ITK0020
ITK0020
ITK0020
from
$618.00
Price in reward points: 618
- Catalog: ITK0020
- Gene/Protein: Lysine
- Product Description: Immunotag™ Acetyl Lys proteins Polyclonal Antibody
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Description
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Specifications
Antibody Specification Datasheet 
IMPORTANT NOTE This product is custom manufactured with a lead time of 3-4 weeks. Once in production, this item cannot be cancelled from an order and is not eligible for return. Target Protein Lysine Clonality Polyclonal Storage/Stability -20°C/1 year Application WB,IHC-p,IF,ELISA Recommended Dilution WB: 1:500-1:2000, IHC-p: 1:100-300 EIA: 1:20000 Concentration 1 mg/ml Reactive Species Human,Mouse,Rat,Monkey Host Species Rabbit Immunogen Synthesized acetyl-peptide derived from human acetylation Lys proteins. Specificity Acetyl-Lys proteins Polyclonal Antibody detects endogenous levels of acetylated Lys proteins. Purification The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen Form Liquid in PBS containing 50% glycerol, 05% BSA and 002% sodium azide Gene Name Lysine Description 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. Usage For Research Use Only! Not for diagnostic or therapeutic procedures. - Reviews
| Antibody Specification | |
| Datasheet | |
| IMPORTANT NOTE | This product is custom manufactured with a lead time of 3-4 weeks. Once in production, this item cannot be cancelled from an order and is not eligible for return. |
| Target Protein | Lysine |
| Clonality | Polyclonal |
| Storage/Stability | -20°C/1 year |
| Application | WB,IHC-p,IF,ELISA |
| Recommended Dilution | WB: 1:500-1:2000, IHC-p: 1:100-300 EIA: 1:20000 |
| Concentration | 1 mg/ml |
| Reactive Species | Human,Mouse,Rat,Monkey |
| Host Species | Rabbit |
| Immunogen | Synthesized acetyl-peptide derived from human acetylation Lys proteins. |
| Specificity | Acetyl-Lys proteins Polyclonal Antibody detects endogenous levels of acetylated Lys proteins. |
| Purification | The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen |
| Form | Liquid in PBS containing 50% glycerol, 05% BSA and 002% sodium azide |
| Gene Name | Lysine |
| Description | 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. |
| Usage | For Research Use Only! Not for diagnostic or therapeutic procedures. |