Analytical Data
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Gene name
CHST10
- Application
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Alternative Names
CHST10；Carbohydrate sulfotransferase 10
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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
O43529
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Expression Region
28-356aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MTFKDPDVYS AKQEFLFLTT MPEVRKLPEE KHIPEELKPT GKELPDSQLV QPLVYMERLE LIRNVCRDDA LKNLSHTPVS KFVLDRIFVC DKHKILFCQT PKVGNTQWKK VLIVLNGAFS SIEEIPENVV HDHEKNGLPR LSSFSDAEIQ KRLKTYFKFF IVRDPFERLI SAFKDKFVHN PRFEPWYRHE IAPGIIRKYR RNRTETRGIQ FEDFVRYLGD PNHRWLDLQF GDHIIHWVTY VELCAPCEIM YSVIGHHETL EDDAPYILKE AGIDHLVSYP TIPPGITVYN RTKVEHYFLG ISKRDIRRLY ARFEGDFKLF GYQKPDFLLN
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Molecular Weight
41 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
Related Products
Protein Description
CHST10, or Carbohydrate Sulfotransferase 10, is an important enzyme involved in the biosynthesis of sulfated glycosaminoglycans, particularly in the modification of heparan sulfate. This enzyme plays a critical role in various biological processes, including cell signaling, development, and disease progression. Alterations in CHST10 activity have been linked to several pathological conditions, including cancer and inherited disorders characterized by glycosaminoglycan metabolism disruption. Recent advances in recombinant protein technology have enabled the production and characterization of CHST10, providing insights into its functional mechanisms and structural properties. Studies focus on understanding the enzyme’s substrate specificity and catalytic efficiency, as well as its interactions with other proteins and cellular components. Understanding CHST10's role in glycosaminoglycan sulfation is crucial, as it could lead to the development of therapeutic strategies targeting diseases associated with its dysregulation. By employing recombinant methods, researchers aim to elucidate CHST10’s biochemical pathways, paving the way for potential interventions in conditions linked to aberrant sulfation processes. Such research not only enhances our understanding of CHST10's biological significance but also contributes to the broader field of glycobiology and its implications in health and disease.
