Adducin alpha Phospho (pS436) (ADD1) antibody 
RabMAb®
Cat.#: 3664-1
Rabbit Monoclonal Antibody
Swiss Prot: P35611
Mol Weight: 130kDa
Price: $285*
Availability: Ship next business day
Description
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 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).
Recommended Applications
WB
Applications and Recommended Dilution Factors
WB: 1:1,000 - 10,000
Species Reactivity *
Human, Mouse, Rat
*Species cross-reactivity is based on WB analysis
Products Data
 |
| Western blot analysis on HeLa cell lysates using anti-Phospho-Adducin alpha (pS436) RabMAb (cat. #3664-1). Cells were either (A) untreated (B) treated with Lambda Phosphatase. |
Specificity
A phospho specific peptide corresponding to residues surrounding Serine 436 of human Adducin alpha was used as an immunogen. This antibody only detects Adducin alpha phosphorylated at Serine 436.
Storage Condition and Buffer
Store at -20 °C. Buffer: Antibody buffer, sodium azide, glycerol, and BSA. Stable for 12 months from date of receipt.
Alternative Names
ADD1 antibody, ADDA antibody, MGC3339 antibody, MGC44427 antibody, Alpha-adducin antibody, Erythrocyte adducin subunit alpha antibody
Description References
1. Gardner K, Bennett V., J Biol Chem 261:1339-1348, 1986.
2. Kuhlman PE, et al. J Biol. Chem, 271: 7986-7991, 1996.
3. Dong, LC, et al. J Biol Chem 270: 25534-25540, 1995.
4. Palfrey HC, et al. J Biol Chem. 260:16021-16029, 1985.
5. Fukata, et al. J Cell Biol, 145:347-361, 1995.
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