Find where to buy products from suppliers in the USA, including: distributors, industrial manufacturers in America, bulk supplies and wholesalers of raw ingredients & finished goods.
Search for products or services, then visit the American suppliers website for prices, SDS or more information. You can also view suppliers in Australia, NZ or the UK.
| Product | Description | |
|---|---|---|
| Transglutaminase | Transglutaminase. Group: Food ingredients. |  |
| Transglutaminase 1 from Human keratinocyte, Recombinant | Transglutaminase is based on the TGM1-allele from I.M.A.G.E.-clone IRAKp961M1628 isolated from human skin squamous cell carcinoma. It is N-terminally fused to a hexahistidine-tag resulting in the encoded N-terminal amino acid sequence MHHHHHHMDGPR. Transglutaminase is purified by IMAC to more than 90 % purity. Applications: This product catalyzes acyl transfer reactions from glutamin residues in proteins or peptides to primary amines, e. g. the formation of ε-(γ-glutamyl) lysine bonds between proteins by transferring the acyl group of a peptide-bound glutamine residue to the primary amino group of a peptide-bound lysine residue. this enzyme may also ...odansylcadaverine-incorporation into N,N-dimethylated casein according to Lorand et al., Anal. Biochem. 44 (221-231)]. Appearance: White lyophilized solid. Storage: Store at ≤ - 20°C. Store working aliquots at ≤ - 20°C. Avoid repeated freezing and thawing.Delivery at ambient temperature is possible. Form: The transglutaminase is lyophilized from 50 mM Tris-HCl pH 8.0, 10 mM Glutathion. Source: E. coli. Species: Human. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine & |  |
| Transglutaminase 2 from Cynomolgus, Recombinant | Transglutaminases are a family of enzymes that catalyze the posttranslational modification of proteins by inserting an isopeptide bond within or between polypeptide chains. These enzymes catalyze the acyl transfer reaction between the γ-carboxyamide groups of peptide-bound glutamine residues and a variety of primary amines, particularly the ε-amino group of lysine. The resulting crosslink is of great significance, since it is highly stable and also resistant to mechanical and proteolytic degradation. Applications: Labeling, immobilisation, conjugation and modification of proteins. Group: Enzymes. Synonyms: transglutaminase; EC 2.3.2.13; 80146-85-6; trans...l., Anal. Biochem. 44 (221-231). Appearance: White lyophilized solid. Storage: Store at -20°C in working aliquots. Repeated freezing and thawing is not recommended.Delivery is possible at ambient temperature. Form: The purified transglutaminase is lyophilized from 10 mM Tris-HCl pH 7.4, 300 mM NaCl, 1 mM DTT, 1 mM EDTA, contains maltodextrin. Source: HEK-293F. Species: Cynomolgus. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase; protein-glutamine & | |
| Transglutaminase 2 from Dog, Recombinant | This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. Applications: The transglutaminase 2 catalyzes acyl transfer reactions from glutamine residues in proteins or peptides to primary amines, e. g. the formation of ε-(γ-glutamyl) lysine bonds between proteins by transferring the acyl group of a peptide-bound glutamine residue to the primary amino group of a peptide-bound lysine residue. the transglutaminase 2 may also be used for immunoprecipitation. Group: Enzymes. Synonyms: transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor X...1). Appearance: White lyophilized solid. Storage: Store working aliquots at ≤ - 20°C. Avoid repeated freezing and thawing.Delivery is possible at ambient temperature. Form: The transglutaminase is lyophilized from 10 mM Tris-HCl pH 8.1, 150 mM NaCl, 1 mM EDTA, 5 mM DTT. Sample contains maltodextrin. Source: Insect cells. Species: Dog. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase; protein-glutamine γ-glutamyltransferase; TG1. Pack: 250 μ | |
