HSP70 Antibody

SKU:BHA11900001
—
Suppliers
StressMarq Biosciences Inc.
StressMarq Biosciences Inc.
Details Products
Overview
Click light‑blue chips for details
Mouse Anti-Human HSP70 Monoclonal IgG1
Target HSP70
Clone number C92F3A-5
Clonality Monoclonal
Application(s) WB, IHC, ICC/IF, ELISA, FCM, FACS, IEM, Bl, AM
Host Mouse
Options selector
Catalog no. Size Conjugate(s)
SMC-100B 200 ug
Available Options

Select the variant that best fits your experiment. Availability and lead time may vary by option.

  • Options: Size (1) — 200 ug; Conjugate(s) (10) — Unconjugated, ATTO 390, ATTO 488, ATTO594, APC, BI, FITC, HRP, PCP, RPE
  • Lead time: options listed as “in stock at manufacturer” typically ship in 2–3 business days; other statuses may take longer.
  • Storage: -20ºC, Conjugated antibodies should be stored according to the product label
  • Shipping: cold-chain shipment (typically with ice packs).
  • Upon receipt: store at the recommended temperature as soon as possible.
  • Sales terms and conditions: Please review prior to ordering.
Field Specification
Target HSP70
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
Accession number NP_005336.3
Host Mouse
Clone C92F3A-5
Clonality
  • Monoclonal
Isotype
  • IgG1
Reactivity
  • Human
  • Mouse
  • Rat
  • Bovine
  • C. elegans
  • Dog
  • Chicken
  • Drosophila
  • Carp
  • Guinea Pig
  • Hamster
  • Monkey
  • Pig
  • Rabbit
  • Sheep
Applications
  • Western Blot
  • Immunohistochemistry
  • Immunofluorescence
  • ELISA
  • Flow Cytometry
  • Calcium Imaging
Immunogen Human HSP70
Purification Protein G Purified
Cellular localization Cytoplasm
Concentration 1 mg/ml
Storage -20ºC, Conjugated antibodies should be stored according to the product label
Shipping Blue Ice or 4ºC
Catalog no. (Mfr.) SMC-100
Main SKU BHA11900001

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-100 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: HSP70 Antibody (StressMarq Biosciences | Victoria, BC CANADA, Catalog# SMC-100B, RRID: AB_854199)

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.

1. Welch W.J. and Suhan J.P. (1986) J Cell Biol. 103: 2035-2050.
2. Boorstein W. R., Ziegelhoffer T. & Craig E. A. (1993) J.Mol. Evol. 38(1): 1-17.
3. Rothman J. (1989) Cell 59: 591-601.
4. DeLuca-Flaherty et al. (1990) Cell 62: 875-887.
5. Bork P., Sander C. & Valencia A. (1992) Proc. Nut1 Acad. Sci. USA 89: 7290-7294.
6. Fink A.L. (1999) Physiol. Rev. 79: 425-449.
7. Galan A., et al. (2000) J. Biol. Chem. 275: 11418-11424.
8. Kondo T., et al. (2000) J. Biol. Chem. 275: 8872-8879.
9. Misaki T., et al. (1994) Clin. Exp. Immun. 98: 234-239.
10. Pockley A.G., et al. (1998) Immunol. Invest. 27: 367-377.
11. Moon I.S., et al. (2001) Cereb Cortex 11(3): 238-248.
12. Dressel et al. (2000) J. Immunol. 164: 2362-2371.
13. Verma A.K., et al. (2007) Fish and Shellfish Immunology. 22(5): 547-555.
14. Banduseela V.C., et al. (2009) Physiol Genomics. 39(3): 141-159.

Get a Quote

Please use this form for bulk quantity requests or customized products.

Contact Information

Product Information

Try Celltrypse Free – Request Your Sample Today

Experience the power of Celltrypse™, c-LEcta's innovative enzyme solution for gentle and efficient cell dissociation. Request your free sample and discover a superior alternative for your cell culture workflows.

Try Celltrypse Free – Request Your Sample Today

Try Celltrypse Free – Request Your Sample Today

Experience the power of Celltrypse™, c-LEcta's innovative enzyme solution for gentle and efficient cell dissociation. Request your free sample and discover a superior alternative for your cell culture workflows.

Try Celltrypse Free – Request Your Sample Today