Lysine (lys) (acetylated) anticorps

N° du produit ABIN2486064

Cet anticorps Lapin Polyclonal détecte spécifiquement dans ELISA, WB, ICC, IF et IP. Il présente une réactivité envers et a été mentionné dans 1 publication.

Aperçu rapide pour Lysine (lys) (acetylated) anticorps (ABIN2486064)

Antigène: Lysine (lys)

Hôte: Lapin

Clonalité: Polyclonal

Conjugué: Inconjugué

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

Détail du produit

Épitope: acetylated

Specificité: Detects proteins containing acetylated lysine residues. No reaction to non-acetylated proteins.

Purification: Protein A Purified

Immunogène: Acetylated KLH Conjugated

Information d'application

Indications d'application:

• WB (1:250)
• ICC/IF (1:100)
• optimal dilutions for assays should be determined by the user.

Commentaires:

A 1/250 dilution of ABIN2486064 was sufficient to detect the acetylated histone from TSA treated mouse spleen cell in western blot analysis.

Restrictions: For Research Use only

Stockage

Format: Liquid

Concentration: 1 mg/mL

Buffer: PBS, 50 % glycerol, 0.09 % 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

Référence

Ishiguro, Ando, Maeda, Watanabe, Goto: "Cutting edge: tubulin ? functions as an adaptor in NFAT-importin ? interaction." dans: Journal of immunology (Baltimore, Md. : 1950), Vol. 186, Issue 5, pp. 2710-3, (2011) (PubMed).

Détail du antigène

Antigène: Lysine (lys)

Autre désignation: Lysine

Classe de substances: Amino Acid

Sujet: Post-translational modifications of proteins play critical roles in the regulation and function of many known biological processes. Proteins can be post-translationally modified in many different ways, and a common post-transcriptional modification of Lysine involves acetylation (1). The conserved amino-terminal domains of the four core histones (H2A, H2B, H3 and H4) contain lysines that are acetylated by histone acetyltransferases (HATs) and deacetylated by histone deacetylases (HDACs) (2). Protein posttranslational reversible lysine Nε-acetylation and deacetylation have been recognized as an emerging intracellular signaling mechanism that plays critical roles in regulating gene transcription, cell-cycle progression, apoptosis, DNA repair, and cytoskeletal organization (3). The regulation of protein acetylation status is impaired in the pathologies of cancer and polyglutamine diseases (4), and HDACs have become promising targets for anti-cancer drugs currently in development (5).