CD224 Recombinant Protein 
Datasheet
COA
MSDS
SHIP
Product Name :
CD224 Recombinant Protein Swiss-Prot :
P19440 Host :
E.coli Tag :
Amino acid Sequence :
PSASKEPDNHVYTRAAVAADAKQCSKIGRDALRDGGSAVDAAIAALLCVGLMNAHSMGIGGGLFLTIYNSTTRKAEVINAREVAPRLAFATMFNSSEQSQKGGLSVAVPGEIRGYELAHQRHGRLPWARLFQPSIQLARQGFPVGKGLAAALENKRTVIEQQPVLCEVFCRDRKVLREGERLTLPQLADTYETLAIEGAQAFYNGSLTAQIVKDIQAAGGIVTAEDLNNYRAELIEHPLNISLGDVVLYMPSAPLSGPVLALILNILKGYNFSRESVESPEQKGLTYHRIVEAFRFAYAKRTLLGDPKFVDVTEVVRNMTSEFFAAQLRAQISDDTTHPISYYKPEFYTPDDGGTAHLSVVAEDGSAVSATSTINLYFGSKVRSPVSGILFNNEMDDFSSPSITNEFGVPPSPANFIQPGKQPLSSMCPTIMVGQDGQVRMVVGAAGGTQITTATALAIIYNLWFGYDVKRAVEEPRLHNQLLPNVTTVERNIDQAVTAALETRHHHTQIASTFIAVVQAIVRTAGGWAAASDSRKGGEPAGY Restriction sites :
NdeI-XhoI Background :
GGT (g-glutamyltranspeptidase) acts as a glutathionase and catalyzes the transfer of the glutamyl moiety of glutathione to a variety of amino acids and dipeptide acceptors. This enzyme is located on the outer surface of the cell membrane and is widely distributed in mammalian tissues involved in absorption and secretion. In humans, hepatic GGT activity is elevated in some liver diseases. GGT1 is released into the bloodstream after liver damage, and an elevated level of the enzyme may be a useful early sign of hepatocellular carcinoma. GGT5 converts leukotriene C4 to leukotriene D4; it does not, however, convert synthetic substrates that are commonly used to assay GGT. In human serum and in human tissues, there is a marked heterogeneity in GGT, but this heterogeneity can be attributed to different glycosylation of the same peptide rather than to the products of different genes. Soluble :
PBS, 4M Urea, PH7.4 Purification&Purity :
Transferred into competent cells and the supernatant was purified by NI column affinity chromatography and the purity is > 85% (by SDS-PAGE). Storage&Stability :
Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze-thaw cycles. Expression vector :
pet-22b(+) BiowMW :
~60kDa Note :
For research use only, not for use in diagnostic procedure. concentration :
CD224 Recombinant Protein Swiss-Prot :
P19440 Host :
E.coli Tag :
Amino acid Sequence :
PSASKEPDNHVYTRAAVAADAKQCSKIGRDALRDGGSAVDAAIAALLCVGLMNAHSMGIGGGLFLTIYNSTTRKAEVINAREVAPRLAFATMFNSSEQSQKGGLSVAVPGEIRGYELAHQRHGRLPWARLFQPSIQLARQGFPVGKGLAAALENKRTVIEQQPVLCEVFCRDRKVLREGERLTLPQLADTYETLAIEGAQAFYNGSLTAQIVKDIQAAGGIVTAEDLNNYRAELIEHPLNISLGDVVLYMPSAPLSGPVLALILNILKGYNFSRESVESPEQKGLTYHRIVEAFRFAYAKRTLLGDPKFVDVTEVVRNMTSEFFAAQLRAQISDDTTHPISYYKPEFYTPDDGGTAHLSVVAEDGSAVSATSTINLYFGSKVRSPVSGILFNNEMDDFSSPSITNEFGVPPSPANFIQPGKQPLSSMCPTIMVGQDGQVRMVVGAAGGTQITTATALAIIYNLWFGYDVKRAVEEPRLHNQLLPNVTTVERNIDQAVTAALETRHHHTQIASTFIAVVQAIVRTAGGWAAASDSRKGGEPAGY Restriction sites :
NdeI-XhoI Background :
GGT (g-glutamyltranspeptidase) acts as a glutathionase and catalyzes the transfer of the glutamyl moiety of glutathione to a variety of amino acids and dipeptide acceptors. This enzyme is located on the outer surface of the cell membrane and is widely distributed in mammalian tissues involved in absorption and secretion. In humans, hepatic GGT activity is elevated in some liver diseases. GGT1 is released into the bloodstream after liver damage, and an elevated level of the enzyme may be a useful early sign of hepatocellular carcinoma. GGT5 converts leukotriene C4 to leukotriene D4; it does not, however, convert synthetic substrates that are commonly used to assay GGT. In human serum and in human tissues, there is a marked heterogeneity in GGT, but this heterogeneity can be attributed to different glycosylation of the same peptide rather than to the products of different genes. Soluble :
PBS, 4M Urea, PH7.4 Purification&Purity :
Transferred into competent cells and the supernatant was purified by NI column affinity chromatography and the purity is > 85% (by SDS-PAGE). Storage&Stability :
Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze-thaw cycles. Expression vector :
pet-22b(+) BiowMW :
~60kDa Note :
For research use only, not for use in diagnostic procedure. concentration :
Blocking peptide available as NCP0378P