Recombinant Human Serine Racemase (SRR) Protein (His-GST)

Name: Recombinant Human Serine Racemase (SRR) Protein (His-GST)
Brand: Beta LifeScience
SKU: BLC-06977P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Serine Racemase (SRR) Protein (His-GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q9GZT4
Target Symbol	SRR
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-GST
Target Protein Sequence	MCAQYCISFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPDALERKPKAVVTHSSGNHGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIAGQGTIALEVLNQVPLVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMPNLYPPETIADGVKSSIGLNTWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQTVSPEVKNICIVLSGGNVDLTSSITWVKQAERPASYQSVSV
Expression Range	1-340aa
Protein Length	Full Length
Mol. Weight	68.1 kDa
Research Area	Neuroscience
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Catalyzes the synthesis of D-serine from L-serine. D-serine is a key coagonist with glutamate at NMDA receptors. Has dehydratase activity towards both L-serine and D-serine.
Protein Families	Serine/threonine dehydratase family
Database References	HGNC: 14398 OMIM: 606477 KEGG: hsa:63826 STRING: 9606.ENSP00000339435 UniGene: PMID: 28580277 rs391300 SNP, located on the serine racemase (SRR) gene and linked to increased susceptibility to type 2 diabetes, was associated with progression from mild cognitive impairment to probable Alzheimer's disease. PMID: 29338921 Study found an inverse association between the genetic risk off schizophrenia based on 108 genome-wide significantly associated SNPs and the prevalence for treated migraine in a general population sample. This association was primary linked to SNPs associated with genes encoding proteins involved in glutamatergic neurotransmission and could be attributed to the single intronic variant rs4523957 in SRR. PMID: 27394076 Data suggest that Ser-84 and Arg-135 are important in catalysis and substrate specificity of SRR. PMID: 28696262 Magnesium and calcium ions differentially affect human serine racemase activity and modulate its quaternary equilibrium toward a tetrameric form PMID: 28089597 MiR-193a-3p and miR-193a-5p play important roles in osteosarcoma metastasis through down-regulation of the Rab27B and SRR genes and therefore may serve as useful biomarkers for the diagnosis of osteosarcoma PMID: 26913720 Loss-of-function mutation of the gene encoding serine racemase significantly attenuates excitotoxicity in retina. PMID: 26485193 Serine racemase activity and dynamics are regulated by halides, ATP and malonate. PMID: 25331425 In serine racemase, similarly to the related enzyme alanine racemase, the unprotonated pyridoxal-5'-phosphate -substrate intermediate is stabilized mostly due to solvation effects contributed by water molecules and active-site residues. PMID: 25493718 FBXO22 protein is required for optimal synthesis of NMDA receptor coagonist D-serine by interacting with serine racemase, activating it, and preventing its targeting to membranes. PMID: 25336657 cross-talk between allosteric and active sites, leading to the stabilization of two alternative protein conformations with ATP affinities of ~ 10 muM and 1.8 mm PMID: 23992455 S84A serine racemase mutant behaved like serine dehydratase, whereas A65S serine dehydratase mutant acquired an additional function of using D-serine as a substrate. PMID: 23112234 The structural characteristics of SR obtained from live cells suggest that SR is sensitive to oxidation in vivo, perhaps consistent with a scenario in which such modification plays a role in feedback or other forms of regulation. PMID: 22151352 Serine racemase and D-serine are involved in both pre-symptomatic and progressive phases of amyotrophic lateral sclerosis, demonstrating a link between mutant superoxide dismutase (SOD)1 and a glial-derived toxic mediator in transgenic mice. PMID: 22117694 The SRR mRNA is elevated in people death with suicide. PMID: 20385472 The structure of mammalian serine racemase: evidence for conformational changes upon inhibitor binding PMID: 20106978 Data report on the isolation of a cDNA encoding a human serine racemase (SRR) from a human neuronal like cell line. PMID: 15193426 D-serine is synthesized in human placenta by the racemization of L-serine by serine racemase. PMID: 15219883 serine racemase catalyzes the degradation of cellular D-serine itself, through the alpha,beta-elimination of water PMID: 15536068 The frequency of the genotypes showed that 5'-G/C serine racemase is not a major risk factor for schizophrenia. PMID: 16446740 Expression of serine racemaseusing Western blot analysis in postmortem hippocampus and cortex in schizophrenia and a comparison group. PMID: 16837850 Not associated with schizophrenia in a Gefman case-control study. PMID: 17413455 Not associated with bipolar disorder in a German case-control study. PMID: 17413456 observed activation of serine racemase by divalent cations has been assumed to be a side-effect associated with ATP binding, which is known to form a complex with Mg(2+) ions PMID: 17697119 serine racemase and D-amino acid oxidase are expressed in human brain and demonstrate aberrant D-serine metabolism in schizophrenia PMID: 17880399 Analysis of SRR genetic variants in humans identified a robust association with schizophrenia. PMID: 19483194

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.