Analytical Data
-
基因名
HSPA5/GRP-78
- Application
-
别名
MIF2; BIP; GRP78; Immunoglobulin heavy chain-binding protein; Glucose Regulated Protein 78; Binding Immunoglobulin Protein; Endoplasmic reticulum lumenal Ca binding grp78
-
种属
Mouse
-
表达系统
E. coli
-
标签
N- GST
-
纯度
Greater than 90% as determined by SDS-PAGE.
-
蛋白编号
P20029
-
表达区间
Glu20~Leu655
-
分子量
97kDa
-
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
HSPA5, also known as GRP78 (Glucose Regulated Protein 78), is a critical member of the heat shock protein family, primarily involved in the endoplasmic reticulum (ER) stress response and protein folding. It serves as a molecular chaperone, facilitating the correct folding of nascent proteins and preventing misfolded proteins from accumulating, which is essential for cellular homeostasis. Over the years, research has highlighted HSPA5's significant role in various physiological and pathological processes, including cancer, neurodegenerative diseases, and metabolic disorders. Its expression is often upregulated in response to ER stress, which can occur due to factors such as nutrient deprivation, oxidative stress, and hyperglycemia. As a result, HSPA5 is being investigated as a potential biomarker and therapeutic target, given its involvement in tumor progression and resistance to apoptosis. The recombinant expression of HSPA5/GRP78 has garnered interest not only for its potential diagnostic applications but also for therapeutic strategies aimed at enhancing cellular survival and resilience under stress conditions. Furthermore, recombinant forms of HSPA5 are being explored for their utility in vaccine development and as drug delivery systems, highlighting their versatility in biotechnological applications. Understanding the mechanistic pathways involving HSPA5/GRP78 could provide significant insights into designing novel therapies for diseases characterized by ER stress and protein misfolding, making it an essential focus for ongoing biomedical research.
