Analytical Data
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Gene name
SHMT2
- Application
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Alternative Names
Serine methylase; Glycine hydroxymethyltransferase
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P34897
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Expression Region
Asn30~His504
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Molecular Weight
60kDa
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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
SHMT2 (serine hydroxymethyltransferase 2) is a mitochondrial enzyme crucial for one-carbon metabolism and the regulation of cellular methylation reactions, playing a significant role in nucleotide synthesis and cellular proliferation. Altered expression of SHMT2 has been implicated in various cancers, as its activity influences the availability of metabolites required for DNA and RNA synthesis, thereby affecting tumor growth and survival. Understanding the structure and function of SHMT2 is essential for elucidating its role in cancer biology and potential therapeutic strategies. Recent studies have focused on the production of recombinant SHMT2 protein, enabling detailed investigation of its enzymatic properties, substrate specificity, and interactions with other metabolic pathways. Employing techniques such as recombinant DNA technology, researchers can produce SHMT2 in suitable expression systems, allowing for functional assays and structural studies using techniques like X-ray crystallography and NMR spectroscopy. These advancements pave the way for a deeper understanding of SHMT2's role in cellular metabolism and its potential as a target for cancer treatment. By exploring the biochemical characteristics and regulatory mechanisms of SHMT2, researchers aim to uncover novel insights into its involvement in tumorigenesis and develop strategies for pharmacological modulation of its activity in cancer therapy.
