Lysine (lys) (methylated) antibody (FITC)

Catalog No. ABIN5650787

The Rabbit Polyclonal anti- antibody has been validated for ICC, IF, IP, ELISA and WB. It is suitable to detect in samples from .

Quick Overview for Lysine (lys) (methylated) antibody (FITC) (ABIN5650787)

Target: Lysine (lys)

Host: Rabbit

Clonality: Polyclonal

Conjugate: FITC

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

Product Details

Binding Specificity: methylated

Specificity: Detects proteins containing methylated lysine residues.

Purification: Protein A Purified

Immunogen: Methylated KLH Conjugated

Application Details

Application Notes:

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

Comment:

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

Handling

Format: Liquid

Concentration: 1 mg/mL

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

Storage: 4 °C

Storage Comment: Conjugated antibodies should be stored at 4°C

Target Details

Target: Lysine (lys)

Alternative Name: Lysine

Target Type: Amino Acid

Background: 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).