Acetylated Lysine (acLys) antibody (HRP)

Details for Product No. ABIN361692
Request Want additional data for this product?

The Independent Validation Initiative strives to provide you with high quality data. Find out more

Antigen
Epitope
acLys
(2)
Reactivity
All Species
(46), (4), (4), (2), (2), (1), (1), (1)
Host
Rabbit
(28), (26)
Clonality
Polyclonal
Conjugate
HRP
(3), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (1)
Application
Western Blotting (WB), ELISA, Immunoprecipitation (IP), Immunofluorescence (IF)
(53), (51), (40), (24), (24), (2), (1), (1), (1)
Pubmed 7 references available
Quantity 400 μL
Options
Shipping to United States (Change)
Availability Will be delivered in 3 to 4 Business Days
Request Want additional data for this product?

The Independent Validation Initiative strives to provide you with high quality data. Find out more

Catalog No. ABIN361692
457.60 $
Plus shipping costs $45.00

Order hotline:

  • +1 404 474 4654
  • +1 888 205 9894 (TF)
Immunogen Acetylated KLH
Isotype IgG
Specificity Detects proteins containing acetylated lysine residues in SDS PAGE immunoblots.
Background Synonyms:
lysine, acetyl lysine
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 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. 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.
Research Area Cell Signaling
Application Notes Recommended Dilution: 1:250 (WB)
Restrictions For Research Use only
Format Liquid
Concentration 0.25 mg/mL
Buffer PBS, 50 % glycerol, 0.09 % sodium azide
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
Background 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).

Martínez-Balbás, 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).

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).

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

Validation Images
Did you look for something else?
back to top