Home  >  Products  >  SDSL, Recombinant, Human, aa1-329, His-tag (Serine Dehydratase-like, L-serine Deaminase, L-serine Dehydratase/L-threonine Deaminase, L-threonine Dehydratase, TDH, Serine Dehydratase 2, SDH 2)

SDSL, Recombinant, Human, aa1-329, His-tag (Serine Dehydratase-like, L-serine Deaminase, L-serine Dehydratase/L-threonine Deaminase, L-threonine Dehydratase, TDH, Serine Dehydratase 2, SDH 2)

Cat no: S0570-07


Supplier: United States Biological
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SDSL (serine dehydratase-like) is like L-serine dehydratase, uses pyridoxal phosphate. L-serine dehydratase, known simply as serine dehydratase (SDS), is one of three main enzymes that are involved in the metabolism of Glycine and serine. One of several members of the serine/threonine dehydratase family, SDSL may function as a serinespecific dehydratase that plays a role in protein metabolism. It has low serine dehydratase and threonine dehydratase activity. Source: Recombinant corresponding to aa1-329 from human SDSL, fused to His-tag at N-terminal expressed in E.coli. AA Sequence: MGSSHHHHHH SSGLVPRGSH MGSHMDGPVA EHAKQEPFHV VTPLLESWAL SQVAGMPVFL KCENVQPSGS FKIRGIGHFC QEMAKKGCRH LVCSSGGNAG IAAAYAARKL GIPATIVLPE STSLQVVQRL QGEGAEVQLT GKVWDEANLR AQELAKRDGW ENVPPFDHPL IWKGHASLVQ ELKAVLRTPP GALVLAVGGG GLLAGVVAGL LEVGWQHVPI IAMETHGAHC FNAAITAGKL VTLPDITSVA KSLGAKTVAA RALECMQVCK IHSEVVEDTE AVSAVQQLLD DERMLVEPAC GAALAAIYSG LLRRLQAEGC LPPSLTSVVV IVCGGNNINS RELQALKTHL GQV Molecular Weight: ~37.3kD (MALDI-TOF) Storage and Stability: May be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees 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.
Catalogue number: S0570-07
Size: 50ug
Form: Supplied as a liquid in 20mM Tris-HCl buffer, pH 8.0, 2mM DTT, 10% glycerol, 100mM sodium chloride.
Purity: ~90% (SDS-PAGE)
References: 1. Yamada T., et al. (2008) Biochim. Biophys. Acta 1780:809-818 2. Xue, H.H., et al. (1999) J. Biol. Chem. 274:16028-16033.

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