Phosphothreonine anticorps (FITC)

N° du produit ABIN2486277

Détail du produit anti-Phosphothreonine anticorps (FITC)

Antigène: Phosphothreonine

Hôte: Lapin

Clonalité: Polyclonal

Conjugué: Cet anticorp Phosphothreonine est conjugé à/à la FITC

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

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

Purification: Peptide Affinity Purified

Immunogène: Phosphothreonine conjugated to KLH

Information d'application

Indications d'application:

• WB (1:500)
• ICC/IF (1:60)
• ELISA (1:2000)
• IP (1:100)
• optimal dilutions for assays should be determined by the user.

Commentaires:

2 μg/ml of ABIN2486277 was sufficient for detection of phosphorylation signal in western blot analysis using mouse spleen extract treated with Vanadium.

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 Phosphothreonine

Antigène: Phosphothreonine

Abstract: Phosphothreonine Produits

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).