Analytical Data
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Gene name
SHMT2
- Application
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Alternative Names
SHMT2；Serine hydroxymethyltransferase. mitochondrial
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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
P34897
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Expression Region
30-504aa
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AA Sequence
N AAQTQTGEAN RGWTGQESLS DSDPEMWELL QREKDRQCRG LELIASENFC SRAALEALGS CLNNKYSEGY PGKRYYGGAE VVDEIELLCQ RRALEAFDLD PAQWGVNVQP YSGSPANLAV YTALLQPHDR IMGLDLPDGG HLTHGYMSDV KRISATSIFF ESMPYKLNPK TGLIDYNQLA LTARLFRPRL IIAGTSAYAR LIDYARMREV CDEVKAHLLA DMAHISGLVA AKVIPSPFKH ADIVTTTTHK TLRGARSGLI FYRKGVKAVD PKTGREIPYT FEDRINFAVF PSLQGGPHNH AIAAVAVALK QACTPMFREY SLQVLKNARA MADALLERGY SLVSGGTDNH LVLVDLRPKG LDGARAERVL ELVSITANKN TCPGDRSAIT PGGLRLGAPA LTSRQFREDD FRRVVDFIDE GVNIGLEVKS KTAKLQDFKS FLLKDSETSQ RLANLRQRVE QFARAFPMPG FDEH
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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 an enzyme that plays a critical role in one-carbon metabolism, converting serine and tetrahydrofolate to glycine and 5,10-methylenetetrahydrofolate, which are essential for nucleotide synthesis and methylation reactions. The importance of SHMT2 has gained attention due to its association with various diseases, particularly cancer, where altered levels can influence tumor metabolism and growth. Inhibition or overexpression of SHMT2 has been linked to changes in cellular proliferation and survival, suggesting its potential as a therapeutic target. Additionally, SHMT2 participates in the regulation of cellular responses to oxidative stress and hypoxia, further underscoring its significance in maintaining cellular homeostasis. The production of recombinant SHMT2 protein enables detailed biochemical analyses, structural studies, and the exploration of its regulatory mechanisms under various physiological and pathological conditions. Understanding SHMT2's function and regulation could provide insights into metabolic rewiring in cancer and other metabolic disorders, highlighting the need for continued research into its properties and potential as a biomarker or therapeutic target.
