1. Search Result
Search Result
Isoforms Recommended: HSP70
Results for "

Hsp70

" in MedChemExpress (MCE) Product Catalog:

52

Inhibitors & Agonists

3

Peptides

3

Natural
Products

12

Recombinant Proteins

2

Isotope-Labeled Compounds

7

Antibodies

1

Click Chemistry

Cat. No. Compare Product Name Species Source
  • HY-P71824

    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; 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; 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, 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

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

    Human Sf9 insect cells
    The HSP70/HSPA1B protein is an important molecular chaperone that ensures proteome integrity by protecting against stress, aiding in protein folding, activating proteolysis, and regulating protein complex assembly. It remains accurately folded through the ATP cycle and co-chaperones such as HSP40, BAG1/2/3, HOPX and STUB1. HSP70/HSPA1B Protein, Human (SF9, His) is the recombinant human-derived HSP70/HSPA1B protein, expressed by Sf9 insect cells , with N-His labeled tag.
  • HY-P701386

    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-P701004

    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

    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.
  • HY-P701387

    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-P703148

    Heat shock 70 kDa protein 1-like; Heat shock 70 kDa protein 1-Hom; Hsp70-Hom; Heat shock protein family A member 1L; HspA1L; Homo sapiens; Human; Heat shock 70 kDa protein 1L

    Human E. coli
  • HY-P703569

    GRP75; HspA9B; mt-Hsp70

    Human Sf9 insect cells
    CCR5 Protein, Human (Sf9, Flag, His) is the recombinant human-derived CCR5, expressed by Sf9 insect cells , with His, Flag labeled tag. ,
  • HY-P702943

    GRP75; HspA9B; mt-Hsp70; Mortalin Protein

    Human Sf9 insect cells
    HSPA9 protein, Human (sf9, GST) is the recombinant human-derived HSPA9, expressed by Sf9 insect cells , with GST labeled tag. The total length of HSPA9 protein, Human (sf9, GST) is 633 a.a.,
  • HY-P71340
    STUB1 Protein, Human
    2 Publications Verification

    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.

Inquiry Online

Your information is safe with us. * Required Fields.

Salutation

 

Country or Region *

Applicant Name *

 

Organization Name *

Department *

     

Email Address *

 

Product Name *

Cat. No.

 

Requested quantity *

Phone Number *

     

Remarks

Inquiry Online

Inquiry Information

Product Name:
Cat. No.:
Quantity:
MCE Japan Authorized Agent: