Analytical Data
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基因名
VWA5B2
- Application
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别名
VWA5B2；von Willebrand factor A domain-containing Protein 5B2
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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
Q8N398
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表达区间
781-862aa
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氨基酸序列
PRKPSLGAILDGPSPEPGQQLGQGLDDSGNLLSPAPMDWDMLMEPPFLFTAVPPSGELAPPAVPPQAPRCHVVIRGLCGEQP
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分子量
24.6 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
The VWA5B2 protein, a member of the von Willebrand factor A (VWA) domain-containing proteins, has garnered significant attention in recent years due to its potential role in various biological processes and disease mechanisms. Initially identified as a gene linked to specific developmental and physiological functions, VWA5B2 has been implicated in cellular adhesion, migration, and signaling pathways. Research indicates that alterations in VWA5B2 expression may be associated with certain pathological conditions, including cancer progression and neurological disorders. The protein’s unique structural features, including its VWA domain, suggest a complex interaction network with other cellular components. As a result, recombinant expressions of VWA5B2 have been pursued to facilitate detailed studies on its functional roles and therapeutic potentials. Advances in recombinant DNA technology have enabled the production of this protein in various expression systems, allowing for biochemical characterization, functional assays, and structural analyses. Understanding VWA5B2’s mechanism of action could provide valuable insights into its role in health and disease, paving the way for potential therapeutic strategies targeting its functions. Enhanced knowledge about VWA5B2 may eventually contribute to the development of biomarkers for disease diagnosis and prognosis, as well as novel treatments for related disorders.
