Replaces Prod. #: ALX-201-214
Product Details
| Alternative Name: | Heat shock protein 70, HspA1A, HspA1B, HSP72 |
| |
| MW: | ~72kDa |
| |
| Source: | Produced in E. coli. |
| |
| UniProt ID: | P0DMV8 (HSPA1A), P0DMV9 (HSPA1B) |
| |
| GenBank ID: | M11717 |
| |
| Gene/Protein Identifier: | NP_005336.3 (RefSeq), NM_005345 (RefSeq), 3303 (Entrez GeneID), 140550 (OMIM) |
| |
| Formulation: | Liquid. In Dulbecco's PBS. |
| |
| Purity: | ≥90% (SDS-PAGE; Western blot) |
| |
| Purity Detail: | Purified by multi-step chromatography. |
| |
| Endotoxin Content: | <50EU/mg purified protein (LAL test) |
| |
| Applications: | ELISA, WB
Activity assay, in vitro Assay
|
| |
| Application Notes: | ATPase activity assay (positive). Western blot control. |
| |
| Shipping: | Dry Ice |
| |
| Long Term Storage: | -80°C |
| |
| Scientific Background: | The Hsp70 family of heat shock protiens contains multiple homologs ranging in size from 66-78 kDa, and are the eukaryotic equivalents of the bacterial DnaK. The most studied Hsp70 members include the cytosolic stress-induced Hsp70 (Hsp72), the constitutive cytosolic Hsc70 (Hsp73), and the ER-localized BiP (Grp78). Hsp70 family members contain highly conserved N-terminal ATP-ase and C-terminal protein binding domains. Binding of peptide to Hsp70 is assisted by Hsp40, and stimulates the inherent ATPase activity of Hsp70, facilitating ATP hydrolysis and enhanced peptide binding. Hsp70 nucleotide exchange and substrate binding coordinates the folding of newly synthesized proteins, the re-folding of misfolded or denatured proteins, coordinates trafficking of proteins across cellular membranes, inhibits protein aggregation, and targets the degradation of proteins via the proteasomal pathway. |
| |
| Regulatory Status: | RUO - Research Use Only |
| |
SDS-PAGE analysis of HSP70 (low endotoxin) (human), (recombinant): Lane 1: MW marker, Lane 2: 1µg, Lane 3: 2µg, Lane 4: 5µg HSP70.
Western Blot Analysis of HSP70 (low endotoxin) (human), (recombinant): Left blot probed with HSP70 mAb (Prod. No. ADI-SPA-810) - Lane 1: MW Marker, Lane 2: HeLa lysate (Prod. No. ADI-LYC-HL100), Lane 3: Heat-shocked HeLa lysate (Prod. No. ADI-LYC-HL101), Lane 4: HSP70. Right blot probed with DnaK mAb (Prod. No. ADI-SPA-880) - Lane 5: MW Marker, Lane 6: DnaK (Prod. No. ADI-SPP-630), Lane 7: HSP70.
Please mouse over
Product Literature References
The effect of temperature and heat shock protein 72 on the ex vivo acute inflammatory response in monocytes: S.P. Hoekstra, et al.; Cell Stress Chaperones
24, 461 (2019),
Application(s): experimental treatement- human male blood,
Abstract;
Cardioprotection mediated by exosomes is impaired in the setting of type II diabetes but can be rescued by the use of non‐diabetic exosomes in vitro: S.M. Davidson, et al.; J. Cell. Mol. Med.
22, 141 (2018),
Abstract;
Full Text
Extracellular Hsp70 induces inflammation and modulates LPS/LTA-stimulated inflammatory response in THP-1 cells: A. Hulina, et al.; Cell Stress Chaperones
23, 373 (2018),
Application(s): Immune and inflammatory response assays using THP-1 cells,
Abstract;
Molecular AFM imaging of Hsp70-1A association with dipalmitoyl phosphatidylserine reveals membrane blebbing in the presence of cholesterol: C. Lamprecht, et al.; Cell Stress Chaperones
23, 673 (2018),
Abstract;
Heat shock protein 70 potentiates interferon alpha production by plasmacytoid dendritic cells: relevance for cutaneous lupus and vitiligo pathogenesis: C. Jacquemin, et al.; Br. J. Dermatol.
177, 1367 (2017),
Abstract;
Bacterial Hsp70 (DnaK) and mammalian Hsp70 interact differently with lipid membranes: V. Lopez, et al.; Cell Stress Chaperones
21, 609 (2016),
Abstract;
Full Text
The Molecular Chaperone Hsp70 Promotes the Proteolytic Removal of Oxidatively Damaged Proteins by the Proteasome: S. Reeg, et al.; Free Radic. Biol. Med.
99, 153 (2016),
Application(s): Proteasomal degradation of oxidized actin,
Abstract;
Differential expression patterns among heat-shock protein genes and thermal responses in the whitefly Bemisia tabaci (MEAM 1): F. Diaz, et al.; J. Therm. Biol.
52, 199 (2015),
Abstract;
Role of exogenous Hsp72 on liver dysfunction during sepsis: T.N. Tsai, et al.; BioMed Res. Int.
2015, 508101 (2015),
Application(s): Subcutaneous injection in rat,
Abstract;
Full Text
Interaction of heat shock protein 70 with membranes depends on the lipid environment: G. Armijo, et al.; Cell Stress Chaperones
19, 877 (2014),
Abstract;
Mutations in the substrate binding site of human heat-shock protein 70 indicate specific interaction with HLA-DR outside the peptide binding groove: K.M. Rohrer, et al.; Immunology
142, 237 (2014),
Abstract;
Full Text
Putative role of protein kinase C in neurotoxic inflammation mediated by extracellular heat shock protein 70 after ischemia-reperfusion: G. Dvoriantchikova, et al.; J. Neuroinflammation
11, 81 (2014),
Abstract;
Full Text
Stimulation of TLR4 by recombinant HSP70 requires structural integrity of the HSP70 protein itself: M. Luong, et al.; J. Inflamm. (Lond.)
9, 11 (2012),
Abstract;
Full Text
Endotoxin contamination in recombinant human heat shock protein 70 (Hsp70) preparation is responsible for the induction of tumor necrosis factor alpha release by murine macrophages: M.F. Tsan, et al. ; J. Biol. Chem.
278, 174 (2003),
Application(s): In Vitro Assay using human samples,
Abstract;
Related Products
