85-1782-10　GCAT, Recombinant, Human, aa22-419, His-Tag (Glycine C-acetyltransferase, KBL) 100ug　137064

特徴

• The degradation of L-threonine to glycine consists of a two-step biochemical pathway involving the enzymes L-threonine dehydrogenase and 2-amino-3-ketobutyrate coenzyme A ligase. L-Threonine is first converted into 2-amino-3-ketobutyrate by L-threonine dehydrogenase. GCAT is the second enzyme in this pathway, which then catalyzes the reaction between 2-amino-3-ketobutyrate and coenzyme A to form glycine and acetyl-CoA. The enzyme is considered a class II pyridoxal-phosphate-dependent aminotransferase.
• Source:Recombinant protein corresponding to human GCAT, fused to His-tag at N-terminal expressed in E.coli.
• Molecular Weight:~45.0kD (419aa)
• AA Sequence:MGSSHHHHHH SSGLVPRGSH MSALAQLRGI LEGELEGIRG AGTWKSERVI TSRQGPHIRV DGVSGGILNF CANNYLGLSS HPEVIQAGLQ ALEEFGAGLS SVRFICGTQS IHKNLEAKIA RFHQREDAIL YPSCYDANAG LFEALLTPED AVLSDELNHA SIIDGIRLCK AHKYRYRHLD MADLEAKLQE AQKHRLRLVA TDGAFSMDGD IAPLQEICCL ASRYGALVFM DECHATGFLG PTGRGTDELL GVMDQVTIIN STLGKALGGA SGGYTTGPGP LVSLLRQRAR PYLFSNSLPP AVVGCASKAL DLLMGSNTIV QSMAAKTQRF RSKMEAAGFT ISGASHPICP VMLGDARLAS RMADDMLKRG IFVIGFSYPV VPKGKARIRV QISAVHSEED IDRCVEAFVE VGRLHGALP
• Enzyme Activity:Not determined. This product is recommended for use in applications that do not require a catalytically active form of the protein.
• Storage and Stability:May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.