|
|
Cat. No |
Model |
Description |
Unit |
Price (VATº°µµ) |
³³±â |
Àç°í |
DataSheet |
ÁÖ¹®/°ßÀû |
LCA-24-345313 |
AM03158PU-N |
Acetylated Lysine//Avis, Bovine/Mouse |
1/EA |
|
|
|
|
¹®ÀÇ |
|
|
|
|
|
|
Subject
|
Acetylated Lysine |
Description
|
/ Avis, Bovine/Mouse |
Clonality
|
Mono |
Company
|
Acris Antibodies GmbH |
Application
|
Frozen sections, Enzyme Immunoassay, Western blot / Immunoblot |
Conjugation
|
|
Immunogen
|
|
Contents
|
Description: Manufacturer | Acris Antibodies GmbH | Quantity | 0.1 mg | Reactivity | Avis, Bovine | Presentation | Purified | Applications | Frozen sections, Enzyme Immunoassay, Western blot / Immunoblot | Isotype | IgG1 | Host | Mouse | Clone | 7F8 | PDF datasheet | view | Shipping to | Worldwide | Synonyms | acetyl Lysine, acetyl-Lysine | Immunogen | Acetylated KLH | Product Type | Antibodies | Recommended Isotype Control | AM03095PU-N | Storage | Store the antibody at 2 - 8 °C up to one month or (in aliquots) at -20 °C for longer. Avoid repeated freezing and thawing. Shelf life: one year from despatch. | References | 1. Yang XJ. (2005). Oncogene. 24:1653-1662. 2. Hassig, C.A. and Schreiber, S.L. (1997). Curr. Opin. Chem. Biol. 1(3): 300-308. 3. Yang XJ. (2004). Bioessays 26:1076-1087. 4. Hughes, R.E. (2002). Curr. Biol. 12: R141-R143. 5. Vigushin, D.M. and Coombes, R.C. (2004). Curr. Cancer Drug Targets 4: 205-218. | |
Format | State: Liquid Ig fraction | ? | Purification: Protein G affinity chromatography | ? | Buffer System: PBS, pH 7.4, 0.09 % sodium azide in 50 % glycerol | |
Specificity | Detects proteins containing acetylated lysine residues in ELISA and WBs. Does not detect non-acetylated lysine residues. | Application | Western blot (1 ?g/ml was sufficient for detection of 20 ?g acetylated chicken erythrocyte histones. ELISA. Immunohistochemistry. | 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 posttranscriptional 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 Nu-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 anticancer drugs currently in development (5). | Concentration | 1.0 mg/ml | |
|
|
|
|