Hsp70 Antibody (YA728)
(Synonyms: Heat shock 70 kDa protein 1-like, Heat shock 70 kDa protein 1L, Heat shock 70 kDa protein 1-Hom, Heat shock protein family A member 1L, HSP70-Hom, HSPA1L)Based on 1 Customer Validation
Hsp70 Antibody (YA728) is a Mouse-derived and non-conjugated monoclonal antibody, targeting to Hsp70.
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Host:
Mouse
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Application:
WB, IHC-P, ICC/IF
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Reactivity :
Human, Mouse, Rat
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Formulation:
Supplied in 1*PBS ( pH 7.4) and 50% Glycerol. Preservative: 0.02% sodium azide
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Conjugation:
Non-conjugated
Applications
| Application |
WB
WB: Western Blot
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ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
IHC-P
IHC-P: Immunohistochemistry-Paraffin
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|---|---|---|---|
| Dilution Ratio | 1:1000-1:2000 | 1:100-200 | 1:50-300 |
Product Details
Hsp70 Antibody (YA728) is a Mouse-derived and non-conjugated monoclonal antibody, targeting to Hsp70.
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Host Mouse
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Clonality Monoclonal
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Species ReactivityHuman, Mouse, Rat
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Observed Molecular WeightObserved band size: 70 kDaNote: 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
Entrez Gene: 15511 Human ; 3303 Human ; 193740 Mouse ; 3304 Mouse ; 24472 Rat 294254
SwissProt: P0DMV8 Human ; P0DMV9 Human ; P17879 Mouse ; Q61696 Mouse ; P0DMW0 Rat P0DMW1
OMIM: 140550 Human
Synthetic Peptide of HSP70
Endogenous
Immunogen affinity purified.
Non-conjugated
Unmodified
Product Properties
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Appearance
Solution
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Formulation
Supplied in 1*PBS ( pH 7.4) and 50% Glycerol. Preservative: 0.02% sodium azide
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Concentration
Batch-dependent, Please check the COA for the concentration of each lot. Check Lot Concentration
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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.
Verification Images
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Western blot analysis of extracts from A431 (lane2(20μg), HEK293 (lane3(20μg), Hela (lane4(20μg) and Jurkat (lane5(20μg) using Hsp70 Antibody (HY-P80412). Proteins were transferred to a PVDF membrane and blocked with 5% non-fat milk in TBST at 4°C overnight. The primary antibody (1/1000) and Loading control antibody (Beta Actin, HY-P80993, 1/10,000) was used in 5% non-fat milk in TBST for 2 hour at room temperature. Goat Anti-Mouse IgG-HRP Secondary Antibody (HY-P8004, 1/10,000) was used for 1 hour at room temperature.
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Immunocytochemistry analysis of HeLa cells labeling HSP70 Antibody (HY-P80412) at 1/50 dilution. Cells were fixed in 4% paraformaldehyde for 15 minutes at room temperature, permeabilized with 0.1% Triton X-100 for 10 minutes at room temperature, then blocked with BSA for Immunol Staining for 10 min at room temperature. Cells were then incubated with HSP70 Antibody (HY-P80412) at 1/50 dilution in BSA for Immunol Staining at 4 ℃overnight. AF488-conjugated AffiniPure Goat Anti-Mouse IgG H&L(HY-P8005, Green) was used as the secondary antibody at 1/1,000 dilution. PBS instead of the primary antibody was used as the secondary antibody only control. The Nuclear counterstain was DAPI (Blue).
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Immunocytochemistry analysis of NIH/3T3 cells labeling HSP70 Antibody (HY-P80412) at 1/50 dilution. Cells were fixed in 4% paraformaldehyde for 15 minutes at room temperature, permeabilized with 0.1% Triton X-100 for 10 minutes at room temperature, then blocked with BSA for Immunol Staining for 10 min at room temperature. Cells were then incubated with HSP70 Antibody (HY-P80412) at 1/50 dilution in BSA for Immunol Staining at 4 ℃overnight. AF488-conjugated AffiniPure Goat Anti-Mouse IgG H&L(HY-P8005, Green) was used as the secondary antibody at 1/1,000 dilution. PBS instead of the primary antibody was used as the secondary antibody only control. The Nuclear counterstain was DAPI (Blue).
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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Expression
Tissue_specificity:Expression in sperm cells
Induction:Not induced by heat shock -
Subunit
Interacts with PRKN
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SwissProt ID
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Synonyms
Heat shock 70 kDa protein 1-like, Heat shock 70 kDa protein 1L, Heat shock 70 kDa protein 1-Hom, Heat shock protein family A member 1L, HSP70-Hom, HSPA1L
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Research Field
Signal Transduction
Documentation
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Data Sheet (262 KB)
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SDS (252 KB)
- English - EN (252 KB)
- Français - FR (252 KB)
- Deutsch - DE (252 KB)
- Norwegian - NO (252 KB)
- Español - ES (252 KB)
- Swedish - SV (252 KB)
- Italian - IT (252 KB)
- Korean - KR (252 KB)
- Portuguese - PT (252 KB)
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User Guide for Antibodies (1077 KB)
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]