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

The HSPA5/GRP-78 protein is an endoplasmic reticulum chaperone involved in protein folding and quality control. It interacts with DNAJC10/ERdj5 to fold and degrade misfolded proteins. HSPA5/GRP-78 Protein, Mouse (P.pastoris, His) is the recombinant mouse-derived HSPA5/GRP-78 protein, expressed by P. pastoris , with N-6*His, N-His labeled tag.

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.

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

Mouse

P. pastoris

N-6*His

P20029 (E20-L655)

14828  [NCBI]

Full Length of Mature Protein

EEEDKKEDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVVEKKTKPYIQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFFEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVLSGDQDTGDLVLLDVCPLTLGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEIDVNGILRVTAEDKGTGNKNKITITNDQNRLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDKEKLGGKLSSEDKETMEKAVEEKIEWLESHQDADIEDFKAKKKELEEIVQPIISKLYGSGGPPPTGEEDTSEKDEL

Approximately 72.5 kDa

≥ 90%, as determined by reducing SDS-PAGE.

Lyophilized powder.

Lyophilized from a 0.22 μm filtered solution of 20 mM Tris-HCl, 0.5 M NaCl, 6% trehalose, pH 8.0.
Note: For SPR assay, please replace the buffer. Primary amine components (e.g., Tris, imidazole) can affect protein-coupled chips.

<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 from date of receipt. 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.