| Transglutaminase 2 from Human tissue, Recombinant | This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. Applications: Transglutaminase 2 catalyzes acyl transfer reactions from glutamin residues in proteins or peptides to primary amines, e. g. the formation of ε-(γ-glutamyl) lysine bonds between proteins by transferring the acyl group of a peptide-bound glutamine residue to the primary amino group of a peptide-bound lysine residue. transglutaminase 2 may also be used for immunoprecipitation. Group: Enzymes. Synonyms: transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa...e: White lyophilized solid. Storage: Store working aliquots at ≤ - 20°C. Avoid repeated freezing and thawing.Delivery is possible at ambient temperature. Form: The transglutaminase is lyophilized from 10 mM Tris-HCl pH 8.1, 150 mM NaCl, 1 mM EDTA, 5 mM DTT. Sample contains maltodextrin. Source: Insect cells. Species: Human. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase; protein-glutamine γ-glutamyltransferase; TG1. Pack: 250 μg; 1mg. | |
| Transglutaminase 2 from Mouse, Recombinant | Transglutaminase 2 is based on clone IRAKp961C066Q. It is N-terminally fused to a hexahistidine-tag resulting in the encoded N-terminal amino acid sequence MHHHHHHAEELLL. Transglutaminase 2 is produced in E. coli and purified by ion metal chelating chromatography to more than 95 % purity. Applications: The transglutaminase 2 catalyzes acyl transfer reactions from glutamine residues in proteins or peptides to primary amines, e. g. the formation of ε-(γ-glutamyl) lysine bonds between proteins by transferring the acyl group of a peptide-bound glutamine residue to the primary amino group of a peptide-bound lysine residue. the transglutaminase 2 may also be used... monodansylcadaverine-incorporation into N,N-dimethylated casein according to Lorand et al., Anal. Biochem. 44 (221-231). Appearance: White lyophilized solid. Storage: Store working aliquots at ≤ - 20°C. Avoid repeated freezing and thawing.Delivery is possible at ambient temperature. Form: The transglutaminase is lyophilized from 50 mM NaH2PO4, 150 mM NaCl, pH 8. Sample contains maltodextrin. Source: E. coli. Species: Mouse. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine &ga | |
| Transglutaminase 2 from Rabbit, Recombinant | This enzyme is based on the NCBI database sequence XM_008256006. It is N-terminally fused to a hexahistidine-tag resulting in the encoded N-terminal amino acid sequence MHHHHHHAEDLIL . This enzyme is produced in E. coli and purified by ion metal chelating chromatography to more than 95 % purity. Applications: The transglutaminase 2 catalyzes acyl transfer reactions from glutamin residues in proteins or peptides to primary amines, e. g. the formation of ε-(γ-glutamyl) lysine bonds between proteins by transferring the acyl group of a peptide-bound glutamine residue to the primary amino group of a peptide-bound lysine residue.the transglutaminase 2 may also b...lyzed monodansylcadaverine-incorporation into N,N-dimethylated casein according to Lorand et al., Anal. Biochem. 44 (221-231)]. Appearance: White lyophilized solid. Storage: Store at -20 °C in working aliquots. Repeated freezing and thawing is not recommended.Delivery is possible at ambient temperature. Form: The enzyme is lyophilized from 50 mM NaH2PO4, 150 mM NaCl, pH 8.0.Sample contains maltodextrin. Source: E. coli. Species: Rabbit. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide: | |
| Transglutaminase 2 from Rat, Recombinant | Transglutaminase 2 is based on clone IRBPp993H102D. It is N-terminally fused to a hexahistidine-tag resulting in the encoded N-terminal amino acid sequence MHHHHHHAEELNL. Transglutaminase 2 is produced in E. coli and purified by ion metal chelating chromatography to more than 95 % purity. Applications: The transglutaminase 2 catalyzes acyl transfer reactions from glutamine residues in proteins or peptides to primary amines, e. g. the formation of ε-(γ-glutamyl) lysine bonds between proteins by transferring the acyl group of a peptide-bound glutamine residue to the primary amino group of a peptide-bound lysine residue. the transglutaminase 2 may also be used ...d monodansylcadaverine-incorporation into N,N-dimethylated casein according to Lorand et al., Anal. Biochem. 44 (271-231). Appearance: White lyophilized solid. Storage: Store working aliquots at ≤ - 20°C. Avoid repeated freezing and thawing.Delivery is possible at ambient temperature. Form: The transglutaminase is lyophilized from 50 mM NaH2PO4, 150 mM NaCl, pH 8. Sample contains maltodextrin. Source: E. coli. Species: Rat. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine &gamm | |
