Pleckstrin Homology Domain-Containing Family A Member 4 (PLEKHA4) Antibody
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Description
PLEKHA4 binds specifically to phosphatidylinositol-3-phosphate (PtdIns3P), but not to other phosphoinositides.
Documents del producto
Product specifications
| Category | Primary Antibodies |
| Immunogen Target | Pleckstrin Homology Domain-Containing Family A Member 4 (PLEKHA4) |
| Host | Rabbit |
| Reactivity | Human |
| Recommended Dilution | WB: 1/1000, IHC-P: 1/10 - 1/50, FCM: 1/10 - 1/50. Not tested in IHC-F. 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, IHC, FCM |
| 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 | Q9H4M7 |
| Alias | PEPP1,PH domain-containing family A member 4,Phosphoinositol 3-phosphate-binding protein 1 |
| Background | Antibody anti-PLEKHA4 |
| Status | RUO |
Descripción
PLEKHA4 is a pleckstrin homology (PH) domain-containing protein that binds phosphoinositides, primarily PI(4,5)P2, to localize at plasma and endosomal membranes where it regulates intracellular signaling and membrane trafficking. It plays an important role in the Wnt/β-catenin signaling pathway by interacting with components like Dishevelled proteins, influencing cellular processes such as proliferation, differentiation, and development. PLEKHA4 is expressed in epithelial and immune tissues, where it is involved in actin cytoskeleton remodeling, cell polarity, and vesicular dynamics. Dysregulation of PLEKHA4 has been linked to cancer progression, particularly melanoma, where it enhances Wnt signaling and promotes tumor cell proliferation and migration. Knockdown studies show disrupted Wnt signaling, impaired membrane localization, and defects in actin organization, highlighting its role in phosphoinositide-mediated signaling and cytoskeletal regulation during development and tumorigenesis.
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