HSP70 anticorps

N° du produit ABIN2485875

Cet anticorps Rat Monoclonal détecte spécifiquement HSP70 dans WB, ELISA, IF et ICC. Il présente une réactivité envers Drosophila melanogaster et a été mentionné dans 1 publication.

Aperçu rapide pour HSP70 anticorps (ABIN2485875)

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

Reactivité: Drosophila melanogaster

Hôte: Rat

Clonalité: Monoclonal

Conjugué: Cet anticorp HSP70 est non-conjugé

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

Clone: 7FB

Détail du produit anti-HSP70 anticorps

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

Réactivité croisée: Drosophila melanogaster

Purification: Protein G Purified

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

Isotype: IgG2b

Information d'application

Indications d'application:

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

Commentaires:

1 μg/ml of ABIN2485875 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

Stockage

Format: Liquid

Concentration: 1 mg/mL

Buffer: PBS pH 7.4, 50 % glycerol, 0.1 % sodium azide, Storage buffer may change when conjugated

Agent conservateur: Sodium azide

Précaution d'utilisation: This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

Stock: -20 °C

Stockage commentaire: -20°C

Références pour anticorps anti-HSP70 (ABIN2485875)

Merkling, Overheul, van Mierlo, Arends, Gilissen, van Rij: "The heat shock response restricts virus infection in Drosophila." dans: Scientific reports, Vol. 5, pp. 12758, (2015) (PubMed).

Détails sur HSP70

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

Autre désignation: HSP70

Sujet: 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.

ID gène: 48582

NCBI Accession: NP_524927

UniProt: Q9BIS2