SDSL Human
Serine Dehydratase-Like Human Recombinant
Cat. No.
BT5406
Source
E.coli.
Synonyms
Serine dehydratase-like, SDS-RS1, Serine dehydratase 2, TDH, L-serine dehydratase/L-threonine deaminase, SDH 2, serine dehydratase related sequence 1, EC 4.3.1.17, EC 4.3.1.19.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description
SDSL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 353 amino acids (1-329) and having a molecular mass of 37.3 kDa.
SDSL is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
SDSL is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Introduction
Serine dehydratase L-serine ammonia-lyase (SDSL) is a member of the serine/threonine dehydratase family and acts as a serine-specific dehydratase. This enzyme utilizes pyridoxal phosphate as a cofactor and plays a crucial role in the metabolism of glycine and serine alongside two other key enzymes.
Description
Recombinant human SDSL, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 353 amino acids (residues 1-329) with a molecular weight of 37.3 kDa. This protein is engineered with a 20 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Physical Appearance
Clear, colorless solution, sterile-filtered.
Formulation
The SDSL solution is supplied at a concentration of 0.5 mg/ml in a buffer consisting of 20mM Tris-HCl (pH 8.0), 2mM DTT, 0.1M NaCl, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, freeze the solution at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
Purity is determined to be greater than 90% by SDS-PAGE analysis.
Synonyms
Serine dehydratase-like, SDS-RS1, Serine dehydratase 2, TDH, L-serine dehydratase/L-threonine deaminase, SDH 2, serine dehydratase related sequence 1, EC 4.3.1.17, EC 4.3.1.19.
Source
E.coli.
Amino Acid 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.
Product Science Overview
Gene and Protein Structure
Enzymatic Activity
SDSL exhibits low serine dehydratase and threonine dehydratase activity. It also possesses glutamate racemase activity, which is crucial for the synthesis of D-glutamate and the degradation of L-serine and L-threonine . The enzyme’s activity is dependent on pyridoxal phosphate (PLP) as a cofactor but does not require metal ions or nucleotides .
Functional Significance
The enzyme plays a vital role in maintaining amino acid homeostasis within cells. It is involved in the isoleucine biosynthetic process and the threonine catabolic process . The dehydratase activity of SDSL contributes to the degradation of L-serine and L-threonine, while its racemase activity aids in the synthesis of D-glutamate .
Clinical Relevance
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