| Transglutaminase 4 from Human prostate, Recombinant | This enzyme is based on clone IMAGp958A10818Q2. It is N-terminally fused to a hexahistidine-tag resulting in the encoded N-terminal amino acid sequence MHHHHHHAEELLL . This enzyme is produced in E. coli and purified by ion metal chelating chromatography to more than 95 % purity. Applications: The transglutaminase 4 catalyzes acyl transfer reactions from glutamine residues in proteins or peptides to primary amines, e. g. the formation of ε-(γ-glutamyl) lysine bonds between proteins by transferring the acyl group of a peptide-bound glutamine residue to the primary amino group of a peptide-bound lysine residue. the transglutaminase 4 may also be used for ...verine-incorporation into N,N-dimethylated casein according to Lorand et al., Anal. Biochem. 44 (221-231). Appearance: White lyophilized solid. Storage: Store at -20 °C in working aliquots. Repeated freezing and thawing is not recommended.Delivery is possible at ambient temperature. Form: The transglutaminase is lyophilized from 10 mM Tris-HCl pH 8.1, 150 mM NaCl, 5 mM DTT, 1 mM EDTA. Sample contains maltodextrin. Source: E. coli. Species: Human. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-gluta | |
| Transglutaminase 7 from Human, Recombinant | Transglutaminase 7 is based on the TGM7-gene on plasmid pCRII-hTGz cl.14 (isolated by Daniel Aeschlimann), corrected by the insertion of a C at position 1169. It is N-terminally fused to a hexahistidine-tag. Applications: The transglutaminase 7 catalyzes acyl transfer reactions from glutamin residues in proteins or peptides to primary amines, e. g. the formation of ε-(γ-glutamyl) lysine bonds between proteins by transferring the acyl group of a peptide-bound glutamine residue to the primary amino group of a peptide-bound lysine residue. the transglutaminase 7 may also be used for immunoprecipitation. Group: Enzymes. Synonyms: transglutaminase; EC 2.3.2.13; ...nd et al., Anal. Biochem. 44 (221-231). Appearance: White lyophilized solid. Storage: Store at ≤ -20?°C.Store working aliquots at ≤ -20?°C. Avoid repeated freezing and thawing.Delivery at ambient temperature is possible. Form: The Transglutaminase is lyophilized from 50 mM Tris-HCl pH 8. Source: E. coli. Species: Human. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase; protein-glutamine γ-glutamyltransferase; TG1. Pack: 250 μg. Cat No: | |
| Transglutaminase from Cynomolgus, Recombinant | Transglutaminases are a family of enzymes that catalyze the posttranslational modification of proteins by inserting an isopeptide bond within or between polypeptide chains. These enzymes catalyze the acyl transfer reaction between the γ-carboxyamide groups of peptide-bound glutamine residues and a variety of primary amines, particularly the ε-amino group of lysine. The resulting crosslink is of great significance, since it is highly stable and also resistant to mechanical and proteolytic degradation. Applications: Labeling, immobilisation, conjugation and modification of proteins. Group: Enzymes. Synonyms: transglutaminase; EC 2.3.2.13; 80146-85-6; transg... casein according to Lorand et al., Anal. Biochem. 44 (221-231). Appearance: White lyophilized solid. Storage: Store at -20°C in working aliquots. Repeated freezing and thawing is not recommended.Delivery is possible at ambient temperature. Form: The purified transglutaminase is lyophilized from 20 mM Tris-HCl pH 7.5, 150 mM NaCl, 1 mM DTT, 1 mM EDTA, contains maltodextrin. Source: Insect cells. Species: Cynomolgus. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutam | |
