Human, Mouse, Rat Drosophila, Housefly, Rabbit, Sponge, Yeast
Applications:
IHC, IP, WB
Recommended Dilutions/Conditions:
Western Blot (1:1,000, colorimetric) Suggested dilutions/conditions may not be available for all applications. Optimal conditions must be determined individually for each application.
Application Notes:
Detects a band of ~72kDa by Western blot.
Purity Detail:
Protein G affinity purified.
Formulation:
Liquid. In PBS, pH 7.2, containing 50% glycerol and 0.09% sodium azide.
Handling:
Avoid freeze/thaw cycles.
Shipping:
Blue Ice
Long Term Storage:
-20°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
Western blot analysis of HSC70/HSP70 mAb (BB70) (Prod. No. ADI-SPA-822): Lane 1: MW marker, Lane 2:HSC70(HSP73) (Prod. No. ADI-SPP-751), Lane 3:HSP70(HSP72) (Prod. No. ADI-NSP-555), Lane 4:HeLa Cell Lysate (heat shocked)(Prod. No. ADI-LYC-HL101), Lane 5:PC-12 Cell Lysate (heat shocked)(Prod. No. ADI-LYC-PC101), Lane 6:RK-13 Cell Lysate (heat shocked), Lane 7: 3T3 Cell Lysate (heat shocked)(Prod. No. ADI-LYC-3T101)
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Product Literature References
Lack of Hikeshi activates HSF1 activity under normal conditions and disturbs the heat-shock response: S. Kose, et al.; Life Sci. Alliance 5, e202101241 (2022), Abstract;
Modulation of Expression of PVYNTN RNA-Dependent RNA Polymerase (NIb) and Heat Shock Cognate Host Protein HSC70 in Susceptible and Hypersensitive Potato Cultivars: E. Koziel, et al.; Vaccines (Basel) 9, 1254 (2021), Abstract;
Tah1, A Key Component of R2TP Complex that Regulates Assembly of snoRNP, is Involved in De Novo Generation and Maintenance of Yeast Prion [URE3]: A. Puri, et al.; J. Mol. Biol. 433, 166976 (2021), Abstract;
Modulation of Protein Quality Control and Proteasome to Autophagy Switch in Immortalized Myoblasts from Duchenne Muscular Dystrophy Patients: M. Wattin, et al.; Int. J. Mol. Sci. 19, 178 (2018), Application(s): Western Blot, Abstract; Full Text
The cellular stress response of the scleractinian coral Goniopora columna during the progression of the black band disease: D. Seveso, et al.; Cell Stress Chaperones 22, 225 (2017), Application(s): Western Blot, Abstract; Full Text
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), Application(s): Western Blot, Abstract;
HSP90 inhibitor-SN-38 conjugate strategy for targeted delivery of topoisomerase I inhibitor to tumors: D.A. Proia, et al.; Mol. Cancer Ther. 14, 2422 (2015), Application(s): Immunoblotting , Abstract; Full Text
Identification and quantitative analysis of cellular proteins affected by treatment with withaferin A using A SILAC-based proteomics approach: M. Narayan, et al.; J. Ethnopharmacol. 8741, 30149 (2015), Application(s): Western Blot, Abstract;
Prion-like transmission of neuronal huntingtin aggregates to phagocytic glia in the Drosophila brain: M. M. Pearce, et al.; Nat. Commun. 6, 6768 (2015), Application(s): Immunofluorescence , Abstract;
The Expression of Tubulin Polymerization Promoting Protein TPPP/p25α is Developmentally Regulated in Cultured Rat Brain Oligodendrocytes and Affected by Proteolytic Stress: C. Richter-Landsberg, et al. ; Glia 56, 1736 (2008), Application(s): WB, IF using rat tissue, Abstract;
Uptake of the antifungal cationic peptide Histatin 5 by Candida albicans Ssa2p requires binding to non-conventional sites within the ATPase domain: M. Edgerton, et al. ; Mol. Microbiol. 70, 1246 (2008), Application(s): WB using yeast cell lysates, Abstract;
Developmental and hyperthermia-induced expression of the heat shockproteins HSP60 and HSP70 in tissues of the housefly Musca domestica:An in vitro study: P. Tiwari, et al. ; Genet. Mol. Biol. 30, 159 (2007), Application(s): WB, IHC using housefly tissue, Abstract;
Phosphoglucose isomerase genotype affects running speed and heat shockprotein expression after exposure to extreme temperatures in a montanewillow beetle: N. Rank, et al. ; J. Exp. Biol. 210, 750 (2007), Application(s): WB using insect cell lysates, Abstract;
Co-translational folding of caspase-activated DNase with Hsp70, Hsp40, and inhibitor of caspase-activated DNase: S. Nagata, et al. ; J. Biol. Chem. 277, 3364 (2002), Application(s): IP using rabbit samples, Abstract;
Tumor necrosis factor receptor 1 is an ATPase regulated by silencer of death domain: E.M. Eddy, et al. ; Mol. Cell. Biol. 22, 2536 (2002), Application(s): WB using mouse samples, Abstract;
Modulation of Drosophila heat shock transcription factor activity by the molecular chaperone DROJ1: C. Wu, et al. ; EMBO J. 20, 499 (2001), Application(s): WB using drosophila samples, Abstract;
Regional distribution of Hsp70 in the CNS of young and old food-restricted rats following hyperthermia: P.A. Mason, et al. ; Brain Res. Bull. 55, 367 (2001), Application(s): WB using rat samples, Abstract;
Identification of genes that modify ataxin-1-induced neurodegeneration: J. Botas, et al. ; Nature 408, 101 (2000), Application(s): IHC using drosophila samples, Abstract;
Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1: R. Voellmy, et al. ; Cell 94, 471 (1998), Application(s): WB, IP using human samples, Abstract;
A molecular chaperone that assists in the folding of emerging polypeptides and the refolding of denatured proteins.
Produced in E. coli., ≥95% (SDS-PAGE; Western blot), ELISA, IHC, WB, Activity assay, Antigen microarray, Apoptosis assay, in vitro Assay | Print as PDF
