Lysine (lys) (methylated) anticorps
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- Antigène
- Lysine (lys)
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Épitope
- methylated
- Reactivité
- Veuillez nous consulter SVP
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Hôte
- Lapin
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Clonalité
- Polyclonal
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Conjugué
- Inconjugué
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Application
- Western Blotting (WB), Immunocytochemistry (ICC), Immunofluorescence (IF), Immunoprecipitation (IP), ELISA
- Specificité
- Detects proteins containing methylated lysine residues.
- Purification
- Protein A Purified
- Immunogène
- Methylated KLH Conjugated
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- Indications d'application
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- WB (1:20000)
- ICC/IF (1:200)
- optimal dilutions for assays should be determined by the user.
- Commentaires
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0.2-0.5 μg/ml of SPC-158 was sufficient for detection of the methylated histone by western blot analysis using melanoma cells in TBSt.
- Restrictions
- For Research Use only
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- Format
- Liquid
- Concentration
- 1 mg/mL
- Buffer
- PBS, 50 % glycerol, Storage buffer may change when conjugated
- Stock
- -20 °C
- Stockage commentaire
- -20°C
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-Characterization of pyruvate kinase from the anoxia tolerant turtle, Trachemys scripta elegans: a potential role for enzyme methylation during metabolic rate depression." dans: PeerJ, Vol. 6, pp. e4918, (2018) (PubMed).
: "Purification and Properties of White Muscle Lactate Dehydrogenase from the Anoxia-Tolerant Turtle, the Red-Eared Slider, Trachemys scripta elegans." dans: Enzyme research, Vol. 2013, pp. 784973, (2013) (PubMed).
: "Stable Suppression of Lactate Dehydrogenase Activity during Anoxia in the Foot Muscle of Littorina littorea and the Potential Role of Acetylation as a Novel Posttranslational Regulatory Mechanism." dans: Enzyme research, Vol. 2013, pp. 461374, (2013) (PubMed).
: "
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-Characterization of pyruvate kinase from the anoxia tolerant turtle, Trachemys scripta elegans: a potential role for enzyme methylation during metabolic rate depression." dans: PeerJ, Vol. 6, pp. e4918, (2018) (PubMed).
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- Antigène
- Lysine (lys)
- Autre désignation
- Lysine
- Synonymes
- anticorps lysine, anticorps lys
- Classe de substances
- Amino Acid
- Sujet
- 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).
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