Analytical Data
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Gene name
CHST3
- Application
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Alternative Names
CHST3；Carbohydrate sulfotransferase 3
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Species
Mouse
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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
O88199
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Expression Region
39-472aa
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AA Sequence
EKENKIISRV SDKLKQIPHF VADANSTDPA LLLSENASLL SLSELDSTFS HLRSRLHNLS LQLGVEPAME SQEAGAEKPS QQAGAGTRRH VLLMATTRTG SSFVGEFFNQ QGNIFYLFEP LWHIERTVFF QQRGASAAGS ALVYRDVLKQ LLLCDLYVLE PFISPPPEDH LTQFLFRRGS SRSLCEDPVC TPFVKKVFEK YHCRNRRCGP LNVTLAGEAC RRKDHVALKA VRIRQLEFLQ PLVEDPRLDL RVIQLVRDPR AVLASRIVAF AGKYENWKKW LSEGQDQLSE DEVQRLRGNC ESIRLSAELG LRQPAWLRGR YMLVRYEDVA RRPLQKAREM YSFAGIPLTP QVEDWIQKNT QATRDSSDVY STQKNSSEQF EKWRFSMPFK LAQVVQAACG PTMHLFGYKL ARDAASLTNR SISLLEERGT FWVT
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Molecular Weight
52 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
CHST3, or carbohydrate sulfotransferase 3, is a critical enzyme involved in the biosynthesis of sulfated glycosaminoglycans, particularly heparan sulfate. Understanding the function and regulation of CHST3 is essential due to its implications in various biological processes, including cell signaling, development, and disease pathogenesis. Research has shown that aberrations in CHST3 activity can contribute to conditions such as cancer, where altered glycosylation patterns affect tumor cell behavior and interaction with the extracellular matrix. Additionally, CHST3 is implicated in congenital disorders that affect sulfation patterns, leading to significant developmental issues. The recombinant production of CHST3 protein enables detailed studies of its enzymatic properties, substrate specificity, and mechanisms of regulation. Furthermore, studying CHST3 would deepen insights into the therapeutic potential of targeting sulfation pathways in diseases associated with altered glycosaminoglycan function. As the field moves towards precision medicine, understanding the role of CHST3 can pave the way for novel strategies in diagnosis and treatment, particularly in targeting its sulfation pathways for managing diseases characterized by dysregulated glycosylation.
