Application

Western Blotting Analysis: 1:500 dilution from a representative lot detected mtHsp70 in HeLa and U2OS cell lysates.

Immunocytochemistry Analysis: A representative lot detected mtHsp70 in Immunocytochemistry applications (Green, J.M., et. al. (1995). Hybridoma. 14(4):347-54; McCormick, A.L., et. al. (2005). J Virol. 79(19):12205-17).

Immunoprecipitation Analysis: A representative lot immunoprecipitated mtHsp70 in Immunoprecipitation applications (Green, J.M., et. al. (1995). Hybridoma. 14(4):347-54).

ELISA Analysis: A representative lot detected mtHsp70 in ELISA applications (Green, J.M., et. al. (1995). Hybridoma. 14(4):347-54).

Western Blotting Analysis: A representative lot detected mtHsp70 in Western Blotting applications (Green, J.M., et. al. (1995). Hybridoma. 14(4):347-54).

Research CategorySignaling

Anti-mtHsp70, clone JG1, Cat. No. MABS1955, is a mouse monoclonal antibody that detects Heat shock 70 kDa protein 1A and has been tested for use in ELISA, Immunocytochemistry, Immunoprecipitation, and Western Blotting.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

General description

Heat shock 70 kDa protein 1A (UniProt: Q61696; also known as Heat shock 70 kDa protein 3, HSP70.3, Hsp68, PBP74, Grp75) is encoded by the Hspa1a (also known as Hsp70-3, Hsp70A1) gene (Gene ID: 193740) in murine species. The 70-kDa heat shock protein (HSP70) is highly conserved, ubiquitous protein that functions as a molecular chaperone and helps in folding of newly synthesized or denatured proteins and in activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Heat shock 70 kDa protein 1A is localized in cytoplasmic mRNP granules containing untranslated mRNAs. It is acetylated at Lysine 77 by NA110 in response to cellular stress and then it is
gradually deacetylated by HDAC4 at later stages. Its acetylation enhances its chaperone activity and determines whether it will function as a chaperone for protein refolding or degradation by controlling its binding to co-chaperones HOPX and STUB1. The acetylated form and the non-acetylated form are shown to bind to HOPX and STUB1, respectively. It contains four ATP-binding regions and its N-terminal nucleotide binding domain (NBD; ATPase domain) is responsible for binding and hydrolyzing ATP. Its substrate binding domain (SBD) is localized to the C-terminal region. When ADP is bound in the NBD, a conformational change enhances the affinity of the SBD for client proteins. (Ref.: Green, JM et al. (1995). Hybridoma 14(4); 347-354).

Immunogen

A linear peptide corresponding to 19 amino acids from the C-terminal region of murine mtHSP70 and conjugated to amino acids 582-599 of Tetnus toxoid at its N-terminal.

Epitope: C-terminus

Other Notes

Concentration: Please refer to lot specific datasheet.

Physical form

Protein G purified

Purified mouse monoclonal antibody IgG3 in PBS without azide.

Format: Purified

Quality

Evaluated by Western Blotting in MCF7-10A cell lysate.

Western Blotting Analysis: 1:500 dilution of this antibody detected mtHsp70 in MCF7-10A cell lysate.

Specificity

Clone JG1 specifically detects Heat shock 70 kDa protein 1A (MtHSP70).

Storage and Stability

Stable for 1 year at -20°C from date of receipt. Handling Recommendations: Upon receipt and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.

Target description

~75 kDa observed; 70.08 kDa calculated. Uncharacterized bands may be observed in some lysate(s).