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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

550/250mg

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

630/250mg

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

730/250mg

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

40/1 g

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.

680/1g

Prepared from native albumin

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

735/25g

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.

345/100mg

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

495/5g

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

450/5U

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/mg
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.

550/0.5 mg

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 mg

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

655/10ml

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

125/10mg

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

425/5ml

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

285/5 mg
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

435/50000U

Product can be applied as blocking reagent in various blotting procedures

49/1 kg

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

265/1g

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

810/100mg

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

755/10mg

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

375/1mg

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

475/1mg

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.

175/1mg

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 specific 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

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

325/1g

It is prepared from F0001

385/1g

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

45/0.1mg

It is prepared from F003

52/0.1mg

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

2025/mg

About 65-75% of the protein is clottable.

255/5g

About 65-75% of the protein is clottable.

245/5 g

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

250/5 mg

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

175/100 mg

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

85/100mg

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

105/100mg

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

125/mg

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

1350/100mg
195/ 100 mg
265/100 mg
205/100 mg

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.

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

225/10 mg
FITC

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

225/2 mg
peroxidase

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

150/1 mg

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 mg

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

195/10mg

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

557/10ml

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

135/1mg

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

115/2 mg

The preparation can be applied for affinity purification of some glycoproteins

255/25 ml

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 mg

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

155/1 mg

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

125/2 mg

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

205/10mg

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

557/10ml

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

155/1mg

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

105/2mg

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

125/10mg

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

557/10ml

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

135/1mg

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

105/mg

L0134 Soy bean lectin conjugated with Sepharose. The preparation can be applied for purification of some glycoproteins

255/25 ml

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.

225/10mg

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

145/1mg

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 mg

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

205/10 mg

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

155/1 mg

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

135/2 mg

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.

575/100mg

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

557/10ml

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

145/1 mg

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 mg

The preparation can be applied for purification of some glycoproteins.

255/25 ml

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

215/10g

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

335/100000 U

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.

65/1mg

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.

58/50U

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

315/0.1mg

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 mg

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

72/10x4ml

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

63/10x4ml

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/g

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

910/1g

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

305/1 g

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

95/50mg

The preparation is homogeneous by electrophoresis in 10 % PAAG

185/1mg

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

115/1ml

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

350/0.5mg

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

350/1 mg

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

102/25000 U

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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  • Isolation and purification of higly purified proteins and enzymes from animal and plant sources.
  • Development of monospecific polyclonal antibodies to animal and plant antigens.
  • Immobilization of enzymes on the various matrixes by various methods with consequent recommendation for large scale industrial processes.
 
 
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Product description

  • Proteins and enzymes
  • Antibodies
  • Diagnostic kits
  • Nanopartivles
  • Quantum dots
  • Reagents