anti- PLEKHA1 antibody
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Description
Binds specifically to phosphatidylinositol 3,4-diphosphate(PtdIns3,4P2), but not to other phosphoinositides. May recruit other proteins to the plasma membrane.
Documents del producto
Product specifications
| Category | Primary Antibodies |
| Immunogen Target | pleckstrin homology domain containing, family A(phosphoinositide binding specific) member 1 |
| Host | Rabbit |
| Reactivity | human,mouse,rat |
| Recommended Dilution | WB: 1:500-1:2000; IHC: 1:20-1:200 |
| Clonality | polyclonal |
| Conjugation | Unconjugated |
| Isotype | IgG |
| Observed MW | 46 kDa |
| Purity | ≥95% as determined by SDS-PAGE |
| Purification | Immunogen affinity purified |
| Size 1 | 100µg |
| Form | liquid |
| Tested Applications | ELISA, WB, IHC |
| Storage | PBS with 0.02% sodium azide and 50% glycerol pH 7.3,-20℃ for 12 months(Avoid repeated freeze / thaw cycles.) |
| UniProt ID | Q9HB21 |
| Gene ID | 59338 |
| Alias | PLEKHA1, TAPP1, PH domain-containing family A member 1,Tandem PH domain-containing protein 1 |
| Background | Antibody anti-PLEKHA1 |
| Status | RUO |
| Note | This product is for research use only. |
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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