Phosphoserine anticorps (Atto 390)

N° du produit ABIN2486250

Cet anticorps Lapin Polyclonal détecte spécifiquement Phosphoserine dans WB, ELISA, IP, IHC, ICC et IF. Il présente une réactivité envers .

Aperçu rapide pour Phosphoserine anticorps (Atto 390) (ABIN2486250)

Antigène: Phosphoserine

Reactivité: Veuillez nous consulter SVP

Hôte: Lapin

Clonalité: Polyclonal

Conjugué: Cet anticorp Phosphoserine est conjugé à/à la Atto 390

Application: Western Blotting (WB), ELISA, Immunoprecipitation (IP), Immunohistochemistry (IHC), Immunocytochemistry (ICC), Immunofluorescence (IF)

Détail du produit anti-Phosphoserine anticorps (Atto 390)

Specificité: Detects proteins phosphorylated on serine residues. Does not cross-react with phosphotyrosine.

Purification: Peptide Affinity Purified

Immunogène: Phosphoserine conjugated to KLH, and phosvitin mixture

Information d'application

Indications d'application:

• WB (1:500)
• ICC/IF (1:50)
• ELISA (1:250)
• IP (1:100)
• optimal dilutions for assays should be determined by the user.

Commentaires:

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.

Restrictions: For Research Use only

Stockage

Format: Liquid

Concentration: 0.25 mg/mL

Buffer: PBS, 50 % glycerol, 0.01 % sodium azide, Storage buffer may change when conjugated

Agent conservateur: Sodium azide

Précaution d'utilisation: This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

Stock: 4 °C

Stockage commentaire: Conjugated antibodies should be stored at 4°C

Détails sur Phosphoserine

Antigène: Phosphoserine

Classe de substances: Amino Acid

Sujet: 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).