Home >PTM Proteomics > Protein Acetylation

Acetyl Lysine Antibody, Agarose

Catalog # Pack Size Price(USD)
ICP0388 2 mg $525.00

Quantity:

Product Description
The acetylated Lysine antibody is immobilized to beaded agarose via amide linkages. The product could be utilized as an affinity matrix for rapid isolation and purification of the species of proteins or peptides with acetyl Lysine residues.
  
  The acetylated peptide profile from the acetyl-lysine-specific affinity chromatography (matrix=ICP0388). Approximately 5 mg of the trypsinated crude protein from the TSA treated MMRU cells was loaded
Formulation
0.5 mL beaded agarose suspended in 1 mL of glycerol.
Antibody Immobilized
4 mg/mL, antibody is covalently linked through amide bonds with NHS activated-SMCC then linked to thiolated Agarose beads via thiol ether bonds.
Specificity
The antibody selectively captures the peptides and proteins with acetylated lysine residues (N-epsilon). There is no cross-reaction with methylated proteins or mono- and dimethylated proteins.
Binding Capacity
Approximately 0.2 mg of acetylated histone/ml
Applications
Rapid isolation and purification of peptides or proteins with acetylated lysine residues from mixtures of cell lysates or protease-digested mixtures.
Scientific Description
Protein acetylation is a form of post-translational modification known to regulate many diverse biological processes. Detection, isolation, and identification of the acetylated protein/peptide is essential in proteomic studies. Affinity chromatography is one of the most efficient and rapid method to enrich and purify the acetylated species for further MS/MS identification.
Storage & Stability
Product is stable for several weeks at 4°C. For extended storage, aliquot content and store product at –20ºC. Avoid cycles of freezing and thawing. Expiration date is one year from date of shipping if properly stored.
 
Publications

 

 

1.Science,  2009. 325, 834-840

2.Cell, 2010. 140, 257-267 ( View PDF )

3.PROTEOMICS, 2010. 10, 1029-1039 ( View PDF )

4.Plant Physiology, 2011. 155, 1779-1790 ( View PDF)

5.Nucleic Acids Research, 2011, 1-19

6.Euro. J. Cell Biol, 2011. Vol. 90, 128-135

7. Molecular & Cellular Proteomics. 2012. 11: 1510-1522

8.Molecular & Cellular Proteomics. 2012. 11: 945-956

9.J. Proteome Res, 2012. Vol. 11. 1633-1643  

10.PNAS, 2012. Vol. 109, 111330-11138

11.Science Report, 2012. August 16.

12.J. Lipid Res, 2012. Vol 53, 1864-1876  

13.Molecular Cell, 2012. Vol 39, 247- 258 

14.CELL, 2012. Vol 149, 214-231

15.Experimental hematology. 2012. 40 (4): 342-355

16.PLoS ONE. 2012. 7 (12): e50545

17.PLoS Genetics. 2012. 8 (9): e1002948

18.European Journal of Cell Biology. 2012. 91 (11-12): 950-960

19.Biochemical and Biophysical Research communications, 2013. 435 (3): 403-407

20. The American Society for Biochemistry and Molecular Biology, 2013. Doi: 10.1074/jbc.M113.486753

21.Molecular Microbiology, 2013. 89 (4): 660-675

22.Proceedings of the National Academy of Sciences, 2013. 110 (9): 3339-3344

23.Molecular Cell, 2013. 51 (2): 265-272

24.Molecular and Cellular Biology, 2013. 33 (8): 1487-1502

25.PLoS ONE, 2013. 8 (6): e64953

26.Nature Methods, 2013. 10 (7): 634-637