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Validated All-in-One™ qPCR Primer for ANXA6(NM_001155.4) Search again
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
Summary
Annexin VI belongs to a family of calcium-dependent membrane and phospholipid binding proteins. Although their functions are still not clearly defined, several members of the annexin family have been implicated in membrane-related events along exocytotic and endocytotic pathways. The annexin VI gene is approximately 60 kbp long and contains 26 exons. It encodes a protein of about 68 kDa that consists of eight 68-amino acid repeats separated by linking sequences of variable lengths. It is highly similar to human annexins I and II sequences, each of which contain four such repeats. Exon 21 of annexin VI is alternatively spliced, giving rise to two isoforms that differ by a 6-amino acid insertion at the start of the seventh repeat. Annexin VI has been implicated in mediating the endosome aggregation and vesicle fusion in secreting epithelia during exocytosis. [provided by RefSeq].
Gene References into function
- Data show that annexin 6 is a candidate receptor for chondroitin sulfate chains.
- Characterization of phosphorylation-mimicking mutant annexin VI (T356D) reveals a potential regulatory mechanism leading to a higher degree of flexibility and possibly a higher calcium binding affinity of annexin VI upon phosphorylation.
- The nucleotide-binding site of ANXA6 is formed by the amino acid residues located in both halves of the protein, in two distinct domains.
- cell surface annexin VI may function as an acidic pH binding site or receptor and may also function as a co-receptor with LRP-1 at neutral pH
- endogenous annexin 6 could regulate the Maxi-chloride channel in placenta
- TPD52 bound to annexin VI in a Ca(2+)-dependent manner suggesting that these molecules may act in concert to regulate secretory processes in plasma cells
- Macrophage reprogramming during oxidative stress occurs through the cytosolic mobilization of annexin VI from lipid rafts.
- It is a first report supporting the hypothesis of a direct implication of AnxA6 in vitamin A-dependent tissue mineralization.
- Annexin A6 has roles in alterations in cholesterol transport and caveolin export from the Golgi complex
- analysis of the pH-induced membrane binding of annexins A6 and A2-S100A10
- analysis of translocation and assembly at the plasma membrane and the nuclear envelope
- AnxA6 interferes with caveolin transport through the inhibition of cPLA(2).
- annexin A6 contributes to the calcium-dependent cell surface exposition of the membrane associated-S100A8/A9 complex
