Pleckstrin Homology Domain Containing Family A, Member 1 (PLEKHA1) Antibody
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Description
Polyclonal Antibody to Pleckstrin Homology Domain Containing Family A, Member 1 (PLEKHA1).
Documents del producto
Product specifications
| Category | Primary Antibodies |
| Immunogen Target | Pleckstrin Homology Domain Containing Family A, Member 1 (PLEKHA1) |
| Host | Rabbit |
| Reactivity | Human |
| Recommended Dilution | WB: 0.01-2 µg/ml, IHC: 5-20 µg/ml, IF/ICC: 5-20 µg/ml. Optimal dilutions/concentrations should be determined by the end user. |
| Clonality | Polyclonal |
| Conjugation | Unconjugated |
| Purification | Purified by antigen-specific affinity chromatography, followed by Protein A affinity chromatography. |
| Size 1 | 100 µl |
| Size 2 | 200 µl |
| Size 3 | 1 ml |
| Form | Liquid |
| Tested Applications | WB, IHC, IF/ICC |
| Buffer | 0.01 M PBS, pH 7.4, containing 0.05% Proclin-300, 50% glycerol. |
| Availability | Shipped within 5-7 working days. |
| Storage | Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles. |
| Dry Ice | No |
| Alias | PLEKHA1, TAPP1, PH domain-containing family A member 1,Tandem PH domain-containing protein 1 |
| Background | Antibody anti-PLEKHA1 |
| Status | RUO |
Descripción
PLEKHA1 is a pleckstrin homology (PH) domain-containing protein that binds to phosphoinositides, particularly phosphatidylinositol 3-phosphate (PI3P), to regulate intracellular signaling and membrane trafficking. It plays a role in endosomal sorting, vesicle transport, and cellular localization of signaling proteins, linking membrane lipids to downstream effectors. PLEKHA1 is expressed in various tissues, including immune cells and epithelial tissues, where it participates in pathways controlling cell signaling, migration, and vesicular dynamics. Emerging evidence suggests that PLEKHA1 is involved in autophagy and receptor internalization processes, particularly in response to growth factor stimulation. Dysregulation of PLEKHA1 has been implicated in cancer progression and immune dysfunction due to defects in endosomal signaling and protein trafficking. Knockdown studies reveal disrupted endosome formation, impaired membrane dynamics, and altered cellular signaling, underscoring its role in phosphoinositide-mediated cellular processes and intracellular trafficking.
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