Adducin alpha (pSer59) antibody

Antigen: Adducin alpha

Binding Site: pSer59

Clonality: Monoclonal

Host: Rabbit

Reactivity: Human

Application: Western Blotting (WB), Immunoprecipitation (IP)

Certificates: ISO 9001:2008

Catalog no.: ABIN649256

Additional Information

Gene ID: 118

UniProt: P35611

Description: Other names: ADD1, ADDA, Alpha-adducin, Erythrocyte adducin subunit alpha

Characteristics: Rabbit Monoclonal Antibody

Specificity: A synthetic phospho-peptide corresponding to residues surrounding Ser59 of human alpha Adducin was used as an immunogen. The antibody only detects alpha Adducin phosphorylated on Serine 59.

Molecular Weight: 115 kDA

Comments:

Background: Alpha adducin is a 80-120 kD member of the aldolase class II family and adducin subfamily. Adducin is a membrane skeletal protein that binds to actin filaments (F-actin) and promotes the association of spectrin with F-actin to form a spectrin-actin meshwork beneath plasma membranes (1-2). Adducin is a heterodimeric protein that consists of related subunits, α, and β,, or α, and γ, subunits (3). Adducin binds with high affinity to Ca(2+)/calmodulin and is a substrate for protein kinase C (PKC), and protein kinase A (PKA) (4). PKA specifically phosphorylates Ser59, Ser408, Ser436, and Ser481 located in the neck domain of alpha Adducin. Phosphorylation of Adducin alpha by Rho-kinase at Thr445 and Thr480 enhances the F-actin-binding activity of Adducin alpha (5).

Application Details

Application Notes: The suggested dilution is: WB: ~~ 1:1000~10000 IP: ~~ 1:40

Buffer: 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.

Storage: Adducin alpha Antibody Phospho (pS59) can be stored at -20°C for up to 12 months from time of receipt.

Research Area: Signaling, Phospho-specific antibodies, Protein Modifications, Cell Structure

Restrictions: For Research Use only

Publications

Product: Kuhlman, Hughes, Bennett et al.: "A new function for adducin. Calcium/calmodulin-regulated capping of the barbed ends of actin filaments." in: The Journal of biological chemistry, Vol. 271, Issue 14, pp. 7986-91, 1996 (PubMed).