GGH, 25-318aa, Human

Category: Proteins
Catalog
01-P1399
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Product Name GGH, 25-318aa, Human
Description Gamma-glutamyl hydrolase, also known as GGH, is a homodimeric protein that catalyzes the cleavage of the gamma-glutamyl chain of folylpoly-gamma-glutamyl substrates and is a central enzyme in folyl and antifolyl poly-gamma-glutamate metabolism. GGH may play an important role in the bioavailability of dietary pteroylpolyglutamates and in the metabolism of pteroylpolyglutamates and antifolates. Recombinant human GGH protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.
Synonyms Gamma-glutamyl hydrolase, GH
Host E. coli
Molecular Weight 25.0kDa (234aa), confirmed by MALDI-TOF
Amino Acid Sequence MGSSHHHHHH SSGLVPRGSH MRPHGDTAKK PIIGILMQKC RNKVMKNYGR YYIAASYVKY LESAGARVVP VRLDLTEKDY EILFKSINGI LFPGGSVDLR RSDYAKVAKI FYNLSIQSFD DGDYFPVWGT CLGFEELSLL ISGECLLTAT DTVDVAMPLN FTGGQLHSRM FQNFPTELLL SLAVEPLTAN FHKWSLSVKN FTMNEKLKKF FNVLTTNTDG KIEFISTMEG YKYPVYGVQW HPEKAPYEWK NLDGISHAPN AVKTAFYLAE FFVNEARKNN HHFKSESEEE KALIYQFSPI YTGNISSFQQ CYIFD
Reactivity Human
Applications SDS-PAGE
Form Liquid, in 20mM Tris-HCl buffer (pH 8.0) containing 1mM DTT, 10% glycerol, 100mM NaCl
Concentration 0.5mg/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 Rhee M S., et al. (1998) Mol Pharmacol. 53:1040-1046. Galivan J., et al. (1999) Semin Oncol. 26:33-37.
Background Gamma-glutamyl hydrolase, also known as GGH, is a homodimeric protein that catalyzes the cleavage of the gamma-glutamyl chain of folylpoly-gamma-glutamyl substrates and is a central enzyme in folyl and antifolyl poly-gamma-glutamate metabolism. GGH may play an important role in the bioavailability of dietary pteroylpolyglutamates and in the metabolism of pteroylpolyglutamates and antifolates. Recombinant human GGH protein, 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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