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Product Name
Acetylated Lysine Antibody
Catalog #
SPC-155F
Package size
400ul
Price
$295.00 USD
Bulk Quote
Type
Polyclonal
Conjugate
N/A
Datasheet
SPC 155 Acetylated Lysine Cell Signaling
Description
Anti-Acetylated Lysine
Research Area
Cell Signaling, Post-translational Modifications
Alternative Names
lysine, acetyl lysine
Clone Number
N/A
Host Species
Rabbit
Isotype
N/A
Immunogen
Acetylated KLH Conjugated
Applications
WB, IP, ELISA, IF
Species Reactivity
Acetylated lysine residues. No reaction to non-acetylated proteins.
Accession Number
N/A
SwissProt
N/A
Background Info
Detects proteins containing acetylated lysine residues in SDS PAGE immunoblots.
Recommended Dilutions
1:250 (WB)
Form
Affinity Purified
Storage Buffer
PBS, 50% glycerol, 0.09% sodium azide
Concentration
250µg/mL
Certificate of Analysis
A 1/250 dilution of SPC-155 was sufficient to detect the acetylated histone from TSA treated mouse spleen cell in western blot analysis.
Storage Temp
-20°C
Shipping Temp
Blue Ice or 4°C

This antibody is available conjugated to several dyes. Please select one of the conjugates from the lists below:

ATTO Conjugates:

ATTO-Conjugates.pdf

Enzyme & Fluorescent Conjugates:

Enzyme-Fluorescent-Conjugate.pdf

Western blot analysis of the acetylated histone from TSA-treated mouse spleen cells.


Western blot analysis of acetylated lysine in BSA (Left) and Acetylated BSA (Right) using a 1:1000 dilution of SPC-155.
Research 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).
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.
6. Chan, H.M. et al. (2001). Nat. Cell Biol. 3: 667- . 674.
7. Martinez-Balbas, M.A. et al. (2000). EMBO J. 19: 662-671.
Cited References
1. Kazuhiro Ishiguro, Takafumi Ando, Osamu Maeda, Osamu Watanabeand Hidemi Goto. Cutting Edge: Tubulin α Functions as an Adaptor in NFAT–Importin β Interaction. J Immunol 2011 186:2710-2713; published ahead of print January 28, 2011, doi:10.4049/jimmunol.1003322
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