Analytical Data
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Gene name
HS2ST1
- Application
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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 90% as determined by SDS-PAGE.
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Uniprot
Q7LGA3
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Expression Region
Asn29~Asn356
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Molecular Weight
43kDa
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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
Related Products
Protein Description
The HS2ST1 protein, or Heparan Sulfate 2-O-sulfotransferase 1, is an enzyme critical for the biosynthesis of heparan sulfate, a complex glycosaminoglycan found on cell surfaces and in the extracellular matrix. This protein plays a pivotal role in various biological processes, including cell signaling, growth factor interaction, and the regulation of cell adhesion. Dysregulation of HS2ST1 has been implicated in several diseases, including cancer, where altered heparan sulfate modifications affect tumor progression and metastasis. Furthermore, HS2ST1 is essential for the modification of proteoglycans that mediate interactions between cells and the extracellular environment. Understanding the structure, function, and regulation of HS2ST1 is important for developing therapeutic strategies aimed at modulating its activity, potentially offering new avenues for the treatment of diseases linked to heparan sulfate dysfunction. The investigation of HS2ST1 and its recombinant forms can provide insights into its catalytic mechanisms and the specific modifications it imparts to heparan sulfate, thereby contributing to the broader field of glycoscience and its applications in medicine and biotechnology.
