ANXA9 antibody
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Description
Low affinity receptor for acetylcholine known to be targeted by disease-causing pemphigus vulgaris antibodies in keratinocytes.
Documents del producto
Product specifications
| Category | Primary Antibodies |
| Immunogen Target | annexin A9 (ANXA9) |
| Host | Rabbit |
| Reactivity | Human, Mouse |
| Recommended Dilution | WB: 1:200-1:1000; IHC: 1:50-1:500; IF: 1:10-1:100 |
| Clonality | polyclonal |
| Conjugation | Unconjugated |
| Isotype | IgG |
| Observed MW | 38 kDa |
| Purity | ≥95% as determined by SDS-PAGE |
| Purification | Immunogen affinity purified |
| Size 1 | 100µg |
| Form | liquid |
| Tested Applications | ELISA, WB, IHC, IF |
| Storage | PBS with 0.02% sodium azide and 50% glycerol pH 7.3, -20℃ for 12 months(Avoid repeated freeze / thaw cycles.) |
| UniProt ID | O76027 |
| Gene ID | 8416 |
| Alias | ANXA9,ANX31 |
| Background | Antibody anti-ANXA9 |
| Status | RUO |
| Note | Mol. Weight 38 kDa |
Descripción
ANXA9 is a unique member of the annexin family characterized by its calcium-independent phospholipid-binding activity. Unlike other annexins, ANXA9 can interact with cell membranes without requiring calcium ions, suggesting distinct roles in membrane organization and signal transduction. ANXA9 is expressed in epithelial tissues and has been associated with keratinocyte differentiation and epithelial homeostasis, where it contributes to processes such as membrane repair and cell adhesion. Emerging evidence links ANXA9 to cancer progression, where altered expression correlates with epithelial-mesenchymal transition (EMT), a critical process in metastasis. Its calcium-independent function and role in epithelial cell regulation make it a unique regulator of membrane stability and cancer biology.
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ANXA9 antibody
Low affinity receptor for acetylcholine known to be targeted by disease-causing pemphigus vulgaris antibodies in keratinocytes.
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Annexin A9 (ANXA9) Antibody
The annexins are a family of calcium-dependent phospholipid-binding proteins. Members of the annexin family contain 4 internal repeat domains, each of which includes a type II calcium-binding site. The calcium-binding sites are required for annexins to aggregate and cooperatively bind anionic phospholipids and extracellular matrix proteins. This gene encodes a divergent member of the annexin protein family in which all four homologous type II calcium-binding sites in the conserved tetrad core contain amino acid substitutions that ablate their function. However, structural analysis suggests that the conserved putative ion channel formed by the tetrad core is intact.
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