Analytical Data
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基因名
HS3ST1
- Application
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别名
HS3ST1;3OST;3OST1;Heparan sulfate glucosamine 3-O-sulfotransferase 1
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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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
21-307aa
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氨基酸序列
MGSSHHHHHH SSGLVPRGSH MGSRPAELGQ QELLRKAGTL QDDVRDGVAP NGSAQQLPQT IIIGVRKGGT RALLEMLSLH PDVAAAENEV HFFDWEEHYS HGLGWYLSQM PFSWPHQLTV EKTPAYFTSP KVPERVYSMN PSIRLLLILR DPSERVLSDY TQVFYNHMQK HKPYPSIEEF LVRDGRLNVD YKALNRSLYH VHMQNWLRFF PLRHIHIVDG DRLIRDPFPE IQKVERFLKL SPQINASNFY FNKTKGFYCL RDSGRDRCLH ESKGRAHPQV DPKLLNKLHE YFHEPNKKFF ELVGRTFDWH
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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, or Heparan Sulfate 3-O-Sulfotransferase 1, is an essential enzyme involved in the biosynthesis of heparan sulfate (HS), a glycosaminoglycan that plays critical roles in various biological processes, including cell signaling, development, and tissue repair. HS3ST1 specifically adds sulfate groups to the 3-O position of certain glucosamine residues in heparan sulfate chains, influencing the binding and activity of numerous growth factors, cytokines, and morphogens. Dysregulation of HS synthesis, including anomalies in HS3ST1, has been implicated in various pathologies, such as cancer, inflammation, and congenital disorders, making it a significant target for therapeutic intervention. Recent studies have focused on the structural and functional characterization of HS3ST1, revealing its intricate mechanisms and the effects of specific mutations on its activity. Understanding HS3ST1's role in heparan sulfate modification provides insights into its involvement in disease processes and highlights its potential as a biomarker and therapeutic target. This research is crucial for developing strategies to manipulate HS pathways for therapeutic purposes, with the aim of improving treatment outcomes in diseases associated with aberrant HS signaling.
