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Lysine (lys) (acetylated) anticorps (APC)

L’anticorps Lapin Polyclonal anti- a été validé pour ICC, IF, IP, ELISA et WB. Il convient pour détecter dans des échantillons de .
N° du produit ABIN2486074

Aperçu rapide pour Lysine (lys) (acetylated) anticorps (APC) (ABIN2486074)

Antigène

Lysine (lys)

Hôte

  • 19
  • 10
Lapin

Clonalité

  • 19
  • 10
Polyclonal

Conjugué

  • 3
  • 3
  • 3
  • 3
  • 3
  • 3
  • 3
  • 3
  • 3
  • 2
APC

Application

  • 29
  • 29
  • 29
  • 29
  • 29
  • 10
Immunocytochemistry (ICC), Immunofluorescence (IF), Immunoprecipitation (IP), ELISA, Western Blotting (WB)
  • Épitope

    • 19
    • 10
    acetylated

    Specificité

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

    Purification

    Protein A Purified

    Immunogène

    Acetylated KLH Conjugated
  • 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 ABIN2486074 was sufficient to detect the acetylated histone from TSA treated mouse spleen cell in western blot analysis.

    Restrictions

    For Research Use only
  • 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

    4 °C

    Stockage commentaire

    Conjugated antibodies should be stored at 4°C
  • 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).
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