Analytical Data
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Gene name
CHST1
- Application
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Alternative Names
CHST1; Carbohydrate sulfotransferase 1; Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 1; GST-1; Keratan sulfate Gal-6 sulfotransferase; KS6ST; KSGal6ST; KSST
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O43916
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Expression Region
168-267aa
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AA Sequence
PPGPADLVLEEGDCVRKCGLLNLTVAAEACRERSHVAIKTVRVPEVNDLRALVEDPRLNLKVIQLVRDPRGILASRSETFRDTYRLWRLWYGTGRKPYNL
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Molecular Weight
36.74 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
CHST1, or carbohydrate sulfotransferase 1, is an enzyme that plays a crucial role in the sulfation of glycosaminoglycans (GAGs), particularly in the biosynthesis of heparan sulfate. This process is essential for various biological functions, including cell signaling, development, and tissue repair. Abnormalities in CHST1 activity have been linked to several diseases, including certain types of cancer and developmental disorders, underscoring the enzyme's significance in health and disease. The recombinant expression of CHST1 has become a focal point in biochemical research, as it allows for the detailed study of the enzyme’s structure-function relationships and its interactions with substrates. Furthermore, the availability of recombinant CHST1 enables the exploration of potential therapeutic approaches to modulate its activity, aiming to correct sulfation defects or to engineer novel glycosaminoglycan-based therapeutics. In this context, studies on CHST1 not only enhance our understanding of glycosylation processes but also offer insights into the therapeutic benefits of targeting sulfation pathways in various diseases. Exploring the biochemical properties and functional implications of CHST1 through recombinant techniques can pave the way for innovative strategies in regenerative medicine and targeted therapies.
