Phosphoserine Antikörper (Atto 390)
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- Target Alle Phosphoserine Produkte
- Phosphoserine
- Reaktivität
- Bitte anfragen
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Wirt
- Kaninchen
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Klonalität
- Polyklonal
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Konjugat
- Dieser Phosphoserine Antikörper ist konjugiert mit Atto 390
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Applikation
- Western Blotting (WB), ELISA, Immunoprecipitation (IP), Immunohistochemistry (IHC), Immunocytochemistry (ICC), Immunofluorescence (IF)
- Spezifität
- Detects proteins phosphorylated on serine residues. Does not cross-react with phosphotyrosine.
- Aufreinigung
- Peptide Affinity Purified
- Immunogen
- Phosphoserine conjugated to KLH, and phosvitin mixture
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- Applikationshinweise
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- WB (1:500)
- ICC/IF (1:50)
- ELISA (1:250)
- IP (1:100)
- optimal dilutions for assays should be determined by the user.
- Kommentare
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2 μg/ml of ABIN2486250 was sufficient for detection of phosphorylation signal in western blot analysis using human MMRU cells treated with 0.1 μM okadaic acid.
- Beschränkungen
- Nur für Forschungszwecke einsetzbar
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- Format
- Liquid
- Konzentration
- 0.25 mg/mL
- Buffer
- PBS, 50 % glycerol, 0.01 % sodium azide, Storage buffer may change when conjugated
- Konservierungsmittel
- Sodium azide
- Vorsichtsmaßnahmen
- This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
- Lagerung
- 4 °C
- Informationen zur Lagerung
- Conjugated antibodies should be stored at 4°C
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- Target
- Phosphoserine
- Abstract
- Phosphoserine Produkte
- Substanzklasse
- Amino Acid
- Hintergrund
- Protein phosphorylation is an important posttranslational modification that serves many key functions to regulate a protein's activity, localization, and protein-protein interactions. Phosphorylation is catalyzed by various specific protein kinases, which involves removing a phosphate group from ATP and covalently attaching it to to a recipient protein that acts as a substrate. Most kinases act on both serine and threonine, others act on tyrosine, and a number (dual specificity kinases) act on all three. Because phosphorylation can occur at multiple sites on any given protein, it can therefore change the function or localization of that protein at any time (1). Changing the function of these proteins has been linked to a number of diseases, including cancer, diabetes, heart disease, inflammation and neurological disorders (2-4).
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