HSP70 antibody (PE)

Catalog No. ABIN2485891

The Rat Monoclonal anti-HSP70 antibody has been validated for WB, ELISA, IF and ICC. It is suitable to detect HSP70 in samples from Drosophila melanogaster.

Quick Overview for HSP70 antibody (PE) (ABIN2485891)

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

Reactivity: Drosophila melanogaster

Host: Rat

Clonality: Monoclonal

Conjugate: This HSP70 antibody is conjugated to PE

Application: Western Blotting (WB), ELISA, Immunofluorescence (IF), Immunocytochemistry (ICC)

Clone: 7FB

Product Details anti-HSP70 Antibody (PE)

Specificity: Detects ~70 kDa (heat-inducible form).

Cross-Reactivity: Drosophila melanogaster

Purification: Protein G Purified

Immunogen: Prepared from Drosophila tissue culture cells heat shocked at 36.5C for 3 hours, and isolated using SDS PAGE.

Isotype: IgG2b

Application Details

Application Notes:

• WB (1:2000)
• optimal dilutions for assays should be determined by the user.

Comment:

1 μg/ml of ABIN2485891 was sufficient for detection of Drosophila HSP70 using an indirect assay with rabbit anti-rat IgG and goat anti-rabbit IgG:HRP.

Restrictions: For Research Use only

Handling

Format: Liquid

Concentration: 1 mg/mL

Buffer: PBS pH 7.4, 50 % glycerol, 0.1 % 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: 4 °C

Storage Comment: Conjugated antibodies should be stored at 4°C

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 (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: 48582

NCBI Accession: NP_524927

UniProt: Q9BIS2