Analytical Data
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Gene name
SHMT1
- Application
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Alternative Names
SHMT1;Serine hydroxymethyltransferase. cytosolic
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P34896
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Expression Region
1-483aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMTMPVNGAHKDADLWSSHDKMLAQPLKDSD VEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQ RYYGGTEFIDELETLCQKRALQAYKLDPQCWGVNVQPYSGSPANFAVYTA LVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGY INYDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMA HISGLVAAGVVPSPFEHCHVVTTTTHKTLRGCRAGMIFYRKGVKSVDPKT GKEILYNLESLINSAVFPGLQGGPHNHAIAGVAVALKQAMTLEFKVYQHQ VVANCRALSEALTELGYKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEAC SIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKDFQKVAHFIHRGIE LTLQIQSDTGVRATLKEFKERLAGDKYQAAVQALREEVESFASFFPLPGL PDF
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Molecular Weight
55 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
SHMT1 (serine hydroxymethyltransferase 1) is a crucial enzyme involved in the one-carbon metabolism pathway, playing a significant role in cellular folate metabolism and nucleotide synthesis. It catalyzes the reversible conversion of serine and tetrahydrofolate to glycine and 5,10-methylenetetrahydrofolate, facilitating vital processes such as DNA synthesis and repair. Dysregulation of SHMT1 has been implicated in various diseases, including cancer, where altered one-carbon metabolism contributes to uncontrolled cell proliferation and resistance to therapy. Additionally, SHMT1 is associated with conditions such as neurodegenerative disorders and cardiovascular diseases. Given its critical role in metabolism, SHMT1 has garnered attention as a potential therapeutic target. The study of recombinant SHMT1 protein enables researchers to elucidate the enzyme's structure, function, and regulatory mechanisms, providing insights into its involvement in metabolic pathways and disease states. Understanding SHMT1's enzymatic properties can lead to the development of inhibitors or modulators as therapeutic agents, enhancing treatment strategies for diseases linked to metabolic dysregulation. The production and characterization of recombinant SHMT1 protein, therefore, not only advance our biochemical knowledge but also hold promise for innovative therapeutic interventions.
