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Key Documents

AB3561

Sigma-Aldrich

Anti-phospho HSP27 (pS82) Antibody

Chemicon®, from rabbit

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About This Item

Code UNSPSC :
12352203
eCl@ss :
32160702
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Niveau de qualité

Forme d'anticorps

purified immunoglobulin

Type de produit anticorps

primary antibodies

Clone

polyclonal

Espèces réactives

human

Fabricant/nom de marque

Chemicon®

Technique(s)

western blot: suitable

Numéro d'accès NCBI

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Modification post-traductionnelle de la cible

phosphorylation (pSer82)

Informations sur le gène

human ... HSPB1(3315)

Description générale

Heat Shock Protein 27 (HSP27) is a 27 kDa member of a family of proteins whose expression and function are stimulated by heat shock and other stress stimuli. A major function of these proteins is to serve as chaperones that bind to and stabilize the active conformation of other proteins. HSP27, along with other members of the small HSP group, possesses a C-terminal α-crystalline homology domain. HSP27 is localized to the cytoplasm of unstressed cells but can redistribute to the nucleus in response to stress, where it may function to stabilize DNA and/or the nuclear membrane. Cytoplasmic HSP27 exists in multiple complexes. One complex consists of HSP27, Akt (PKB), MAPKAP-kinase 2, and p38 MAPK. The presence of HSP27 in this complex is required for Akt activation by stress stimuli. Another complex consists of HSP27 and the IKK complex. HSP27 is also an actin capping protein that binds to the barbed (growing) ends of actin filaments, thereby inhibiting filament extension. Phosphorylation of HSP27 on serine 82 by MAPKAP-kinase 2 leads to HSP27 dissociation from the Akt/MAPKAP-kinase 2/p38 complex and from actin filaments, and stimulates HSP27 binding to the IKK complex.

Spécificité

Human HSP27. This antibody does not detect endogenous mouse HSP25 [pS86] protein in extracts of NIH3T3 cells treated with anisomycin; however, interaction with the human HSP27 protein is inhibited by the phosphopeptide used to generate the mouse HSP25 [pS86] antibody.

Immunogène

The antiserum was produced against a chemically synthesized phosphopeptide derived from a region of human HSP27 that contains serine 82.

Application

Anti-phospho HSP27 (pS82) Antibody detects level of phospho HSP27 (pS82) & has been published & validated for use in WB.
Research Category
Protein Trafficking
Research Sub Category
Chaperones

Liaison

Replaces: 04-448

Forme physique

Dulbecco′s phosphate buffered saline (without Mg2+ and Ca2+), pH 7.3 (+/- 0.1), 50% glycerol with 1.0 mg/mL BSA (IgG, protease free) as a carrier. 0.05% sodium azide.
Format: Purified

Stockage et stabilité

Store at -20°C. We recommend a brief centrifugation before opening to settle vial contents. Then, apportion into working aliquots and store at -20°C. For shipment or short-term storage (up to one week), 2-8°C is sufficient.

Remarque sur l'analyse

Control
HeLa cells treated with TNF-α.

Informations légales

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

Clause de non-responsabilité

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 2


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Consulter la Bibliothèque de documents

Thyroxine pretreatment increases basal myocardial heat-shock protein 27 expression and accelerates translocation and phosphorylation of this protein upon ischaemia.
Pantos, Constantinos, et al.
European Journal of Pharmacology, 478, 53-60 (2003)
Angiogenesis inhibitors target the endothelial cell cytoskeleton through altered regulation of heat shock protein 27 and cofilin.
Keezer, S.M., et al.
Cancer Research, 63(19), 6405-6412 (2003)
Madhavi J Rane et al.
The Journal of biological chemistry, 278(30), 27828-27835 (2003-05-13)
Activation of the serine-threonine kinase Akt by cytokines, chemokines, and bacterial products delays constitutive neutrophil apoptosis, resulting in a prolonged inflammatory response. We showed previously that Akt exists in a signaling complex with p38 MAPK, MAPK-activated protein kinase-2 (MAPKAPK-2), and

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