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Description
The cAMP-dependent Protein Kinase (PKA) is compartmentalized within the cell. To maintain the localization of PKA, the regulatory subunits interact with specific anchoring proteins. Several proteins have been identified as PKA anchoring proteins and form a family named AKAP (A-Kinase Anchor Proteins). Fifteen of the AKAP proteins contain a consensus binding motif that allows interaction with the type II regulatory subunit (RII) of the PKA holoenzyme. In addition, three other AKAPs (D-AKAP1, D-AKAP2, and fsc1/AKAP82) can associate with the type I regulatory subunit (RI) of the PKA holoenzyme. AKAP82 was isolated as a component of the mouse sperm fibrous sheath. It is a dual specificity AKAP that contains an RII-binding domain (domain A; amino acids 219 to 232) and an RI-binding domain (domain B; amino acids 335-344). In mouse, pro-AKAP82 is synthesized as a 97 kDa precursor that is transported to the flagellum where proteolytic cleavage of the N-terminal 179 amino acids produces AKAP82. Assembly of AKAP82 into the fibrous sheath surrounding the axoneme of the sperm flagellum is thought to tether PKA close to the axoneme where it can regulate flagellar motility.
Specifications
Specifications
| Antigen | AKAP82 |
| Applications | Western Blot |
| Classification | Monoclonal |
| Clone | 25 |
| Concentration | 250μg/mL |
| Conjugate | Unconjugated |
| Formulation | Aqueous buffered solution containing BSA, glycerol, and ≤0.09% sodium azide. |
| Host Species | Mouse |
| Immunogen | Mouse AKAP82 aa. 555-675 |
| Purification Method | Affinity Purified |
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