HSP70 Antibody, Clone 7FB

Rat Anti-Drosophila HSP70 Monoclonal IgG2B

Product Specifications

Background

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.

CAS Number

9007-83-4

Specifications

Detects ~70kDa (heat-inducible form).

Product Name Alternative

Hsp70Bb, Major heat shock 70 kDa protein Bb, Heat shock protein 70Bb, HSP70-87C1, CG31359, GroEL homolog, dHSP70, HSP70b, HSP70B, Dm-HSP70

Synonyms

HSP70 Antibody, Clone 7FB

UNSPSC

12352203

UN Code

Non-hazardous

Hazard Statement

Non-hazardous

Gene ID

48582

Swiss Prot

Q9BIS2

Accession Number

NP_524927.2

Host

Rat

Species Reactivity

Drosophila

Immunogen

Prepared from Drosophila tissue culture cells heat shocked at 36.5◦C for 3 hours, and isolated using SDS PAGE.

Target

HSP70

Clonality

Monoclonal

Isotype

IgG2B

Clone

7FB

Conjugation

Unconjugated

Type

Monoclonal

Applications

WB | ICC/IF | ELISA

Validated Applications

WB,ICC/IF,ELISA

Field of Research

Purification

Protein G Purified

Limit Of Detection

1 µg/ml of SMC-230 was sufficient for detection of Drosophila HSP70 using an indirect assay with rabbit anti-rat IgG and goat anti-rabbit IgG:HRP.

Concentration

1 mg/ml

Dilution

WB (1:2000) ; optimal dilutions for assays should be determined by the user.

Weight

0.1

Buffer

PBS pH7.4, 50% glycerol, 0.1% sodium azide *Storage buffer changes when conjugated

Precautions

Not for use in humans. Not for use in diagnostics or therapeutics. For in vitro research use only.

References & Citations

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.

Shipping Conditions

Blue Ice or 4ºC

Storage Conditions

-20ºC

Specificity

Detects ~70kDa (heat-inducible form) .

Background Reference 01

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.