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ELK Biotechnology
SKU:ES20844
Acetyl Kine rabbit pAb
Acetyl Kine rabbit pAb
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$250.00 USD
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Applications: WB
Reactivity: Species independent
Source: Rabbit
Dilution: WB: 1:1000-2000
Immunogen: Recombinant Protein of Acetyl Kine
Storage_stability: -20°C/1 year
Clonality: Polyclonal
Isotype: IgG
Other_name: YM3306
Background: Acetylation of lysine, like phosphorylation of serine, threonine or tyrosine, is an important reversible modification controlling protein activity. 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) .Signaling resulting in acetylation/deacetylation of histones, transcription factors, and other proteins affects a diverse array of cellular processes including chromatin structure and gene activity, cell growth, differentiation, and apoptosis.Recent proteomic surveys suggest that acetylation of lysine residues may be a widespread and important form of posttranslational protein modification that affects thousands of proteins involved in control of cell cycle and metabolism, longevity, actin polymerization, and nuclear transport.The regulation of protein acetylation status is impaired in cancer and polyglutamine diseases, and HDACs have become promising targets for anti-cancer drugs currently in development.
Reactivity: Species independent
Source: Rabbit
Dilution: WB: 1:1000-2000
Immunogen: Recombinant Protein of Acetyl Kine
Storage_stability: -20°C/1 year
Clonality: Polyclonal
Isotype: IgG
Other_name: YM3306
Background: Acetylation of lysine, like phosphorylation of serine, threonine or tyrosine, is an important reversible modification controlling protein activity. 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) .Signaling resulting in acetylation/deacetylation of histones, transcription factors, and other proteins affects a diverse array of cellular processes including chromatin structure and gene activity, cell growth, differentiation, and apoptosis.Recent proteomic surveys suggest that acetylation of lysine residues may be a widespread and important form of posttranslational protein modification that affects thousands of proteins involved in control of cell cycle and metabolism, longevity, actin polymerization, and nuclear transport.The regulation of protein acetylation status is impaired in cancer and polyglutamine diseases, and HDACs have become promising targets for anti-cancer drugs currently in development.
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