| Product Name | TGM2, 1-687aa, Human |
|---|---|
| Description | TGM2 also known as Protein-glutamine gamma-glutamyltransferase 2. Transglutaminases are enzymes that catalyze the crosslinking of proteins by epsilon-gamma glutamyl lysine isopeptide bonds. While the primary structure of transglutaminases is not conserved, they all have the same amino acid sequence at their active sites and their activity is calcium-dependent. TGM2 acts as a monomer, is induced by retinoic acid, and appears to be involved in apoptosis. Recombinant human TGM2, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. |
| Synonyms | Protein-glutamine gamma-glutamyltransferase 2 isoform a, Transglutaminase 2, G-ALPHA-h, GNAH, HEL-S-45, TG2; TGC |
| Host | E. coli |
| Molecular Weight | 19.5kDa (178aa) |
| Amino Acid Sequence | MGSSHHHHHH SSGLVPRGSH MGSMAEELVL ERCDLELETN GRDHHTADLC REKLVVRRGQ PFWLTLHFEG RNYEASVDSL TFSVVTGPAP SQEAGTKARF PLRDAVEEGD WTATVVDQQD CTLSLQLTTP ANAPIGLYRL SLEASTGYQG SSFVLGHFIL LFNAWCPADA VYLDSEEERQ EYVLTQQGFI YQGSAKFIKN IPWNFGQFED GILDICLILL DVNPKFLKNA GRDCSRRSSP VYVGRVVSGM VNCNDDQGVL LGRWDNNYGD GVSPMSWIGS VDILRRWKNH GCQRVKYGQC WVFAAVACTV LRCLGIPTRV VTNYNSAHDQ NSNLLIEYFR NEFGEIQGDK SEMIWNFHCW VESWMTRPDL QPGYEGWQAL DPTPQEKSEG TYCCGPVPVR AIKEGDLSTK YDAPFVFAEV NADVVDWIQQ DDGSVHKSIN RSLIVGLKIS TKSVGRDERE DITHTYKYPE GSSEEREAFT RANHLNKLAE KEETGMAMRI RVGQSMNMGS DFDVFAHITN NTAEEYVCRL LLCARTVSYN GILGPECGTK YLLNLNLEPF SEKSVPLCIL YEKYRDCLTE SNLIKVRALL VEPVINSYLL AERDLYLENP EIKIRILGEP KQKRKLVAEV SLQNPLPVAL EGCTFTVEGA GLTEEQKTVE IPDPVEAGEE VKVRMDLLPL HMGLHKLVVN FESDKLKAVK GFRNVIIGPA |
| Tag | His-tag |
| Reactivity | Human |
| Applications | SDS-PAGE |
| Form | Liquid, in 20mM Tris-HCl buffer (pH 8.0) containing 10% glycerol |
| Concentration | 1mg/ml (determined by Bradford assay) |
| Purity | > 85% by SDS-PAGE |
| Storage | Can be stored at +4C short term (1-2 weeks). For long term storage, aliquot and store at -2°C or -7°C. Avoid repeated freezing and thawing cycles. |
| References | Jeong JH.,et al. (2013) J. Korean Med. Sci. 28 (7), 1005-1014 |
| Background | TGM2 also known as Protein-glutamine gamma-glutamyltransferase 2. Transglutaminases are enzymes that catalyze the crosslinking of proteins by epsilon-gamma glutamyl lysine isopeptide bonds. While the primary structure of transglutaminases is not conserved, they all have the same amino acid sequence at their active sites and their activity is calcium-dependent. TGM2 acts as a monomer, is induced by retinoic acid, and appears to be involved in apoptosis. Recombinant human TGM2, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. |
| Supplier | ARP |
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