A2LD1, 1-153aa, Human

Category: Proteins
Catalog
01-P0959
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Product Name A2LD1, 1-153aa, Human
Description A2LD1, also known as gamma-glutamylaminecyclotransferase, is an enzyme that converts gamma-glutamylamines to free amines and 5-oxoproline. It shows high activity toward gamma-glutamyl-epsilon-lysine, derived from the breakdown of fibrin and other proteins cross-linked by transglutaminases. This protein adopts the newly identified cyclotransferase fold, observed in gamma-glutamylcyclotransferase, an enzyme with activity toward gamma-glutamyl-alpha-amino acids. Recombinant human A2LD1 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography.
Synonyms Gamma-glutamylaminecyclotransferase, GGACT
Host E. coli
Molecular Weight 24.1 kDa (217aa) confirmed by MALDI-TOF
Amino Acid Sequence MGSSHHHHHH SSGLVPRGSH MALVFVYGTL KRGQPNHRVL RDGAHGSAAF RARGRTLEPY PLVIAGEHNI PWLLHLPGSG RLVEGEVYAV DERMLRFLDD FESCPALYQR TVLRVQLLED RAPGAEEPPA PTAVQCFVYS RATFPPEWAQ LPHHDSYDSE GPHGLRYNPR ENR
Tag His-tag
Reactivity Human
Applications SDS-PAGE
Form Liquid, in 20mM Tris-HCl buffer (pH 8.0) containing 1mM DTT, 20% glycerol
Concentration 1 mg/ml (determined by Bradford assay)
Purity > 95% 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 Oakley AJ,., et al. (2010), J Biol Chem., 285:9642-8. Danson JW., et al. (2002), Anal Biochem., 303:120-30.
Background A2LD1, also known as gamma-glutamylaminecyclotransferase, is an enzyme that converts gamma-glutamylamines to free amines and 5-oxoproline. It shows high activity toward gamma-glutamyl-epsilon-lysine, derived from the breakdown of fibrin and other proteins cross-linked by transglutaminases. This protein adopts the newly identified cyclotransferase fold, observed in gamma-glutamylcyclotransferase, an enzyme with activity toward gamma-glutamyl-alpha-amino acids. Recombinant human A2LD1 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography.
Supplier ARP

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