| Transglutaminase from guinea pig liver, Recombinant | Transglutaminase from guinea pig liver consists of a single polypeptide chain of 691 amino acid residues. It has six potential glycosylation sites (Asn-X-Ser or Asn-X-Thr), but it is not glycosylated. The molecular mass is approximately 76.6 kDa. It is calcium dependent and has several calcium binding sites. The enzyme is inhibited by iodoacetamide and N-ethylmaleimide in the presence of calcium. It catalyzes the incorporation of small molecular weight amines into γ-glutamine sites of proteins. In the absence of small molecular weight amines, it catalyzes the cross linking of proteins that results in the formation of γ-glutamyl-ε-lysine side chai...tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase; protein-glutamine γ-glutamyltransferase. CAS No. 80146-85-6. Transglutaminase. Activity: > 1.5 units/mg. Storage: at -20°C. Form: Lyophilized powder from 5.0 mM Tris, pH 7.5, 0.5 mM DTE and 1 mM CaCl2. Source: Sf9 cells. Species: Guinea pig liver. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase; protein-glutamine γ-glutamyltransferase. Cat No: NATE-1247. | |
| Transglutaminase from Guinea pig, Recombinant | Catalyzes acyl transfer reactions from glutamine residues in proteins or peptides to primary amines, e. g. the formation of ε-(γ-glutamyl) lysine bonds between proteins by transferring the acyl group of a peptide-bound glutamine residue to the primary amino group of a peptide-bound lysine residue. Group: Enzymes. Enzyme Commission Number: EC 2.3.2.13. CAS No. 80146-85-6. Purity: >95% (SDS-PAGE). Mole weight: ~77kDa. Activity: >8 U/mg. Storage: Store at -20°C. After reconstitution, prepare aliquots and store at -20°C. Avoid freeze/thaw cycles. Form: Lyophilized from 50mM NaH2PO4, pH 8.0, containing 150mM sodium chloride. Sample contains maltodextrin. Source: E.coli. Species: Guinea pig liver. Cat No: NATE-1721. | |
| Transglutaminase from Mouse, Recombinant | This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. Applications: Recombinant mouse transglutaminase is a homodimer (a2) composed of two chains held together by non covalent bonds. after activation of the zymogen by thrombin and ca2+ to its active form (a*2, factor xiiia), factor xiiia catalyzes the formation of covalent bridges (ε-(γ-glutamyl) lysine bonds) between fibrin units to increase the elasticity of the clot network. the resulting cross-linked fibrin is insoluble and resistant to lysis. Group: Enzymes. Synonyms: transglutaminase; EC ...ng to Lorand et al., Anal. Biochem. 44 (221-231)]. Appearance: Liquid. Storage: Store working aliquots at ≤ - 20°C. Avoid repeated freezing and thawing. Form: The transglutaminase is formulated in 10 mM Sodium Phosphate pH 8.0, 15 mM NaCl. Sample contains 50% glycerol. Biotinylated-transglutaminase is a Ca2+-dependent enzyme. Source: Insect cells. Species: Mouse. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase; protein-glutamine γ-glutamyltra | |
| Transglutaminase from Streptoverticillium mobaraense (food grade) | Transglutaminase from Streptoverticillium mobaraense consists of 331 amino acid residues. The molecular mass is approximately 38 kDa. Group: Enzymes. Synonyms: transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase; protein-glutamine γ-glutamyltransferase. Enzyme Commission Number: EC 2.3.2.13. Transglutaminase. Activity: 100 U/g. Source: Streptoverticillium mobaraense. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase; protein-glutamine γ-glutamyltransferase. Cat No: NATE-0879. | |
| Transglutaminase, Streptoverticillium mobaraense | Transglutaminase, Streptoverticillium mobaraense (TG) is an enzyme that forms cross-links between protein molecules. Transglutaminase, Streptoverticillium mobaraense attaches proteins and peptides to small molecules, polymers, surfaces, DNA and other proteins. Transglutaminase, Streptoverticillium mobaraense is widely used in food applications in the meat, fish, dairy and baking industries [1] [2] [3]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: TG. CAS No. 80146-85-6. Pack Sizes: 100 mg; 250 mg; 500 mg. Product ID: HY-P2962. |  |
