Analytical Data
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基因名
HS3ST4
- Application
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别名
HS3ST4; 3OST4Heparan sulfate glucosamine 3-O-sulfotransferase 4; EC 2.8.2.23; Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 4; 3-OST-4; Heparan sulfate 3-O-sulfotransferase 4; h3-OST-4
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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
Q9Y661
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表达区间
1-456aa
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氨基酸序列
MARWPAPPPPPPPPPPLAAPPPPGASAKGPPARKLLFMCTLSLSVTYLCYSLLGGSGSLQFPLALQESPGAAAEPPPSPPPPSLLPTPVRLGAPSQPPAPPPLDNASHGEPPEPPEQPAAPGTDGWGLPSGGGGAQDAWLRTPLAPSEMITAQSALPEREAQESSTTDEDLAGRRAANGSSERGGAVSTPDYGEKKLPQALIIGVKKGGTRALLEAIRVHPDVRAVGVEPHFFDRNYEKGLEWYRNVMPKTLDGQITMEKTPSYFVTNEAPKRIHSMAKDIKLIVVVRNPVTRAISDYTQTLSKKPEIPTFEVLAFKNRTLGLIDASWSAIRIGIYALHLENWLQYFPLSQILFVSGERLIVDPAGEMAKVQDFLGLKRVVTEKHFYFNKTKGFPCLKKPEDSSAPRCLGKSKGRTHPRIDPDVIHRLRKFYKPFNLMFYQMTGQDFQWEQEEGDK
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分子量
49.7 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
HS3ST4 (Heparan Sulfate 3-O-Sulfotransferase 4) is an enzyme that plays a crucial role in the biosynthesis of heparan sulfate, a key glycosaminoglycan widely present on cell surfaces and in the extracellular matrix. Its primary function involves the 3-O-sulfation of glucosamine residues in heparan sulfate chains, a modification that significantly influences the biological activities of the resulting polysaccharides. Research on HS3ST4 has gained momentum due to its implications in various physiological and pathological processes, including cell signaling, development, and disease progression, particularly in cancer and viral infections. Aberrant expression or activity of HS3ST4 is associated with altered heparan sulfate structure, which can affect cell proliferation, migration, and the tumor microenvironment. Understanding the mechanistic details of HS3ST4's activity and its role in heparan sulfate modification is critical for elucidating its functions in health and disease. Furthermore, HS3ST4 represents a potential therapeutic target and biomarker, prompting investigations into its structure-function relationships and the development of specific inhibitors or modulators. This research aims to uncover new avenues for therapeutic interventions in diseases characterized by dysregulated heparan sulfate modifications. By studying HS3ST4 and its role in heparan sulfate biosynthesis, researchers seek to enhance our understanding of cellular communication and pathophysiological mechanisms, ultimately leading to novel strategies for disease management.
