Acetylated Lysine (acLys) antibody (Biotin)

Antigen: Acetylated Lysine

Binding Site: acLys

Clonality: Polyclonal

Host: Rabbit

Reactivity: Please enquire

Conjugate: Biotin

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

Catalog no.: ABIN361691

Additional Information

UniProt: N/A

Immunogen: Acetylated KLH

Description: 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. 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). Protein posttranslational reversible lysine Nepsilon-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. The regulation of protein acetylation status is impaired in the pathologies of cancer and polyglutamine diseases, and HDACs have become promising targets for anti-cancer drugs currently in development.
Synonyms: lysine, acetyl lysine

Specificity: Detects proteins containing acetylated lysine residues in SDS PAGE immunoblots.

Application Details

Application Notes: 1:250 (WB)

Concentration: 0.25mg/mL

Purification: Rabbit immunoglobulin

Buffer: PBS, 50% glycerol

Preservative: 0.09% sodium azide

Storage: Store at -20° C. Shipping Temperature: Blue Ice or 4° C

Storage Shipping Temp Max: Blue Ice or 4 °C

Research Area: Cell Signaling

Restrictions: For Research Use only

Publications

Hassig, Schreiber: "Nuclear histone acetylases and deacetylases and transcriptional regulation: HATs off to HDACs." in: Current opinion in chemical biology, Vol. 1, Issue 3, pp. 300-8, 1998 (PubMed).

Martuinez-Balbuas, Bauer, Nielsen et al.: "Regulation of E2F1 activity by acetylation." in: The EMBO journal, Vol. 19, Issue 4, pp. 662-71, 2000 (PubMed).

Chan, Krstic-Demonacos, Smith et al.: "Acetylation control of the retinoblastoma tumour-suppressor protein." in: Nature cell biology, Vol. 3, Issue 7, pp. 667-74, 2001 (PubMed).

Hughes: "Polyglutamine disease: acetyltransferases awry." in: Current biology : CB, Vol. 12, Issue 4, pp. R141-3, 2002 (PubMed).

Vigushin, Coombes: "Targeted histone deacetylase inhibition for cancer therapy." in: Current cancer drug targets, Vol. 4, Issue 2, pp. 205-18, 2004 (PubMed).

Yang: "Lysine acetylation and the bromodomain: a new partnership for signaling." in: BioEssays : news and reviews in molecular, cellular and developmental biology, Vol. 26, Issue 10, pp. 1076-87, 2004 (PubMed).

Yang: "Multisite protein modification and intramolecular signaling." in: Oncogene, Vol. 24, Issue 10, pp. 1653-62, 2005 (PubMed).