| Biotinylated Transglutaminase from Human, Proenzyme (Zymogen) | This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. Applications: The transglutaminase 3 catalyzes acyl transfer reactions from glutamin residues in proteins or peptides to primary amines, e. g. the formation of ε-(γ-glutamyl) lysine bonds between proteins by transferring the acyl group of a peptide-bound glutamine residue to the primary amino group of a peptide-bound lysine residue. biotinylated transglutaminase 3 may also be used for immunoprecipitation. Group: Enzymes. Synonyms: transglutaminase; EC 2.3.2.13; 80146-85-6; transgl...]. Appearance: Liquid. Storage: Store at -20 °C in working aliquots. Repeated freezing and thawing is not recommended. Form: The transglutaminase is formulated in 10 mM Sodium Phosphate pH 8.0, 15 mM NaCl. Sample contains 50% glycerol. Transglutaminase is a Ca2+-dependent enzyme. Source: E. coli. Species: Human. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase; protein-glutamine γ-glutamyltransferase; TG1. Pack: 100 ug. Cat No: NATE-173 | |
| Biotinylated Transglutaminase from Human, Recombinant | This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. Applications: Recombinant human transglutaminase is a homodimer (a2) composed of two chains held together by non covalent bonds. after activation of the zymogen by thrombin and ca2+ to its active form (a*2, factor xiiia), factor xiiia catalyzes the formation of covalent bridges (ε-(γ-glutamyl) lysine bonds) between fibrin units to increase the elasticity of the clot network. the resulting cross-linked fibrin is insoluble and resistant to lysis. Group: Enzymes. Synonyms: transglutamina... Lorand et al., Anal. Biochem. 44 (221-231). Appearance: Liquid. Storage: Store working aliquots at ≤ - 20°C. Avoid repeated freezing and thawing. Form: The transglutaminase is formulated in 10 mM Sodium Phosphate pH 8.0, 15 mM NaCl. Sample contains 50% glycerol. hFXIII is a Ca2+-dependent enzyme. Source: Insect cells. Species: Human. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase; protein-glutamine γ-glutamyltransferase; TG1. Pack: 50 | |
| Endotoxin free Transglutaminase 2 from Human tissue, Recombinant | This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. Applications: Transglutaminase 2 catalyzes acyl transfer reactions from glutamine residues in proteins or peptides to primary amines, e. g. the formation of ε-(γ-glutamyl) lysine bonds between proteins by transferring the acyl group of a peptide-bound glutamine residue to the primary amino group of a peptide-bound lysine residue. transglutaminase 2 may also be used for immunoprecipitation. this product is suitable for cell culture use. Group: Enzymes. Synonyms: transglutaminase; ...rand et al., Anal. Biochem. 44 (221-231). Appearance: Liquid. Storage: Store working aliquots at ≤ - 20°C. Avoid repeated freezing and thawing. Form: The transglutaminase is supplied in 10 mM Tris-HCl pH 7.2, 150 mM NaCl, 0.5 mM EDTA, 0.5 mM DTT, 10% Glycerol. Source: Insect cells. Species: Human. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase; protein-glutamine γ-glutamyltransferase; TG1. Pack: 250 μg; 1mg. Cat No: NATE-1729. | |
| Native Guinea pig Transglutaminase | Transglutaminase from guinea pig liver consists of a single polypeptide chain of 691 amino acid residues. It has six potential glycosylation sites (Asn-X-Ser or Asn-X-Thr), but it is not glycosylated. The molecular mass is approximately 76.6 kDa. It is calcium dependent and has several calcium binding sites. The enzyme is inhibited by iodoacetamide and N-ethylmaleimide in the presence of calcium. It catalyzes the incorporation of small molecular weight amines into γ-glutamine sites of proteins. In the absence of small molecular weight amines, it catalyzes the cross linking of proteins that results in the formation of γ-glutamyl-ε-lysine side chain peptide...h as huntington?s disease and alzheimer?s disease.transglutaminase has also been used in a study to develop a nonradioactive dot blot assay for transglutaminase activity. Group: Enzymes. Synonyms: transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase; protein-glutamine γ-glutamyltransferase. Enzyme Commission Number: EC 2.3.2.13. CAS No. 80146-85-6. Transglutaminase. Activity: > 1.5 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing Tr | |
