VASP (phospho Ser157) Antibody | 79-198

VASP (phospho Ser157) Antibody | 79-198 | Gentaur UK, US & Europe Distribution

Host: Rabbit

Reactivity: Human, Mouse

Homology: N/A

Immunogen: VASP (Phospho-Ser157) antibody was raised against a peptide sequence around phosphorylation site of serine 157 (R-V-S (p) -N-A) derived from Human VASP.

Research Area: Phospho-Specific

Tested Application: WB, IHC

Application: Western Blot: 1:500~1:1000, Immunohistochemistry: 1:50~1:100

Specificiy: This antibody detects endogenous level of VASP only when phosphorylated at serine 157.

Positive Control 1: N/A

Positive Control 2: N/A

Positive Control 3: N/A

Positive Control 4: N/A

Positive Control 5: N/A

Positive Control 6: N/A

Molecular Weight: 50 kDa

Validation: N/A

Isoform: N/A

Purification: Antibodies were purified by affinity-chromatography using epitope-specific phosphopeptide. Non-phospho specific antibodies were removed by chromatogramphy using non-phosphopeptide.

Clonality: Polyclonal

Clone: N/A

Isotype: N/A

Conjugate: Unconjugated

Physical State: Liquid

Buffer: Antibody supplied in phosphate buffered saline (without Mg2+ and Ca2+) , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.

Concentration: 1 mg/mL

Storage Condition: Store antibody at -20˚C for up to one year.

Alternate Name: STAT5,

User Note: N/A

BACKGROUND: Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance, lamellipodial and filopodial dynamics, platelet activation and cell migration. VASP promotes actin filament elongation. It protects the barbed end of growing actin filaments against capping and increases the rate of actin polymerization in the presence of capping protein. VASP stimulates actin filament elongation by promoting the transfer of profilin-bound actin monomers onto the barbed end of growing actin filaments. Plays a role in actin-based mobility of Listeria monocytogenes in host cells. Regulates actin dynamics in platelets and plays an important role in regulating platelet aggregation.