Phosphoserine antibody (Atto 390)

Catalog No. ABIN2486250

Product Details anti-Phosphoserine Antibody (Atto 390)

Target: Phosphoserine

Reactivity: Please inquire

Host: Rabbit

Clonality: Polyclonal

Conjugate: This Phosphoserine antibody is conjugated to Atto 390

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

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

Purification: Peptide Affinity Purified

Immunogen: Phosphoserine conjugated to KLH, and phosvitin mixture

Application Details

Application Notes:

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

Comment:

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

Handling

Format: Liquid

Concentration: 0.25 mg/mL

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

Preservative: Sodium azide

Precaution of Use: This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

Storage: 4 °C

Storage Comment: Conjugated antibodies should be stored at 4°C

Target Details for Phosphoserine

Target: Phosphoserine

Abstract: Phosphoserine Products

Target Type: Amino Acid

Background: 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).