Pleckstrin Homology Domain-Containing Family A Member 6 (PLEKHA6) Antibody
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Description
PEPP3 contains an N-terminal pleckstrin homology (PH) domain. It shares significant homology with PEPP1 and PEPP2 only in the PH domain.
Documents del producto
Product specifications
| Category | Primary Antibodies |
| Immunogen Target | Pleckstrin Homology Domain-Containing Family A Member 6 (PLEKHA6) |
| Host | Rabbit |
| Reactivity | Human |
| Recommended Dilution | WB: 1/1000. Optimal dilutions/concentrations should be determined by the end user. |
| Clonality | Polyclonal |
| Conjugation | Unconjugated |
| Isotype | IgG |
| Purification | Purified through a protein A column, followed by peptide affinity purification. |
| Size 1 | 80 µl |
| Size 2 | 400 µl |
| Form | Liquid |
| Tested Applications | ELISA, WB |
| Buffer | PBS containing 0.09% sodium azide. |
| Availability | Shipped within 5-10 working days. |
| Storage | Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles. |
| Dry Ice | No |
| UniProt ID | Q9Y2H5 |
| Alias | KIAA0969, PEPP3,PH domain-containing family A member 6,Phosphoinositol 3-phosphate-binding protein 3,PEPP-3 |
| Background | Antibody anti-PLEKHA6 |
| Status | RUO |
| Note | Concentration: 0.34 mg/ml - |
Descripción
PLEKHA6 is a member of the pleckstrin homology (PH) domain-containing protein family that interacts with phosphoinositides, enabling its recruitment to plasma and endosomal membranes for the regulation of intracellular signaling and vesicle trafficking. It functions as a scaffold protein that coordinates the localization and activity of signaling molecules involved in cytoskeletal dynamics, endocytosis, and cellular adhesion. PLEKHA6 is expressed in epithelial, endothelial, and immune cells, where it regulates processes like cell migration, polarity, and tissue remodeling. Dysregulation of PLEKHA6 has been implicated in cancer metastasis and inflammatory disorders due to its role in actin reorganization and cell adhesion dynamics. Knockout studies demonstrate defects in membrane trafficking, impaired cellular adhesion, and reduced migration, highlighting its essential role in coordinating phosphoinositide-mediated signaling pathways, cytoskeletal organization, and cellular polarity.
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