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Laboratory chemicals

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

650/100mgA0145 Asialo-a1-acid glycoprotein prepared from A0018

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

920/100mgA0019 a-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

1150/100mgA0041 Albumin from hen egg white

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

54/250 mgA0079 Albumin acetylated prepared from bovine serum albumin

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.

680/500mgA0078 Albumin glycated prepared from bovine serum albumin

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.

345/20mgA0035 Albumin methylated prepared from bovine serum albumin

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

870/5gA0023 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

440/5UA0024 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

245/mgA0095 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.

345/0.5 mgA0138 Annexin-V-FITC conjugate

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

490/0.1 mgA0096 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

655/10mlA0099 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

390/100mgA0100 Avidin-gold conjugate

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

525/5mlA0101 Avidin-peroxidase conjugate

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

285/5 mgC0020 Calmodulin (phosphodiesterase 3’5’-cyclic nucleotide activator)

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

435/50000UC0011 Casein from bovine milk technical grade

Product can be applied as blocking reagent in various blotting procedures

125/1 kgC0005 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

555/500 mgC0021 Ceruloplasmin from bovine plasma

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

810/20mgC0022 Ceruloplasmin from human plasma

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

825/5mgC0082 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

355/10mgC0048 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

135/1 mgC0017 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.

205/0.5 mgF0001 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 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

345/500mgF0002 Ferritin from bovine spleen (apo-form)

It is prepared from F0001

420/500mgF0003 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

125/1mgF0004 Ferritin from human spleen. (apo form)

It is prepared from F003

120/0.5mgF0073 Fibrinogen from bovine plasma

About 65-75% of the protein is clottable.

125/1gF0123 Fibrinogen from porcine plasma

About 65-75% of the protein is clottable.

155/1 gH0156 Haptoglobin from human plasma

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

750/10 mgH0164 Hemocyanin from Helix pomatia

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

190/25 mgH0008 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

85/100mgH0009 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

105/100mgH0010 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.

145/mgH0012 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

850/50mgI0128 Immunoglobulin G from bovine plasma340/100 mgI0129 Immunoglobulin G from human plasma610/100 mgI0130 Immunoglobulin G from sheep plasma410/100 mgL0039 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.

235/500mg

Lectins

Lectins are group of carbohydrate binding proteins with diverse functions. They have specificity 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

7 Agarwal BB et al Specific binding of concanavalin A to cross-linked dextran gels Biochem J. 1965, v. 96, 23c .

8 Wellman-Labadie O, Lakshminarayanan R Antimicrobial properties of avian eggshell-specific C-type lectin-like proteins FEBS Lett 2008, v 582 699-704.

L0125 C-type lectin like protein from hen egg shell

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

245/10 mgL0013 C-type lectin like protein from hen egg shell conjugated with FITC

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

245/2 mgL0016 C-type lectin like protein from hen egg shell conjugated with peroxidase

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

160/1 mgL0169 Lectin from human plasma (mannose binding lectin)

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

155/1 mgL0089 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

195/10mgL0090 Lectin from lentils (lens culinaris) conjugated with colloidal gold

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

557/10mlL0091 Lectin from lentils (lens culinaris) conjugated with peroxidase

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

135/1mgL0041 Lectin from lentils (lens culinaris) conjugated with FITC

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

215/2 mgL0133 Lectin from lentils conjugated with Sepharose

The preparation can be applied for affinity purification of some glycoproteins

255/25 mlL0150 Lectin from Pleurotus osdiveatus

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

235/10 mgL0151 Lectin from Pleurotus osdiveatus conjugated with peroxidase

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

155/1 mgL0152 Lectin from Pleurotus osdiveatus conjugated with FITC

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

225/2 mgL0139 Lectin from potato tuber

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

205/10mgL0141 Lectin from potato tuber conjugated with colloidal gold

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

557/10mlL0142 Lectin from potato tuber conjugated with peroxidase

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

155/1mgL0085 Lectin from potato tuber conjugated with FITC

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

195/2mgL0086 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

125/10mgL0087 Lectin from soy bean (glycine max) conjugated with colloidal gold

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

557/10mlL0088 Lectin from soy bean (glycine max), peroxidase labeled

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

135/1mgL0014 Lectin from soy bean (glycine max), FITC labeled

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

105/mgL0134 Lectin from soy bean (glycine max) conjugated with Sepharose

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

255/25 mlL0143 Lectin from tomato

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.

225/10mgL0144 Lectin from tomato conjugated with peroxidase

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

145/1mgL0051 Lectin from tomato conjugated with FITC

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

150/2 mgL0153 Lectin from tulip bulbs

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

275/10 mgL0154 Lectin from tulip bulbs conjugated with peroxidase

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

205/1 mgL0155 Lectin from tulip bulbs conjugated with FITC

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

275/2 mgL0097 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.

575/100mgL0098 Lectin from wheat germ (triticum vulgaris) conjugated with colloidal gold

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

557/10mlL0104 Lectin from wheat germ (triticum vulgaris) conjugated with peroxidase

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

145/1 mgL0149 Lectin from wheat germ (triticum vulgaris) conjugated with FITC

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

115/2 mgL0135 Lectin from wheat germ conjugated with Sepharose

The preparation can be applied for purification of some glycoproteins.

255/25 mlL0074 Lysozyme from egg white

Crystallized, dialyzed, lyophilized. The protein is useful for preparation of protoplasts.

215/10gL0115 Lysozyme from human milk

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

335/100000 UM0057 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.

455/1mgP0148 Phosphatase acid from bovine liver

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.

58/50UP0085 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

475/0.1mgS0131 S-100 from bovine brain

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

55/1 mgT0045 Thromboplastin from rabbit brain and 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

89/10x4mlT0124 Thromboplastin from bovine lung

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

76/10x4mlT0006 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

850/gT0007 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

910/1gT0137 Transferrin holo-form from egg white

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

305/1 gT0102 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

95/50mgT0093 Troponin C from human heart

The preparation is homogeneous by electrophoresis in 10 % PAAG

185/1mgT0094 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

115/1mlT0156 Troponin I from human heart

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

350/0.5mgT0157 Troponin T from human heart

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

350/1 mgU0030 Urease from soy bean

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

102/25000 UU0063 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.

295/100U

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