HSPA5/GRP-78 蛋白, Human (His)

HSPA5/GRP-78 is an endoplasmic reticulum chaperone that coordinates protein folding and quality control. It cooperates with DNAJC10/ERdj5 to facilitate correct protein folding and participates in the degradation of misfolded proteins, potentially releasing DNAJC10/ERdj5. HSPA5/GRP-78 Protein, Human (His) is the recombinant human-derived HSPA5/GRP-78 protein, expressed by E. coli , with N-6*His labeled tag. The total length of HSPA5/GRP-78 Protein, Human (His) is 269 a.a., with molecular weight of ~33.6 kDa.

HSPA5/GRP-78 是一种内质网伴侣，在内质网腔内协调蛋白质折叠和质量控制方面发挥着关键作用。它与 DNAJC10/ERdj5 配合，有助于蛋白质的正确折叠，并参与错误折叠对应物的降解，可能促进 DNAJC10/ERdj5 从其底物中释放。作为 ERN1/IRE1 介导的未折叠蛋白反应 (UPR) 的关键抑制因子，HSPA5/GRP-78 在无应激条件下被 DNAJB9/ERdj4 招募到 ERN1/IRE1 的管腔区域，破坏 ERN1/IRE1 二聚化，从而失活ERN1/IRE1。然而，错误折叠蛋白的积累促使 ERN1/IRE1 释放 HSPA5/BiP，从而实现同二聚化并随后激活 ERN1/IRE1。此外，HSPA5/GRP-78 在小前分泌蛋白跨内质网的翻译后运输中充当辅助角色，并与细胞凋亡、细胞增殖和病毒感染有关，充当多种黄病毒（包括登革热病毒）的细胞受体病毒、寨卡病毒和日本脑炎病毒。

HSPA5 has ATPase activity at the time of manufacture of 34.421 µM phosphate liberated/hr/µg protein in a 200 µL reaction at 37°C (pH7.5) in the presence of 10 μL of 4 mM ATP, using a Malachite Green assay.

Human

E. coli

N-6*His

P11021 (E25-E293)

3309  [NCBI]

EDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVVEKKTKPYIQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRREVE

Approximately 33.6 kDa

Greater than 95% as determined by reducing SDS-PAGE.

无菌粉末.

Lyophilized from a 0.2 μm solution of PBS, 6% Trehalose, pH 7.4.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.