Analytical Data
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基因名
HSPB8
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简介
The HSPB8 protein exhibits temperature-dependent chaperone activity and functions as a monomer in its molecular form.It interacts with other cellular proteins to form complexes critical for cellular homeostasis.HSPB8 Protein, Human (His) is the recombinant human-derived HSPB8 protein, expressed by E.coli , with C-6*His labeled tag.
- Application
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别名
Heat shock protein beta-8; HspB8; Alpha-crystallin C chain; E2-induced gene 1 protein; Protein kinase H11; Small stress protein-like protein HSP22; HSPB8; CRYAC; E2IG1; HSP22
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种属
Human
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表达系统
E. coli
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标签
C-6*His
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纯度
Greater than 95% as determined by SDS-PAGE.
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蛋白编号
Q9UJY1
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表达区间
M1-T196
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氨基酸序列
MADGQMPFSCHYPSRLRRDPFRDSPLSSRLLDDGFGMDPFPDDLTASWPDWALPRLSSAWPGTLRSGMVPRGPTATARFGVPAEGRTPPPFPGEPWKVCVNVHSFKPEELMVKTKDGYVEVSGKHEEKQQEGGIVSKNFTKKIQLPAEVDPVTVFASLSPEGLLIIEAPQVPPYSTFGESSFNNELPQDSQEVTCT
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蛋白长度
Full Length
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分子量
23.0 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
HSPB8, a member of the small heat shock protein (sHSP) family, plays a critical role in cellular protection against stress-induced damage and protein misfolding, often associated with neurodegenerative diseases and various forms of cellular stress. Initially identified for its involvement in the cellular response to heat shock, HSPB8 has garnered attention for its functions in the regulation of proteostasis, aggregation of misfolded proteins, and facilitation of autophagy. Its chaperone-like activity, along with its capacity to interact with other proteins involved in cellular stress response pathways, positions HSPB8 as a potential therapeutic target for conditions such as Alzheimer's disease, amyotrophic lateral sclerosis, and other pathologies linked to protein misfolding. Recent studies have focused on the recombinant expression and purification of HSPB8 to clarify its molecular mechanisms and functional role in vivo and in vitro. By generating large quantities of pure HSPB8 protein, researchers aim to investigate its structural characteristics, interactions with client proteins, and its efficacy in modulating stress responses in cells. The findings from these studies contribute to a deeper understanding of the protein's role in neuroprotection and present opportunities for the development of novel therapeutic strategies that leverage HSPB8's protective properties against cellular stress and neurodegeneration. Overall, the exploration of HSPB8 recombinant protein serves as a pivotal step in unraveling its biological significance and its potential application in combating diseases characterized by protein aggregation and cellular stress.
