Analytical Data
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基因名
HS3ST1
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简介
The HS3ST1 protein utilizes PAPS to crucially catalyze the transfer of sulfate to position 3 of the glucosamine residue in heparan sulfate (HS), representing the rate-limiting step in HS biosynthesis. This activity is essential for the formation of the anticoagulant heparan sulfate and completion of the antithrombin pentasaccharide binding site. HS3ST1 Protein, Human (sf9, His) is the recombinant human-derived HS3ST1 protein, expressed by Sf9 insect cells , with N-His labeled tag.
- Application
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别名
Heparan sulfate glucosamine 3-O-sulfotransferase 1; 3-OST-1; 3OST; 3OST1
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种属
Human
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表达系统
Baculovirus
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标签
N-His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
O14792
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表达区间
R21-H307
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蛋白长度
Full Length of Mature Protein
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分子量
36 kDa.
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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
HS3ST1 (Heparan Sulfate Three-O-Sulfotransferase 1) is an enzyme that plays a crucial role in the biosynthesis of heparan sulfate, a naturally occurring glycosaminoglycan involved in various biological processes, including cell-cell interactions, signaling, and the modulation of growth factors. The specific sulfation patterns generated by HS3ST1 significantly influence the biological activity of heparan sulfate. Research into the HS3ST1 recombinant protein has gained momentum due to its potential implications in health and disease, particularly in cancer progression and metastasis, where altered heparan sulfate structures can affect tumor behavior. Furthermore, HS3ST1 is of interest in the study of viral infections, as many pathogens exploit heparan sulfate on cell surfaces for entry. Understanding the structure-function relationships of HS3ST1 and the downstream effects of its enzymatic activity can provide insight into therapeutic targets and strategies. Current studies focus on characterizing the protein's enzymatic properties, its interaction with other glycosyltransferases, and its role in the overarching framework of glycosaminoglycan sulfation. Additionally, the development of HS3ST1 as a recombinant protein offers a valuable tool for high-throughput screening of potential inhibitors or modulators, which could pave the way for novel treatments in conditions linked to aberrant heparan sulfate biosynthesis. Overall, the exploration of HS3ST1 not only enhances our understanding of heparan sulfate biology but also opens avenues for innovative therapeutic interventions against various diseases.
