| Field | Specification |
|---|---|
| Mfr No | |
| Accession Number | |
| Alternative Names | HSPA1A, HSPA1B, HSPA1, HSP70, HSP70-1, HSP70.1, HSP70-2, HSP72, HSP73, HSX70, Heat shock 70 kDa protein 1A, Heat shock 70 kDa protein 1B |
| Cellular Localization | |
| Clonality | |
| Concentration | |
| Host | |
| Immunogen | Human recombinant HSP70 overexpressed in E.coli |
| Isotype | |
| Product Type | |
| Reactivity | |
| Shipping | |
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HSP70 proteins are a highly conserved family of 70-kDa molecular chaperones encoded by a multigene family in most eukaryotes and prokaryotes. Found in nearly all cellular compartments—including the cytosol, nucleus, mitochondria, endoplasmic reticulum, and chloroplasts—HSP70s are constitutively expressed and strongly upregulated in response to cellular stress.
These chaperones play a vital role in protein homeostasis by binding to nascent polypeptides and partially folded or misfolded proteins, preventing aggregation and facilitating proper folding. HSP70s exhibit high-affinity ATP binding and weak ATPase activity, which is stimulated upon interaction with unfolded substrates. ATP hydrolysis triggers conformational changes that regulate substrate binding and release, enabling dynamic cycles of protein folding and refolding.
Structurally, the N-terminal domain of HSP70 is responsible for ATP binding, while the C-terminal domain mediates substrate interaction. This modular design allows HSP70s to coordinate with co-chaperones such as HSP40, HIP, HOP, and BAG-1, integrating folding with degradation and transport pathways.
In neurodegenerative disease research, HSP70 is of particular interest due to its ability to counteract protein misfolding and aggregation—hallmarks of disorders like Alzheimer’s, Parkinson’s, and Huntington’s disease. By stabilizing toxic intermediates and promoting their clearance, HSP70 enhances neuronal survival and resilience under proteotoxic stress.
1 µg/ml of SMC-162 was sufficient for detection of HSP70 in 20 µg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.
Cite this product varies by variant:
- SMC-162D — Size: 100 ug: HSP70 Antibody (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-162D, RRID: AB_2119819)
- SMC-162D-A390 — Size: 100 ug: HSP70 Antibody: ATTO 390 (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-162D-A390, RRID: AB_2698602)
- SMC-162D-A488 — Size: 100 ug: HSP70 Antibody: ATTO 488 (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-162D-A488, RRID: AB_2698603)
- SMC-162D-A594 — Size: 100 ug: HSP70 Antibody: ATTO 594 (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-162D-A594, RRID: AB_2698605)
- SMC-162D-APC — Size: 100 ug: HSP70 Antibody: APC (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-162D-APC, RRID: AB_2698611)
- SMC-162D-BI — Size: 100 ug: HSP70 Antibody: Biotin (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-162D-BI, RRID: AB_2698612)
- SMC-162D-FITC — Size: 100 ug: HSP70 Antibody: FITC (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-162D-FITC, RRID: AB_2698613)
- SMC-162D-HRP — Size: 100 ug: HSP70 Antibody: HRP (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-162D-HRP, RRID: AB_2698614)
- SMC-162D-PCP — Size: 100 ug: HSP70 Antibody: PerCP (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-162D-PCP, RRID: AB_2698616)
- SMC-162D-RPE — Size: 100 ug: HSP70 Antibody: RPE (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-162D-RPE, RRID: AB_2698617)
- SMC-162S — Size: 12 ug: HSP70 Antibody (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-162S, RRID: AB_2119819)
Customization & Add-ons: Can’t find the antibody you need—or require a custom format for your assay? We can help you source the best match or support custom antibody solutions for diverse research needs, including species and isotype selection, conjugations and labeling (e.g., HRP/AP, biotin, fluorophores), purification grade options (Protein A/G, affinity purified), formulation preferences (buffer selection, carrier-free, glycerol-free), custom concentrations and aliquoting, low-endotoxin options for cell-based work, and application-focused QC/validation support (project dependent). Click Talk to a Scientist to submit a request, email us at support@biohippo.com, or explore our Research Services for additional support—our team will follow up with feasibility details and next steps.
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