| Tissue Transglutaminase from Human, Recombinant | Celiac disease is an enteropathy that is characterized by intestinal lesions of variable severity. Tissue-type transglutaminase (tTG) is believed to be the predominant autoantigen for celiac disease and the corresponding autoantibodies show higher sensitivity and specificity than anti-gliadin antibodies. Highly pure recombinant human tTG is now available to replace the traditionally used tTG fraction from guinea pig. Tissue-type transglutaminase antigens have been specifically modified for improved handling: exchange of an active site amino acid eliminates the protein cross-linking activity of the enzyme, while maintaining the native three-dimensional structure and th...tern-blot. Group: Enzymes. Synonyms: Protein-glutamine gamma-glutamyltransferase 2; EC 2.3.2.13; Tissue transglutaminase; TGase C; TGC; TG(C); Transglutaminase-2; TGase-H; TG2; TGM2. Enzyme Commission Number: EC 2.3.2.13. Purity: Greater than 95% as determined by SDS-PAGE. Transglutaminase. Mole weight: 78,018 Da. Stability: Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°Cfor longer periods of time. Avoid multiple freeze-thaw cycles. Source: Sf9 insect cells. Species: Human. Protein-glutamine gamma-glutamyltransferase 2; EC 2.3.2.13; Tissue transglutaminase; TGase C; TGC; TG(C); Transglutaminase-2; TGase-H; TG2; TGM2. Cat No: NATE-0921. | |
| 1-[(Benzyloxy)carbonyl]-2-indolinecarboxylic Acid | 1-[(Benzyloxy)carbonyl]-2-indolinecarboxylic Acid is a reagent in the preparation of dihydroisoxanzoles derivatives transglutaminase 2 enzyme inhibitor. Group: Biochemicals. Grades: Highly Purified. CAS No. 117483-89-3. Pack Sizes: 100mg, 250mg. Molecular Formula: C17H15NO4, Molecular Weight: 297.31. US Biological Life Sciences. |  Worldwide |
| Boc-L-β-homoproline | Boc-L-β-homoproline is an amino acid derivative which is a reagent in the synthesis of dihydroisoxazole inhbitors of human transglutaminase 2, an enzyme that catalyzes the modification of glutamine residues. This enzyme has been implicated in numerous inflmmatory, fibrotic and other diseases. Synonyms: Boc-L-β-HomoPro-OH; (S)-2-(1-Boc-2-pyrrolidinyl)acetic acid; (S)-2-Carboxymethyl-pyrrolidine-1-carboxylic acid tert-butyl ester; Boc-L-beta-homoproline; (S)-2-(1-(tert-Butoxycarbonyl)pyrrolidin-2-yl)acetic acid; BOC-BETA-HOPRO-OH; 2-[(2S)-1-[(tert-butoxy)carbonyl]pyrrolidin-2-yl]acetic acid; [(2s)-1-(tert-butoxycarbonyl)pyrrolidin-2-yl]acetic acid; Boc-beta-Pro-OH; Boc-beta-Homopro-OH; Boc-I(2)-HoPro-OH; Boc-Pro-(C#CH2)OH; Boc beta Homopro OH; Boc beta Pro OH; BOC BETA HOPRO OH. Grades: ≥ 98% (HPLC). CAS No. 56502-01-3. Molecular formula: C11H19NO4. Mole weight: 229.28. |  |
| Cystamine | Cystamine is the disulfide form of the free thiol, cysteamine. Cystamine is an orally active transglutaminase (Tgase) inhibitor. Cystamine also has inhibition activity for caspase-3 with an IC 50 value of 23.6 μM. Cystamine can be used for the research of severals diseases including Huntington's disease (HD) [1] [2] [3]. Uses: Scientific research. Group: Signaling pathways. CAS No. 51-85-4. Pack Sizes: 10 mM * 1 mL; 50 mg; 100 mg; 250 mg; 500 mg. Product ID: HY-124476. | |
| Cystamine dihydrochloride | Cystamine dihydrochloride is the dihydrochloride salt of cystamine, which is an organic disulfide that inhibits tissue transglutaminase (TGM2) with an IC50 value of approximately 2.5 mM. It is orally available, and decreases aggregated and cross-linked huntingtin in transfected cells. It is neuroprotective in mouse models of Huntington's disease. It has exhibited suppressive effects against HIV replication in infected human cells. It could extend survival and improve motor performance in transgenic HD mice. It inhibits caspase 3, increases intracellular glutathione, and reduces inflammation in a rat model of inflammatory bowel disease. Uses: Enzyme inhibitors. Synonyms: 2-(2-aminoethyldisulfanyl)ethanamine; dihydrochloride. Grades: > 97 %. CAS No. 56-17-7. Molecular formula: C4H14Cl2N2S2. Mole weight: 225.20. | |
