Analytical Data
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Gene name
Gly
- Application
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Alternative Names
Gly；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
MTMPVNGAHKDADLWSSHDKMLAQPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYKLDPQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGYINYDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGCRAGMIFYRKGVKSVDPKTGKEILYNLESLINSAVFPGLQGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALSEALTELGYKIVTGGSDNHLILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKDFQKVAHFIHRGIELTLQIQSDTGVRATLKEFKERLAGDKYQAAVQALREEVESFASLFPLPGLPDF
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Molecular Weight
53 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
Glycoproteins, characterized by the covalent attachment of glycans to amino acid residues, play crucial roles in various biological processes, including cell signaling, immune response, and protein stability. The study of glycoproteins, particularly recombinant glycoproteins, has gained significant attention in recent years due to their importance in therapeutic applications and vaccine development. Advances in recombinant DNA technology allow for the production of these complex molecules in host systems such as yeast, bacteria, or mammalian cells, enabling the controlled manipulation of glycosylation patterns. This tailored glycosylation is essential, as it influences the protein's functionality, immunogenicity, and pharmacokinetics. As more therapeutic proteins are engineered to include glycosylation modifications, understanding the biosynthetic pathways and developing efficient production techniques have become vital areas of research. Furthermore, with the increasing recognition of glycosylation's role in disease mechanisms, especially in cancer and infectious diseases, studying recombinant glycoproteins offers insights into disease pathology and potential therapeutic targets. The integration of innovative technologies, such as CRISPR gene editing and bioinformatics for glycan analysis, is propelling the field forward, positioning recombinant glycoproteins at the forefront of biomedicine and biotechnology.
