关键信息
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基因名
HSPA8
- 应用
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别名
MIR155HG;HSPA8-interacting micropeptide miPEP155
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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
P11142
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表达区间
1-646aa
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氨基酸序列
MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERL IGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGR PKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYF NDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDL GGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEFKRKHK KDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRA RFEELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLL QDFFNGKELNKSINPDEAVAYGAAVQAAILSGDKSENVQDLLLLDVTPLS LGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMT KDNNLLGKFELTGIPPAPRGVPQIEVTFDIDANGILNVSAVDKSTGKENK ITITNDKGRLSKEDIERMVQEAEKYKAEDEKQRDKVSSKNSLESYAFNMK ATVEDEKLQGKINDEDKQKILDKCNEIINWLDKNQTAEKEEFEHQQKELE KVCNPIITKLYQSAGGMPGGMPGGFPGGGAPPSGGASSGPTIEEVD
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分子量
72 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.
质检流程
相关产品
背景信息
HSPA8, also known as heat shock protein 70 (Hsp70), is a crucial molecular chaperone involved in protein folding, trafficking, and degradation within cells, playing a significant role in cellular stress response and homeostasis. The study of HSPA8 has gained prominence due to its implications in various cellular processes, including those related to neurodegenerative diseases, cancer, and infectious diseases. Given its essential role in maintaining protein integrity, researchers have focused on the molecular mechanisms that govern HSPA8's function and its interactions with other cellular components. Moreover, the ability to produce recombinant HSPA8 protein has facilitated detailed investigations into its biochemical properties and functional pathways. Understanding these aspects not only aids in elucidating the fundamental biology of HSPA8 but also opens avenues for therapeutic interventions targeting diseases where HSPA8 is implicated. With the advances in recombinant DNA technology, HSPA8 has become a model for studying chaperone-mediated protein transport and stress response mechanisms, further highlighting its potential as a biomarker and target for drug development in various pathological conditions. Hence, the ongoing research into HSPA8 provides critical insights into cellular mechanisms that could lead to the development of innovative therapeutic strategies.
