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Anti-mtHSP70 Mouse Antibody [F16K11]

Catalog No.: F3929

Application: Reactivity: Dog, Human, Mouse, Non-human primate

Usage Information

Dilution
WB1:500 IHC1:2000 IF1:50

Application
WB, IP, IHC, IF

Reactivity
Dog, Human, Mouse, Non-human primate

Source
Mouse

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

Predicted MW
70 kDa

Datasheet & SDS

Biological Description

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

Clone
F16K11

Synonym(s)
68 kDa heat shock protein; dnaK-type molecular chaperone HSP70-1; epididymis secretory protein Li 103; Heat shock 70 kDa protein 1; heat shock 70 kDa protein 1/2; Heat shock 70 kDa protein 1A; heat shock 70 kDa protein 1A/1B; Heat shock 70 kDa protein 1B

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.

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.

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

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

Tech Support

Answers to questions you may have can be found in the inhibitor handling instructions. Topics include how to prepare stock solutions, how to store inhibitors, and issues that need special attention for cell-based assays and animal experiments.

Handling Instructions

Tel: +1-832-582-8158 Ext:3
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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%