Analytical Data
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Gene name
SHMT1
- Application
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Alternative Names
Serine Hydroxymethyltransferase Cytosolic; SHMT; Glycine Hydroxymethyltransferase; Serine Methylase; SHMT1
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Species
Human
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Source
HEK293
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Tag
C-6*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
AAH07979.1
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Expression Region
M3-F483
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AA Sequence
MPVNGAHKDADLWSSHDKMLAQPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYKLDPQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGYINYDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGCRAGMIFYRKGVKSVDPKTGKEILYNLESLINSAVFPGLQGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALSEALTELGYKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKDFQKVAHFIHRGIELTLQIQSDTGVRATLKEFKERLAGDKYQAAVQALREEVESFASFFPLPGLPDF
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Protein Length
Full Length of Mature Protein
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Molecular Weight
55.0 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 vital enzyme involved in the folate and amino acid metabolism, playing a crucial role in the conversion of serine to glycine and the interconversion of tetrahydrofolate derivatives. This enzyme is particularly significant in cellular processes like DNA synthesis and repair, which are essential for normal cell function and proliferation. Dysregulation or mutations in SHMT1 have been associated with various diseases, including cancer, demonstrating its potential as a therapeutic target. The recombinant expression of SHMT1 allows for the detailed study of its structure, function, and regulation, providing insights into its role in metabolic pathways and disease mechanisms. By producing SHMT1 in a controlled laboratory setting, researchers can investigate its kinetics, substrate specificity, and interaction with other biomolecules. Additionally, understanding its enzymatic properties may lead to the development of small molecule inhibitors or modulators, offering new avenues for treatment strategies in conditions where SHMT1 activity is altered. This research underscores the importance of SHMT1 in metabolic regulation and highlights the potential of recombinant proteins in elucidating biological functions and therapeutic applications.
