HSPA5/GRP-78 蛋白, Mouse (P.pastoris, His, solution)

HSPA5/GRP-78 Protein serves as a crucial endoplasmic reticulum chaperone, playing a pivotal role in protein folding and quality control within the endoplasmic reticulum lumen. It engages in correct protein folding and participates in the degradation of misfolded proteins, collaborating with DNAJC10/ERdj5 to facilitate the release of DNAJC10/ERdj5 from its substrate. Furthermore, HSPA5/GRP-78 acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, it is recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, disrupting the dimerization of ERN1/IRE1 and consequently inactivating it. The accumulation of misfolded proteins triggers the release of HSPA5/BiP from ERN1/IRE1, allowing for homodimerization and the subsequent activation of ERN1/IRE1. Additionally, HSPA5/GRP-78 plays an auxiliary role in the post-translational transport of small presecretory proteins across the endoplasmic reticulum and may function as an allosteric modulator for the SEC61 channel-forming translocon complex. It is suggested to cooperate with SEC62 to enable the productive insertion of these precursors into the SEC61 channel. The protein appears to specifically regulate the translocation of precursors with inhibitory residues in their mature region, which weaken channel gating. Beyond its role in protein folding, HSPA5/GRP-78 may also contribute to apoptosis and cell proliferation. HSPA5/GRP-78 Protein, Mouse (P.pastoris, His, solution) is the recombinant mouse-derived HSPA5/GRP-78 protein, expressed by P. pastoris , with N-His labeled tag. The total length of HSPA5/GRP-78 Protein, Mouse (P.pastoris, His, solution) is 636 a.a., with molecular weight of ~72.5 kDa.

HSPA5/GRP-78 蛋白作为重要的内质网伴侣，在内质网腔内的蛋白质折叠和质量控制中发挥着关键作用。它参与正确的蛋白质折叠并参与错误折叠蛋白质的降解，与 DNAJC10/ERdj5 合作促进 DNAJC10/ERdj5 从其底物中释放。此外，HSPA5/GRP-78 是 ERN1/IRE1 介导的未折叠蛋白反应 (UPR) 的关键抑制因子。在无应激的内质网中，它被 DNAJB9/ERdj4 招募到 ERN1/IRE1 的管腔区域，破坏 ERN1/IRE1 的二聚化，从而使其失活。错误折叠蛋白的积累会触发 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转运中发挥辅助作用，并且可能充当 SEC61 通道形成易位子复合物的变构调节剂。建议与 SEC62 合作，将这些前体高效地插入 SEC61 通道中。该蛋白质似乎特异性调节成熟区域中带有抑制残基的前体的易位，从而削弱了通道门控。除了在蛋白质折叠中的作用之外，HSPA5/GRP-78 还可能有助于细胞凋亡和细胞增殖。

The enzyme activity of this recombinant protein is testing in progress, we cannot offer a guarantee yet.

Mouse

P. pastoris

N-His

P20029(20E-655L)

14828  [NCBI]

EEEDKKEDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVVEKKTKPYIQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFFEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVLSGDQDTGDLVLLDVCPLTLGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEIDVNGILRVTAEDKGTGNKNKITITNDQNRLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDKEKLGGKLSSEDKETMEKAVEEKIEWLESHQDADIEDFKAKKKELEEIVQPIISKLYGSGGPPPTGEEDTSEKDEL

Approximately 72.5 kDa

Greater than 90 % as determined by SDS-PAGE.

溶液

Supplied as a 0.2 μm filtered solution of 20 mM Tris-HCl, 0.5M NaCl, pH 8.0, 50% glycerol.

<1 EU/μg, determined by LAL method.

N/A.

Stored at -80°C for 1 year. It is stable at -20°C for 3 months after opening. It is recommended to freeze aliquots at -80°C for extended storage. Avoid repeated freeze-thaw cycles.

Shipping with dry ice.