HSP70/HSC70 antibody

Catalog No. ABIN361706

Product Details anti-HSP70/HSC70 Antibody

Target: HSP70/HSC70 (HSC70-4) (Heat Shock Protein Cognate 4 (HSC70-4))

Reactivity: Human

Host: Mouse

Clonality: Monoclonal

Conjugate: This HSP70/HSC70 antibody is un-conjugated

Application: Western Blotting (WB), Immunoprecipitation (IP), Immunohistochemistry (IHC), Flow Cytometry (FACS), Immunoelectron Microscopy (IEM), Immunocytochemistry (ICC), Immunofluorescence (IF)

Specificity: Detects ~72 (HSP) and ~73 kDa (HSC).

Cross-Reactivity: Beluga, C. elegans, Chicken, Cow, Dog, Drosophila melanogaster, Fish, Guinea Pig, Hamster, Human, Monkey, Mouse, Pig, Plant, Rabbit, Rat, Sheep, Xenopus laevis

Purification: Protein G Purified

Immunogen: Recombinant HSP70/HSC70

Clone: N27F3-4

Isotype: IgG1

Application Details

Application Notes:

• WB (1:1000)
• IHC (1:100)
• ICC/IF (1:50)
• optimal dilutions for assays should be determined by the user.

Comment:

1 μg/ml of ABIN361705 was sufficient for detection of HSP70/HSC70 in 20 μg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.

Restrictions: For Research Use only

Handling

Format: Liquid

Concentration: 1 mg/mL

Buffer: PBS pH 7.2, 50 % glycerol, 0.09 % sodium azide, Storage buffer may change when conjugated

Preservative: Sodium azide

Precaution of Use: This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

Storage: -20 °C

Storage Comment: -20°C

References for anti-HSP70/HSC70 antibody (ABIN361706)

Wang, Kojima, Mobley, West: "Proteomic analysis of urinary extracellular vesicles reveal biomarkers for neurologic disease." in: EBioMedicine, Vol. 45, pp. 351-361, (2019) (PubMed).

Preusse-Prange, Modrow, Schwark, von Wurmb-Schwark: "Detection of constitutive and inducible HSP70 proteins in formalin fixed human brain tissue." in: Forensic science international, Vol. 235, pp. 62-7, (2014) (PubMed).

Morshed, Ma, Latif, Davies: "How one TSH receptor antibody induces thyrocyte proliferation while another induces apoptosis." in: Journal of autoimmunity, Vol. 47, pp. 17-24, (2013) (PubMed).

Sun, Prince, Manjarrez, Scroggins, Matts: "Characterization of the interaction of Aha1 with components of the Hsp90 chaperone machine and client proteins." in: Biochimica et biophysica acta, Vol. 1823, Issue 6, pp. 1092-101, (2012) (PubMed).

Modrow, Preusse-Prange, Meyer, Harder, Schwark, von Wurmb-Schwark: "Highly reliable quantification of proteins such as members of the HSP70 superfamily based on the grey scale index via immune detection stained bands on a Western blot." in: Forensic science international, Vol. 222, Issue 1-3, pp. 256-8, (2012) (PubMed).

Mutsvunguma, Moetlhoa, Edkins, Luke, Blatch, Knox: "Theiler's murine encephalomyelitis virus infection induces a redistribution of heat shock proteins 70 and 90 in BHK-21 cells, and is inhibited by novobiocin and geldanamycin." in: Cell stress & chaperones, Vol. 16, Issue 5, pp. 505-15, (2011) (PubMed).

Chen, Prior, Dargusch, Roberts, Riek, Eichmann, Chiruta, Akaishi, Abe, Maher, Schubert: "A novel neurotrophic drug for cognitive enhancement and Alzheimer's disease." in: PLoS ONE, Vol. 6, Issue 12, pp. e27865, (2011) (PubMed).

Olkku, Leskinen, Lammi, Hynynen, Mahonen: "Ultrasound-induced activation of Wnt signaling in human MG-63 osteoblastic cells." in: Bone, Vol. 47, Issue 2, pp. 320-30, (2010) (PubMed).

Target Details for HSP70/HSC70

Target: HSP70/HSC70 (HSC70-4) (Heat Shock Protein Cognate 4 (HSC70-4))

Alternative Name: HSP70/HSC70 (HSC70-4 Products)

Background: HSP70 genes encode abundant heat-inducible 70- kDa HSPs (HSP70s). In most eukaryotes HSP70 genes exist as part of a multigene family. They are found in most cellular compartments of eukaryotes including nuclei, mitochondria, chloroplasts, the endoplasmic reticulum and the cytosol, as well as in bacteria. The genes show a high degree of conservation, having at least 50 % identity (2). The N-terminal two thirds of HSP70s are more conserved than the C-terminal third. HSP70 binds ATP with high affinity and possesses a weak ATPase activity which can be stimulated by binding to unfolded proteins and synthetic peptides (3). When HSC70 (constitutively expressed) present in mammalian cells was truncated, ATP binding activity was found to reside in an N-terminal fragment of 44 kDa which lacked peptide binding capacity. Polypeptide binding ability therefore resided within the C-terminal half (4). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (5). All HSP70s, regardless of location, bind proteins, particularly unfolded ones. The molecular chaperones of the HSP70 family recognize and bind to nascent polypeptide chains as well as partially folded intermediates of proteins preventing their aggregation and misfolding. The binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein (6). The universal ability of HSP70s to undergo cycles of binding to and release from hydrophobic stretches of partially unfolded proteins determines their role in a great variety of vital intracellular functions such as protein synthesis, protein folding and oligomerization and protein transport. For more information visit our HSP70 Scientific Resource Guide at http://www.HSP70.com.

Gene ID: 3303

NCBI Accession: NP_005336

UniProt: P0DMV8, P0DMV9