Lysine (lys) (acetylated) antibody

Catalog No. ABIN2486064

This Rabbit Polyclonal antibody specifically detects in ICC, IF, IP, ELISA and WB. It exhibits reactivity toward and has been mentioned in 1 publication.

Quick Overview for Lysine (lys) (acetylated) antibody (ABIN2486064)

Target: Lysine (lys)

Host: Rabbit

Clonality: Polyclonal

Conjugate: Un-conjugated

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

Product Details

Binding Specificity: acetylated

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

Purification: Protein A Purified

Immunogen: Acetylated KLH Conjugated

Application Details

Application Notes:

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

Comment:

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

Handling

Format: Liquid

Concentration: 1 mg/mL

Buffer: PBS, 50 % glycerol, 0.09 % sodium azide, Storage buffer may change when conjugated

Preservative: Sodium azide

Precaution of Use: This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

Storage: -20 °C

Storage Comment: -20°C

References

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

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).