Analytical Data
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基因名
HSP27/HSPB1
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简介
The HSP27/HSPB1 protein is a small heat shock protein that acts as a molecular chaperone, possibly maintaining denatured proteins in a foldable state. In addition to its chaperone role, it crucially enhances stress resistance and contributes to actin organization. HSP27/HSPB1 Protein, Human (His) is the recombinant human-derived HSP27/HSPB1 protein, expressed by E. coli , with C-His labeled tag.
- Application
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别名
Heat shock protein beta-1; HspB1; HSP 27; SRP27; HSPB1; HSP28
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种属
Human
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表达系统
E. coli
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标签
C-His
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纯度
Greater than 95% as determined by SDS-PAGE.
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蛋白编号
P04792
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表达区间
M1-K205
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氨基酸序列
MTERRVPFSLLRGPSWDPFRDWYPHSRLFDQAFGLPRLPEEWSQWLGGSSWPGYVRPLPPAAIESPAVAAPAYSRALSRQLSSGVSEIRHTADRWRVSLDVNHFAPDELTVKTKDGVVEITGKHEERQDEHGYISRCFTRKYTLPPGVDPTQVSSSLSPEGTLTVEAPMPKLATQSNEITIPVTFESRAQLGGPEAAKSDETAAK
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蛋白长度
Full Length
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分子量
26-28 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
HSP27, also known as HSPB1, is a member of the small heat shock protein family and plays a crucial role in cellular stress responses, protein folding, and protection against apoptosis. It is widely expressed in various tissues and has been implicated in multiple cellular processes, including the regulation of cytoskeletal dynamics and the modulation of inflammatory responses. Due to its chaperone-like properties, HSP27 has garnered attention in cancer research, neurodegenerative diseases, and muscle disorders, where its expression levels often correlate with disease prognosis. Recombinant HSP27 protein is often produced for experimental studies to elucidate its functional mechanisms and interactions with other cellular proteins. The ability to generate recombinant HSP27 in a controlled manner allows researchers to dissect its roles in cellular signaling pathways, stress response mechanisms, and potential therapeutic applications. Understanding the structure-function relationships of HSP27 and its role in disease could pave the way for novel therapeutic strategies that harness its protective effects, making it a valuable target in biomedical research.