| Cystamine dihydrochloride | Cystamine (dihydrochloride) is the disulfide form of the free thiol, cysteamine. Cystamine is an orally active transglutaminase (Tgase) inhibitor. Cystamine also has inhibition activity for caspase-3 with an IC 50 value of 23.6 μM. Cystamine can be used for the research of severals diseases including Huntington's disease (HD) [1] [2] [3]. Uses: Scientific research. Group: Signaling pathways. CAS No. 56-17-7. Pack Sizes: 10 mM * 1 mL; 10 g. Product ID: HY-W020050. | |
| GK921 | GK921 is a transglutaminase 2 (TGase 2) inhibitor with average GI50 of 0.9 μM in cancer cell lines. Synonyms: GK921; GK-921; GK 921. Grades: >98%. CAS No. 1025015-40-0. Molecular formula: C21H20N4O. Mole weight: 344.41. | |
| Human Factor XIII | Factor XIII is the zymogenic form of the glutaminyl-peptide g-glutamyl transferase factor XIIIa (fibrinoligase, plasma transglutaminase, fibrin stabilizing factor, E.C. 2.3.2.13). Factor XIII is unique among transamidases in that it is a zymogen in vivo. Factor XIII is found both extracellularly in plasma and intracellularly in platelets, megakaryocytes, monocytes, placenta, uterus, liver and prostrate tissues. Plasma factor XIII is synthesized in the liver and circulates as a tetramer (Mr=320,000), composed of 2 pairs of nonidentical subunits (A2B2). The intra-cellular forms are synthesized in the tissues where they reside as dimers (Mr=146,000) of 2 identical A chains (A2). The A ...nly after the Ca2+ (Kd=10-3M) and fibrin(ogen) (Kd=10-8M) dependent dissociation of the B subunit dimer from the A2' dimer.In the coagulation cascade, factor XIIIa functions to stabilize the fibrin clot by crosslinking the a and g-chains of fibrin. Other proteins known to be substrates for Factor XIIIa which may be hemostatically important include fibronectin, α2-antiplasmin, collagen, factor V, von Willebrand Factor and thrombospondin.Factor XIII is purified from fresh frozen human plasma by a modification of the procedures described by Folke and Lorand involving barium citrate, ammonium sulfate and glycine precipitations, ion exchange chromatography and gel filtration. Factor | |
| LDN-27219 | LDN-27219 is a revesible inhibitor of transglutaminase 2 (TG2) that binds to the GTP binidng site of the enzyme and inhbits activity with and IC50 of 600 nM. Synonyms: LDN 27219; LDN 27219. Grades: >98%. CAS No. 312946-37-5. Molecular formula: C20H16N4O2S2. Mole weight: 408.5. | |
| MT-4 | MT-4 is a derivative of a tissue transglutaminase ( TG2 ) inhibitor. MT-4 targets the complex of TG2 and fibronectin (FN) (TG2/FN) and inhibits the adhesion of tumor cells to the matrix. MT-4 inhibits the adhesion of ovarian cancer (OC) cells to the peritoneum and increases the sensitivity of OC cells to paclitaxel. Uses: Scientific research. Group: Signaling pathways. CAS No. 2327925-35-7. Pack Sizes: 10 mM * 1 mL; 5 mg; 10 mg; 25 mg; 50 mg; 100 mg. Product ID: HY-128595. | |
| protein-glutamine γ-glutamyltransferase | Requires Ca2+. The γ-carboxamide groups of peptide-bound glutamine residues act as acyl donors, and the 6-amino-groups of protein- and peptide-bound lysine residues act as acceptors, to give intra- and inter-molecular N6-(5-glutamyl)-lysine crosslinks. Formed by proteolytic cleavage from plasma Factor XIII. Group: Enzymes. Synonyms: transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase. Enzyme Commission Number: EC 2.3.2.13. CAS No. 80146-85-6. Transglutaminase. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2286; protein-glutamine γ-glutamyltransferase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase. Cat No: EXWM-2286. | |
| TG53 | TG53 is a novel inhibitor of tissue transglutaminase (TG2) and fibronectin (FN) protein-protein interaction. Group: Biochemicals. Grades: Highly Purified. CAS No. 946369-04-6. Pack Sizes: 1mg, 2.5mg. Molecular Formula: C21H22ClN5O2, Molecular Weight: 411.88. US Biological Life Sciences. | Worldwide |
| Zampilimab | Zampilimab (UCB-7858) is a monoclonal antibody against transglutaminase 2 ( TG2 ). Zampilimab has potential application in renal transplant [1] [2]. Uses: Scientific research. Group: Inhibitory antibodies. Alternative Names: UCB-7858. CAS No. 2098280-42-1. Pack Sizes: 1 mg; 5 mg; 10 mg. Product ID: HY-P99512. | |
Our database is helping our users find suppliers everyday.
