis and for binding of specified proteins in EIA

The preparation can be used for study of membrane dynamics in various physiological conditions by EIA like analysis and for binding of specified proteins in EIA like assays

A lectin, agglutinates specifically the yeast cells of the Saccharomyces genus, The lectin has specificity to d-mannose, d-mannose 6-phosphate, l-fucose and l-fucosylamine

The preparation can be used for study of membrane dynamics by EIA like analysis and for binding of specified proteins in EIA

The preparation can be used for study of membrane dynamics in various physiological conditions by EIA like analysis and for binding of specified proteins in EIA like assays

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.

The preparation can be used in SEM for study of membrane dynamics

The preparation can be used for study of membrane dynamics by EIA analysis

The preparation can be used for study of membrane dynamics in various physiological conditions by EIA like analysis and for binding of specified proteins in EIA like assays

The preparation can be applied for purification of some glycoproteins.

The preparation is homogeneous by electrophoresis in 10% PAAG. The preparation is suitable for preparation of monospecific antibodies.

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.

Activity 3-5 U/mg of protein. Mol weight is about 14 kDa. The preparation can be applied in sensors for detection of heavy metals and some pesticides.

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

The preparation is homogeneous by electrophoresis in 12% PAAG conducted in non-denaturated conditions. The antibodies to this protein will cross react with human protein and therefore they can be applied for determination of human S-100 in various biological fluids

1. Sarah C. Garrett, Kristen M. Varney, David J. Weber, and Anne R. Bresnick S100A4, a Mediator of Metastasis J. Biol. Chem. 2006 281: 677-680.

2. Miki Okada, Takashi Hatakeyama, Hideaki Itoh, Naoki Tokuta, Hiroshi Tokumitsu, and Ryoji Kobayashi S100A1 Is a Novel Molecular Chaperone and a Member of the Hsp70/Hsp90 Multichaperone Complex J. Biol. Chem. 2004 279: 4221-4233

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

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

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

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

Iron- transport protein. The preparation is homogeneous by electrophoresis in 7% PAAG conducted according to Davis.

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

The preparation is homogeneous by electrophoresis in 10 % PAAG

Protein immobilized 1-3 mg/ ml of gel. This matrix is suitable for affinity purification of human troponin I

Purity more than 90% is estimated by SDS-PAGE in 12% gel

Purity more than 90% is estimated by SDS-PAGE in 12% gel

Partially purified powder. Activity 10-20 U/mg. The preparation is suitable in diagnostic kits for determination of urea.

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.