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Results for "

BiP

" in MedChemExpress (MCE) Product Catalog:

12

Inhibitors & Agonists

5

Peptides

2

Natural
Products

4

Recombinant Proteins

2

Antibodies

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Cat. No. Compare Product Name Species Source
  • HY-P72239
    HSPA5/GRP-78 Protein, Human (His)

    Endoplasmic reticulum chaperone BiP; GRP-78; BiP; GRP78

    		 Human E. coli
    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.
  • HY-P7332
    BMP-3B/GDF10 Protein, Human (His)

    rHuBMP-3B; BiP; BMP-3B; GDF-10

    		 Human E. coli
    Bone morphogenetic protein 3 (BMP-3; GDF10) is a polymorphic ligand protein belonging to the TGF-β family. BMP-3 is the main component of osteoblast and has osteogenic activity. BMP-3 plays an inhibitory role in the carcinogenic process, and inhibits the occurrence of colon tumors through ActRIIB/ SMad2-dependent and TAK1/JNK signaling pathways. BMP-3B/GDF10 Protein, Human has a total length of 110 amino acids (Q369-R478), is expressed in E. coli cells.
  • HY-P71742
    HSPA5/GRP-78 Protein, Mouse (P.pastoris, His)

    Hspa5; Grp78; Endoplasmic reticulum chaperone BiP; EC 3.6.4.10; 78kDa glucose-regulated protein; GRP-78; HSP70 family protein 5

    		 Mouse P. pastoris
    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. The total length of HSPA5/GRP-78 Protein, Mouse (P.pastoris, His) is 636 a.a., with molecular weight of ~72.5 kDa.
  • HY-P71742Y
    HSPA5/GRP-78 Protein, Mouse (P.pastoris, His, solution)

    Hspa5; Grp78; Endoplasmic reticulum chaperone BiP; EC 3.6.4.10; 78kDa glucose-regulated protein; GRP-78; HSP70 family protein 5

    		 Mouse P. pastoris
    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.

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