SPR Mouse
SDR38C1, SPR, Dystonia, Sepiapterin reductase, mCG_128676.
Greater than 95.0% as determined by SDS-PAGE.
Description
SPR Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 285 amino acids (1-262 a.a) and having a molecular mass of 30.3kDa.
SPR is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Sepiapterin Reductase is a crucial enzyme involved in the biosynthesis of tetrahydrobiopterin (BH4), a vital cofactor for aromatic amino acid hydroxylases, including tyrosine hydroxylase, which plays a critical role in dopamine synthesis. This enzyme, belonging to the aldo-keto reductase family, catalyzes the NADPH-dependent reduction of pteridine derivatives. Mutations in the Sepiapterin Reductase gene can lead to DOPA-responsive dystonia due to sepiapterin reductase deficiency, characterized by sustained involuntary muscle contractions, often resulting in abnormal postures. Sepiapterin reductase is also involved in the reduction of exogenous carbonyl compounds and phenylpropanedione.
Recombinant SPR Mouse, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 285 amino acids (with amino acids 1-262 being the SPR protein) and possessing a molecular mass of 30.3 kDa. This protein is engineered with a 23 amino acid His-tag at its N-terminus and is purified using proprietary chromatographic techniques.
The SPR protein solution is provided at a concentration of 1 mg/ml and is formulated in a buffer containing 20 mM Tris-HCl (pH 8.5), 1 mM DTT, and 10% glycerol.
For short-term storage (2-4 weeks), the protein should be stored at 4°C. For extended storage, it is recommended to store the protein at -20°C. To further enhance long-term stability, the addition of a carrier protein (0.1% HSA or BSA) is advisable. It is crucial to avoid repeated freeze-thaw cycles to maintain protein integrity.
The purity of the SPR protein is determined to be greater than 95% using SDS-PAGE analysis.
SDR38C1, SPR, Dystonia, Sepiapterin reductase, mCG_128676.
MGSSHHHHHH SSGLVPRGSH MGSMEAGGLG CAVCVLTGAS RGFGRALAPQ LARLLSPGSV MLVSARSESM LRQLKEELGA QQPDLKVVLA AADLGTEAGV QRLLSAVREL PRPEGLQRLL LINNAATLGD VSKGFLNVND LAEVNNYWAL NLTSMLCLTS GTLNAFQDSP GLSKTVVNIS SLCALQPYKG WGLYCAGKAA RDMLYQVLAA EEPSVRVLSY APGPLDNDMQ QLARETSKDP ELRSKLQKLK SDGALVDCGT SAQKLLGLLQ KDTFQSGAHV DFYDC.
Product Science Overview
Sepiapterin reductase (SPR) is an enzyme that plays a crucial role in the biosynthesis of tetrahydrobiopterin (BH4), an essential cofactor for various enzymatic reactions. This enzyme is part of the short-chain dehydrogenase/reductase (SDR) family and is involved in the reduction of sepiapterin to dihydrobiopterin, which is subsequently converted to BH4 .
SPR is a homodimer composed of two subunits. It catalyzes the NADPH-dependent reduction of various carbonyl substances, including derivatives of pteridines . The enzyme’s active site contains key amino acid residues such as Ser-158, Tyr-171, and Lys-175, which are crucial for proton transfer and stabilization of the carbonyl group of substrates .
BH4 is a key cofactor for several enzymes, including nitric oxide synthases (NOSs), aromatic amino acid hydroxylases, and alkylglycerol monooxygenase. These enzymes are involved in various biological processes such as monoamine neurotransmitter formation, immune response, cardiovascular function, and endothelial dysfunction . Therefore, SPR is indirectly associated with these critical physiological functions.
Recombinant mouse SPR is produced using genetic engineering techniques to express the mouse SPR gene in a suitable host system. This recombinant protein is used in research to study the enzyme’s structure, function, and role in disease. It also serves as a tool for screening potential therapeutic compounds targeting SPR .
