HSPA5/GRP-78 Protein, Human (P.pastoris, 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 (P.pastoris, His) is the recombinant human-derived HSPA5/GRP-78 protein, expressed by P. pastoris, with C-6*His labeled tag.

HSPA5/GRP-78, an endoplasmic reticulum chaperone, assumes a pivotal role in orchestrating protein folding and quality control within the endoplasmic reticulum lumen. Partnering with DNAJC10/ERdj5, it contributes to the proper folding of proteins and participates in the degradation of misfolded counterparts, potentially facilitating the release of DNAJC10/ERdj5 from its substrate. Functioning as a critical suppressor of the unfolded protein response (UPR) mediated by ERN1/IRE1, HSPA5/GRP-78 is recruited to the luminal region of ERN1/IRE1 by DNAJB9/ERdj4 under unstressed conditions, disrupting ERN1/IRE1 dimerization and thereby inactivating ERN1/IRE1. However, the accumulation of misfolded proteins prompts the release of HSPA5/BiP from ERN1/IRE1, allowing for homodimerization and subsequent activation of ERN1/IRE1. Additionally, HSPA5/GRP-78 serves as an auxiliary player in the post-translational transport of small presecretory proteins across the endoplasmic reticulum and is implicated in apoptosis, cell proliferation, and viral infection, acting as a cellular receptor for several flaviviruses, including Dengue virus, Zika virus, and Japanese encephalitis virus.

Human

P. pastoris

C-6*His

P11021 (E19-L654)

3309

Full Length of Mature Protein

EEEDKKEDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVVEKKTKPYIQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFYEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVLSGDQDTGDLVLLDVCPLTLGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEIDVNGILRVTAEDKGTGNKNKITITNDQNRLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDKEKLGGKLSSEDKETMEKAVEEKIEWLESHQDADIEDFKAKKKELEEIVQPIISKLYGSAGPPPTGEEDTAEKDEL

Approximately 66 kDa,based on SDS-PAGE under reducing conditions.

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.