Datasheet

Biological Description

Specificity	Anti-mtHSP70 Mouse Antibody [F16K11] recognizes total endogenous levels of mtHSP70 protein.
Background	Heat shock proteins (HSPs) are highly conserved and universally expressed molecular chaperones found in both prokaryotes and eukaryotes. They are central to maintaining proteostasis and safeguarding cells under stress conditions. HSPs are categorized primarily by molecular weight into large HSPs, HSP90, HSP70, HSP60, HSP40, and small HSPs. Acting as an interconnected chaperone network, they facilitate the folding of nascent polypeptides, refolding of unstable proteins, assembly and disassembly of protein complexes, prevention of aggregation, and degradation of misfolded proteins. Beyond their canonical chaperone roles, HSPs are also critical regulators of signal transduction, cell cycle progression, and apoptosis, linking their dysfunction to a variety of diseases such as cancer, neurodegenerative disorders, and other pathologies. Functionally, HSP families operate as holdases, foldases, sequestrases, aggregases, or disaggregases, providing a robust first line of defense against proteotoxic stress and supporting the entire metabolic cycle of proteins. HSP70 family members are expressed across multiple cellular compartments, including the cytosol, nucleus, endoplasmic reticulum (ER), mitochondria, and extracellular space, where they sustain the balance of protein synthesis, folding, degradation, and trafficking. Within mitochondria, mtHSP70 plays a pivotal role in protein import. Since preproteins must traverse mitochondrial membranes in an unfolded conformation, mtHSP70—together with other inner membrane components—mediates their unfolding and assists in their translocation into the mitochondrial matrix.

Specificity

Anti-mtHSP70 Mouse Antibody [F16K11] recognizes total endogenous levels of mtHSP70 protein.

Background

Heat shock proteins (HSPs) are highly conserved and universally expressed molecular chaperones found in both prokaryotes and eukaryotes. They are central to maintaining proteostasis and safeguarding cells under stress conditions. HSPs are categorized primarily by molecular weight into large HSPs, HSP90, HSP70, HSP60, HSP40, and small HSPs. Acting as an interconnected chaperone network, they facilitate the folding of nascent polypeptides, refolding of unstable proteins, assembly and disassembly of protein complexes, prevention of aggregation, and degradation of misfolded proteins. Beyond their canonical chaperone roles, HSPs are also critical regulators of signal transduction, cell cycle progression, and apoptosis, linking their dysfunction to a variety of diseases such as cancer, neurodegenerative disorders, and other pathologies. Functionally, HSP families operate as holdases, foldases, sequestrases, aggregases, or disaggregases, providing a robust first line of defense against proteotoxic stress and supporting the entire metabolic cycle of proteins. HSP70 family members are expressed across multiple cellular compartments, including the cytosol, nucleus, endoplasmic reticulum (ER), mitochondria, and extracellular space, where they sustain the balance of protein synthesis, folding, degradation, and trafficking. Within mitochondria, mtHSP70 plays a pivotal role in protein import. Since preproteins must traverse mitochondrial membranes in an unfolded conformation, mtHSP70—together with other inner membrane components—mediates their unfolding and assists in their translocation into the mitochondrial matrix.

Usage Information

Application

WB, IP, IHC, IF

Dilution

WB	IHC	IF
1:500	1:2000	1:50

Reactivity

Dog, Human, Mouse, Non-human primate

Source

Mouse

MW

70 kDa

Storage Buffer

PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage
(from the date of receipt)

-20°C (avoid freeze-thaw cycles), 2 years

Exprimental Methods

References

https://pubmed.ncbi.nlm.nih.gov/35928554/

Anti-mtHSP70 Mouse Antibody [F16K11]

Biological Description

Usage Information

References

Application Data