Lysine (lys) (methylated) anticorps (PE)

N° du produit ABIN5650790

L’anticorps Lapin Polyclonal anti- a été validé pour ELISA, WB, ICC, IF et IP. Il convient pour détecter dans des échantillons de .

Aperçu rapide pour Lysine (lys) (methylated) anticorps (PE) (ABIN5650790)

Antigène: Lysine (lys)

Hôte: Lapin

Clonalité: Polyclonal

Conjugué: PE

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

Détail du produit

Épitope: methylated

Specificité: Detects proteins containing methylated lysine residues.

Purification: Protein A Purified

Immunogène: Methylated KLH Conjugated

Information d'application

Indications d'application:

• WB (1:20000)
• ICC/IF (1:200)
• optimal dilutions for assays should be determined by the user.

Commentaires:

0.2-0.5 μg/ml of SPC-158 was sufficient for detection of the methylated histone by western blot analysis using melanoma cells in TBSt.

Restrictions: For Research Use only

Stockage

Format: Liquid

Concentration: 1 mg/mL

Buffer: PBS, 50 % glycerol, Storage buffer may change when conjugated

Stock: 4 °C

Stockage commentaire: Conjugated antibodies should be stored at 4°C

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).