HSP70 antibody

Catalog No. ABIN361821

The Rabbit Polyclonal anti-HSP70 antibody has been validated for WB, IHC, ELISA, IF, IP and ICC. It is suitable to detect HSP70 in samples from Human. There are 4+ publications available.

Quick Overview for HSP70 antibody (ABIN361821)

Target: HSP70 (Heat Shock Protein 70 (HSP70))

Reactivity: Human

Host: Rabbit

Clonality: Polyclonal

Conjugate: This HSP70 antibody is un-conjugated

Application: Western Blotting (WB), Immunohistochemistry (IHC), ELISA, Immunofluorescence (IF), Immunoprecipitation (IP), Immunocytochemistry (ICC)

Product Details anti-HSP70 Antibody

Specificity: Detects a ~70 kDa. May cross-react with HSC70 at lower dilutions.

Cross-Reactivity: Beluga, Carp, Coral, Cow, Dog, Fish, Guinea Pig, Hamster, Human, Leishmania amazonensis, Monkey, Mouse, Pig, Plant, Rat, Shark, Sheep

Purification: Peptide Affinity Purified

Immunogen: Recombinant Full length HSP70 Protein

Application Details

Application Notes:

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

Comment:

A 1:1000 dilution of ABIN361820 was sufficient for detection of HSP70 in 20 μg of HeLa cell lysate by ECL immunoblot analysis.

Restrictions: For Research Use only

Handling

Format: Liquid

Concentration: 1 mg/mL

Buffer: PBS pH 7.4, 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 antibody (ABIN361821)

Woodford, Dunn, Blanden, Capriotti, Loiselle, Prodromou, Panaretou, Hughes, Smith, Ackerman, Haystead, Loh, Bourboulia, Schmidt, Marston Linehan, Bratslavsky, Mollapour: "The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding." in: Nature communications, Vol. 7, pp. 12037, (2018) (PubMed).

Codonho, Costa, Peloso, Joazeiro, Gadelha, Giorgio: "HSP70 of Leishmania amazonensis alters resistance to different stresses and mitochondrial bioenergetics." in: Memórias do Instituto Oswaldo Cruz, (2017) (PubMed).

Watanabe, Tsujimura, Taguchi, Tanaka: "HSF1 stress response pathway regulates autophagy receptor SQSTM1/p62-associated proteostasis." in: Autophagy, Vol. 13, Issue 1, pp. 133-148, (2017) (PubMed).

Silverstein, Ordanes, Wylie, Files, Milligan, Presley, Kavanagh: "Inducing Muscle Heat Shock Protein 70 Improves Insulin Sensitivity and Muscular Performance in Aged Mice." in: The journals of gerontology. Series A, Biological sciences and medical sciences, Vol. 70, Issue 7, pp. 800-8, (2015) (PubMed).

Target Details for HSP70

Target: HSP70 (Heat Shock Protein 70 (HSP70))

Alternative Name: HSP70

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 (1, 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 ATPbinding 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. Looking for more information on HSP70? Visit our new HSP70 Scientific Resource Guide at http://www.HSP70.com.

Gene ID: 3303

NCBI Accession: NP_005336

UniProt: P0DMV8, P0DMV9