Hsp70 Antibody (YA6281)
(Synonyms: HSPA1A; HSPA1; HSPA1B; Heat shock 70 kDa protein 1A/1B; Heat shock 70 kDa protein 1/2; HSP70-1/HSP70-2; HSP70.1/HSP70.2)Hsp70 Antibody (YA6281) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to Hsp70.
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Host:
Rabbit
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Isotype:
IgG
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Application:
WB, IHC-P, ICC/IF, IP, ELISA
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Reactivity :
Human, Mouse, Rat
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Formulation:
Supplied in PBS, 50% glycerol, 0.05% Proclin 300, 0.05%BSA
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Conjugation:
Non-conjugated
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
Applications
| Application |
IHC-P
IHC-P: Immunohistochemistry-Paraffin
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WB
WB: Western Blot
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ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
ELISA
ELISA: Enzyme Linked Immunosorbent Assay
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IP
IP: Immunoprecipitation
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|---|---|---|---|---|---|
| Dilution Ratio | 1:400-1000 | 1:1000-5000 | 1:200-1000 | 1:5000-20000 | 1:50-200 |
Product Details
Hsp70 Antibody (YA6281) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to Hsp70.
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Host Rabbit
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Clonality Monoclonal
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Species ReactivityHuman, Mouse, Rat
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Observed Molecular WeightObserved band size: 70 kDa
Note: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 70 kDa
Protein A
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS, 50% glycerol, 0.05% Proclin 300, 0.05%BSA
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
HSP70 (Heat Shock Protein 70) is a highly conserved ATP-dependent molecular chaperone that maintains proteostasis by promoting protein folding, preventing aggregation of misfolded proteins, facilitating protein complex remodeling, and supporting protein translocation across cellular membranes[1][2]. Mechanistically, HSP70 functions through an ATP-regulated chaperone cycle in which substrate recognition, ATP hydrolysis, and co-chaperone interactions determine whether client proteins are refolded or directed toward degradation pathways[1]. This central role links HSP70 to cellular stress adaptation, because its expression increases in response to environmental and physiological stressors and helps preserve protein homeostasis under conditions that promote protein damage[3][4]. In disease models, impaired proteostasis and reduced chaperone capacity are associated with the accumulation of toxic misfolded proteins, whereas enhanced HSP70 activity has been linked to reduced protein aggregation, inflammation, and neuronal loss in neurodegenerative disorders including Alzheimer’s disease, Parkinson’s disease, Huntington’s disease, and amyotrophic lateral sclerosis[5]. Compared with related heat shock protein families such as HSP90, HSP70 is distinguished by its direct engagement with unfolded polypeptides and its prominent role in determining protein refolding versus degradation outcomes through co-chaperone-dependent quality-control mechanisms[1]. For experimental applications, HSP70 has become an important therapeutic research target, and both pharmacological modulators and recombinant HSP70-based approaches are widely investigated to manipulate proteostasis, cytoprotection, and stress-response pathways in models of neurodegenerative, inflammatory, and other protein-misfolding-associated diseases[1][6].
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Subcellular Localization
P0DMV8: Cytoplasm; Nucleus; Cytoplasm, cytoskeleton, microtubule organizing center, centrosome; Secreted
P0DMV9: Cytoplasm; Cytoplasm, cytoskeleton, microtubule organizing center, centrosome -
Expression
Tissue_specificity: P0DMV9: HSPA1B is testis-specific
Induction: P0DMV8: By heat shock
P0DMV9: By heat shock -
Isoforms & Post-Translational Modification
P0DMV8 has 2 isomers: P0DMV8-1: 70052 Da (predicted); P0DMV8-2: 63937 Da (predicted).
In response to cellular stress, acetylated at Lys-77 by NA110 and then gradually deacetylated by HDAC4 at later stages. Acetylation enhances its chaperone activity and also 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 bind to HOPX and STUB1 respectively. Acetylation also protects cells against various types of cellular stress -
Subunit
P0DMV8: Component of the CatSper complex. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs (PubMed:17289661). Interacts with CHCHD3, DNAJC7, IRAK1BP1, PPP5C and TSC2 (PubMed:12853476, PubMed:15383005, PubMed:15963462, PubMed:17233114, PubMed:18620420, PubMed:21081504).
P0DMV9: May be an auxiliary component of the CatSper complex. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs (PubMed:17289661). -
Synonyms
HSPA1A; HSPA1; HSPA1B; Heat shock 70 kDa protein 1A/1B; Heat shock 70 kDa protein 1/2; HSP70-1/HSP70-2; HSP70.1/HSP70.2
Documentation
References
[1]. Evans CG, et al. Heat shock protein 70 (hsp70) as an emerging drug target. J Med Chem. 2010 Jun 24;53(12):4585-602. [Content Brief]
[2]. Nguyen B, et al. Thermodynamic Bounds on the Ultra- and Infra-affinity of Hsp70 for Its Substrates. Biophys J. 2017 Jul 25;113(2):362-370. [Content Brief]
[3]. Singh MK, et al. Heat Shock Response and Heat Shock Proteins: Current Understanding and Future Opportunities in Human Diseases. Int J Mol Sci. 2024 Apr 10;25(8):4209. [Content Brief]
[5]. Ben Khalaf N. Heat shock proteins (Hsp70 and Hsp90) in neurodegeneration: pathogenic roles and therapeutic potential. Front Aging Neurosci. 2026 Feb 12;18:1711422. [Content Brief]
[6]. Evgen'ev MB, et al. The Role of Hsp70 in Adaptation to Adverse Conditions and Its Possible Medical Application. Front Biosci (Landmark Ed). 2023 Feb 8;28(2):25. [Content Brief]
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