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Isoforms Recommended: HSP70
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Hsp70

" in MedChemExpress (MCE) Product Catalog:

44

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9

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7

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  • HY-P71824
    HSP70/DnaK Protein, E. coli (P.pastoris, His)

    dnaK; Hsp70; Heat shock 70kDa protein; Heat shock protein 70

    		 E.coli P. pastoris
    HSP70/DnaK protein, a molecular chaperone, responds primarily to stress, notably heat shock. It plays a crucial role in aiding the proper folding of proteins during cellular stress, preventing misfolding or aggregation. The chaperone activity is vital for cellular homeostasis and survival under adverse conditions, where maintaining correct protein conformation becomes challenging. HSP70/DnaK's ability to recognize and assist in refolding misfolded or denatured proteins is essential for cellular resilience, preventing proteotoxicity induced by stressors, especially elevated temperatures. HSP70/DnaK Protein, E. coli (P.pastoris, His) is the recombinant E. coli-derived HSP70/DnaK protein, expressed by P. pastoris, with N-6*His labeled tag. The total length of HSP70/DnaK Protein, E. coli (P.pastoris, His) is 638 a.a., with molecular weight of ~71.1 kDa.
  • 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.
  • HY-P73105
    HSP70/HSPA1B Protein, Human (SF9, His)

    Heat shock 70 kDa protein 1B; Hsp70-2; HspA1B; Hsp72

    		 Human Sf9 insect cells
    HSP70/HSPA1B protein, a vital molecular chaperone, ensures proteome integrity by protecting from stress, aiding protein folding, activating proteolysis, and regulating protein complex assembly. It maintains accurate folding through ATP cycles and co-chaperones like HSP40s, BAG1/2/3, HOPX, and STUB1. Its acetylation state modulates competitive binding with HOPX and STUB1, dictating roles in protein refolding and degradation during stress. Beyond protein homeostasis, HSP70 regulates centrosome integrity, influences SMAD3 and FOXP3 degradation, and acts as a post-attachment receptor in rotavirus A infection. HSP70/HSPA1B Protein, Human (SF9, His) is the recombinant human-derived HSP70/HSPA1B protein, expressed by Sf9 insect cells, with N-His labeled tag. The total length of HSP70/HSPA1B Protein, Human (SF9, His) is 640 a.a., with molecular weight of ~72.2 kDa.
  • HY-P701386
    HSPBP1 Protein, Human

    HspBP1; Hsp70-binding protein 1; HspBP1; Heat shock protein-binding protein 1; Hsp70-binding protein 2; HspBP2; Hsp70-interacting protein 1; Hsp70-interacting protein 2

    		 Human E. coli
    HSPBP1 protein regulates HSPA1A chaperone activity by inducing conformational changes in the ATP-binding domain and disrupting ATP binding. This interference inhibits the STUB1-mediated ubiquitination process and blocks chaperone-assisted degradation of immature CFTR. HSPBP1 Protein, Human is the recombinant human-derived HSPBP1 protein, expressed by E. coli , with tag free. The total length of HSPBP1 Protein, Human is 276 a.a., .
  • HY-P701387
    HSPBP1 Protein, Human (His)

    HspBP1; Hsp70-binding protein 1; HspBP1; Heat shock protein-binding protein 1; Hsp70-binding protein 2; HspBP2; Hsp70-interacting protein 1; Hsp70-interacting protein 2

    		 Human E. coli
    HSPBP1 protein regulates HSPA1A chaperone activity by inducing conformational changes in the ATP-binding domain and disrupting ATP binding. This interference inhibits the STUB1-mediated ubiquitination process and blocks chaperone-assisted degradation of immature CFTR. HSPBP1 Protein, Human (His) is the recombinant human-derived HSPBP1 protein, expressed by E. coli , with N-6*His labeled tag. The total length of HSPBP1 Protein, Human (His) is 276 a.a., .
  • HY-P701004
    HSP70/HSPA1A Protein, Human (E110D, His)

    Hsp70-1; HspA1A; Hsp72 ; HspA1; HSX70

    		 Human E. coli
    The HSP70/HSPA1A protein is an important molecular chaperone that protects proteome integrity by counteracting stress, aiding protein folding, activating misfolded proteolysis, and regulating protein complex dynamics. In protein quality control systems, it ensures accurate protein folding, controls substrate targeting for degradation through the ATP cycle, and interacts with co-chaperones such as HSP40, BAG1/2/3, HOPX, and STUB1. HSP70/HSPA1A Protein, Human (E110D, His) is the recombinant human-derived HSP70/HSPA1A protein, expressed by E. coli , with N-His labeled tag and E110D, , , , mutation. The total length of HSP70/HSPA1A Protein, Human (E110D, His) is 640 a.a., with molecular weight of 72.2 kDa.
  • HY-P74877
    HSP70/HSPA1A Protein, Human (HEK293, His)

    Heat shock 70 kDa protein 1A; Hsp70-1; HspA1A; Hsp72

    		 Human HEK293
    The HSP70/HSPA1A protein is an important molecular chaperone that protects proteome integrity by counteracting stress, aiding protein folding, activating misfolded proteolysis, and regulating protein complex dynamics. In protein quality control systems, it ensures accurate protein folding, controls substrate targeting for degradation through the ATP cycle, and interacts with co-chaperones such as HSP40, BAG1/2/3, HOPX, and STUB1. HSP70/HSPA1A Protein, Human (HEK293, His) is the recombinant human-derived HSP70/HSPA1A protein, expressed by HEK293 , with N-His labeled tag. The total length of HSP70/HSPA1A Protein, Human (HEK293, His) is 640 a.a., with molecular weight of ~85 kDa.
  • HY-P71340
    STUB1 Protein, Human

    E3 Ubiquitin-Protein Ligase CHIP; Antigen NY-CO-7; CLL-Associated Antigen KW-8; Carboxy Terminus of Hsp70-Interacting Protein; STIP1 Homology and U Box-Containing Protein 1; STUB1; CHIP

    		 Human E. coli
    STUB1 protein is an E3 ubiquitin protein ligase that cooperates with ATXN3 to regulate ubiquitin chain length on substrates and prevent chain extension. It ubiquitinates NOS1 through Hsp70/Hsp40 and regulates chaperone complexes (Hsp70, Hsc70, Hsp90). STUB1 Protein, Human is the recombinant human-derived STUB1 protein, expressed by E. coli , with tag free. The total length of STUB1 Protein, Human is 303 a.a., with molecular weight of ~33.0 kDa.

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