HSP70 Protein

Human Recombinant HSP70 Protein

Product Specifications

Background

HSP70 is a highly inducible molecular chaperone that plays a pivotal role in protein quality control across all major cellular compartments. In the brain, HSP70 is essential for preventing the aggregation of misfolded proteins, a key pathological feature of neurodegenerative diseases. HSP70 binds to nascent and partially folded polypeptides, stabilizing them and facilitating proper folding or directing them toward degradation pathways. This function is particularly critical in conditions such as Alzheimer’s, Parkinson’s, and ALS, where protein aggregation and impaired proteostasis drive neuronal dysfunction and cell death. The chaperone activity of HSP70 is regulated by ATP binding and hydrolysis, which triggers conformational changes that control substrate binding and release. Its ability to recognize hydrophobic regions of unfolded proteins enables it to suppress aggregation and promote cellular recovery from stress. Therapeutic strategies aimed at enhancing HSP70 expression or activity are under investigation for their potential to reduce neurotoxicity, improve protein clearance, and slow disease progression in neurodegenerative disorders.

Product Name Alternative

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

UNSPSC

12352202

UN Code

Non-hazardous

Hazard Statement

Non-hazardous

Gene ID

3303

Swiss Prot

P0DMV8/P0DMV9

Accession Number

NM_005345

Cellular Locus

Cytoplasm

Expression System

Baculovirus/Sf9

Host

Baculovirus/Sf9 cells

Origin Species

Human

Target

HSP70

Conjugation

His tag

Nature

Recombinant

Sequence

MAKAAAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQSDMKHWPFQVINDGDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNKSINPDEAVAYGAAVQAAILMGDKSENVQDLLLLDVAPLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFDIDANGILNVTATDKSTGKANKITITNDKGRLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSAVEDEGLKGKISEADKKKVLDKCQEVISWLDANTLAEKDEFEHKRKELEQVCNPIISGLYQGAGGPGPGGFGAQGPKGGSGSGPTIEEVD

Applications

WB | SDS-PAGE | ATPase Activity Assay | Functional Assay | ELISA

Field of Research

Purification Method

Affinity Purified | Endotoxin-free

Purification

Affinity Purified | Endotoxin-free

Limit Of Detection

This product has been certified >90% pure using SDS-PAGE analysis. The protein tested positive for ATPase activity using a Malachite Green assay.

Concentration

Lot/batch specific. See included datasheet.

Purity

>90%

Activity

ATPase active

Weight

0.1

Buffer

50mM Tris/HCl, pH 7.5, 0.15M NaCl, 10% glycerol

Molecular Weight

~70 kDa

Precautions

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

References & Citations

1. Zho J. (1998) Cell. 94: 471-480. 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. Natl Acad. Sci. USA. 89: 7290-7294. 6. Fink A.L. (1999) Physiol. Rev. 79: 425-449. 7. Smith D.F., et al., (1993) Mol. Cell. Biol. 13(2): 869-876. 8. Prapapanich V., et al., (1996) Mol. Cell. Biol. 16(11): 6200-6207. 9. Fernandez-Funez et al., (2000) Nature. 408(6808): 101-106.

Shipping Conditions

Blue Ice or 4ºC

Storage Conditions

-20ºC

Background Reference 01

1. Zho J. (1998) Cell. 94: 471-480. 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. Natl Acad. Sci. USA. 89: 7290-7294. 6. Fink A.L. (1999) Physiol. Rev. 79: 425-449. 7. Smith D.F., et al., (1993) Mol. Cell. Biol. 13 (2) : 869-876. 8. Prapapanich V., et al., (1996) Mol. Cell. Biol. 16 (11) : 6200-6207. 9. Fernandez-Funez et al., (2000) Nature. 408 (6808) : 101-106.