Analytical Data
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Gene name
HS2ST1
- Application
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Alternative Names
HS2ST1；HS2ST；KIAA0448；Heparan sulfate 2-O-sulfotransferase 1
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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
Q7LGA3
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Expression Region
1-356aa
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AA Sequence
MGLLRIMMPPKLQLLAVVAFAVAMLFLENQIQKLEESRSKLERAIARHEVREIEQRHTMDGPRQDATLDEEEDMVIIYNRVPKTASTSFTNIAYDLCAKNKYHVLHINTTKNNPVMSLQDQVRFVKNITSWKEMKPGFYHGHVSYLDFAKFGVKKKPIYINVIRDPIERLVSYYYFLRFGDDYRPGLRRRKQGDKKTFDECVAEGGSDCAPEKLWLQIPFFCGHSSECWNVGSRWAMDQAKYNLINEYFLVGVTEELEDFIMLLEAALPRFFRGATELYRTGKKSHLRKTTEKKLPTKQTIAKLQQSDIWKMENEFYEFALEQFQFIRAHAVREKDGDLYILAQNFFYEKIYPKSN
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Molecular Weight
41.8 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
HS2ST1, or Heparan Sulfate 2-O-sulfotransferase 1, is an essential enzyme that plays a critical role in the biosynthesis of heparan sulfate, a glycosaminoglycan involved in numerous biological processes, including cell signaling, cell adhesion, and extracellular matrix formation. The significance of HS2ST1 has gained attention due to its involvement in various pathological conditions, such as cancer progression and viral infections, where heparan sulfate serves as a receptor for pathogens. Understanding the structure and function of HS2ST1 can provide insights into its regulatory mechanisms and potential therapeutic targets. Furthermore, recombinant protein production of HS2ST1 allows for detailed biochemical assays and structural studies that can elucidate its specific enzymatic functions and interaction with substrates. The exploration of HS2ST1 and its role in modifying heparan sulfate chains can offer valuable insights into glycosaminoglycan-mediated biological processes and pave the way for novel strategies in treating diseases associated with heparan sulfate dysregulation.
