Adducin alpha Antibody (C-term)
Rabbit Monoclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application ![]()
| WB, IHC, IF |
---|---|
Primary Accession | P35611 |
Reactivity | Human, Mouse |
Host | Rabbit |
Clonality | Monoclonal |
Clone Names | EP734Y |
Calculated MW | 80955 Da |
Gene ID | 118 |
Other Names | Alpha-adducin, Erythrocyte adducin subunit alpha, ADD1, ADDA |
Target/Specificity | A synthetic peptide corresponding to residues in the C-term of human Adducin was used as immunogen. |
Dilution | WB~~1:500~1000 IHC~~1:250~500 |
Format | 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | Adducin alpha Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | ADD1 |
---|---|
Synonyms | ADDA |
Function | Membrane-cytoskeleton-associated protein that promotes the assembly of the spectrin-actin network. Binds to calmodulin. |
Cellular Location | Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein; Cytoplasmic side |
Tissue Location | Expressed in all tissues. Found in much higher levels in reticulocytes than the beta subunit |

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Provided below are standard protocols that you may find useful for product applications.
Background
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). Phosphorylation of adducing alpha by Rho-kinase at Thr445 and Thr480 enhances the F-actin-binding activity of adducing alpha (5).
References
1. Gardner, K.; Bennett, V. : J. Biol. Chem. 261: 1339-1348, 1986.
2. Kuhlman, P.A., C.A. Hughes, V. Bennett, and V.M. Fowler. 1996. J. Biol. Chem. 271: 7986-7991
3. Dong, L., C. Chapline, B. Mousseau, L. Fowler, K. Ramsay, J.L. Stevens, and S. Jaken. 1995. J. Biol. Chem. 270: 25534-25540
4. Palfrey, H. C., Waseem, A. (1985) J. Biol. Chem. 260, 16021-16029
5. Fukata et al. J. Cell Biol., Volume 145, Number 2, April 19, 1999 347-361

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