Analytical Data
-
基因名
HSPA1B
- Application
-
别名
HSPA1B；HSP72；Heat shock 70 kDa Protein 1B
-
种属
Human
-
表达系统
E. coli
-
标签
His tag N-Terminus
-
纯度
Greater than 90% as determined by SDS-PAGE.
-
蛋白编号
P0DMV9
-
表达区间
1-641aa
-
氨基酸序列
MAKAAAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQSDMKHWPFQVINDGDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNKSINPDEAVAYGAAVQAAILMGDKSENVQDLLLLDVAPLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFDIDANGILNVTATDKSTGKANKITITNDKGRLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSAVEDEGLKGKISEADKKKVLDKCQEVISWLDANTLAEKDEFEHKRKELEQVCNPIISGLYQGAGGPGPGGFGAQGPKGGSGSGPTIEEVD
-
分子量
70 kDa
-
内毒素
< 1.0 EU per μg protein as determined by the LAL method.
-
性状
Freeze-dried powder
-
缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
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
-
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.
-
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.
-
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
Related Products
Protein Description
HSPA1B, a member of the heat shock protein 70 (HSP70) family, plays a crucial role in cellular stress responses and protein homeostasis. It is involved in the folding, stabilization, and transport of proteins, making it integral to various cellular processes, including apoptosis, cell cycle regulation, and immune responses. Research has shown that HSPA1B is upregulated in response to stressors such as heat shock, oxidative damage, and inflammation, indicating its protective functions in maintaining cellular integrity. Its expression is also linked to several pathophysiological conditions, including cancer, neurodegenerative diseases, and autoimmune disorders, suggesting that HSPA1B may serve as a biomarker for disease progression or a potential therapeutic target. In recent studies, the recombinant expression of HSPA1B has been pursued to elucidate its functional roles and interactions with other cellular components. By producing HSPA1B as a recombinant protein, researchers can perform biochemical assays, structural studies, and therapeutic applications, enhancing our understanding of its mechanism and exploring its potential in clinical settings. These efforts aim to harness HSPA1B's properties for innovative treatment strategies, thereby highlighting its significance in both basic and translational research.
