|
ORF cDNA clones
|
CRISPR / TALEN
|
Lentivirus
|
AAV
|
TALE-TF
|
ORF knockin clones
|
|
Antibody
|
Proteins
|
miRNA target clones
|
qPCR primers
|
shRNA clones
|
miRNA products
|
Promoter clones
|
Validated All-in-One™ qPCR Primer for SNAP23(NM_003825.3) 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
Specificity of vesicular transport is regulated, in part, by the interaction of a vesicle-associated membrane protein termed synaptobrevin/VAMP with a target compartment membrane protein termed syntaxin. These proteins, together with SNAP25 (synaptosome-associated protein of 25 kDa), form a complex which serves as a binding site for the general membrane fusion machinery.
Gene References into function
- SNAP-23 and syntaxin-4 are expressed in human eosinophils and are likely candidates for association with VAMP-2 during docking, which is followed by exocytosis.
- cleaved by calpain in activated platelets
- CFTR-mediated chloride currents are inhibited by introducing excess SNAP-23 into HT29-Cl.19A epithelial cells.
- A synaptosome-associated protein of 23 kDa(SNAP23), the ubiqitously expressed homologue of SNAP25, has been shown to interact directly with ubiquitous kinesin heavy chain (uKHC).
- Palmitoylated peptides from the cysteine-rich domain of this protein cause membrane fusion depending on peptide length, position of cysteines, and extent of palmitoylation.
- an examination of the homotetrameric structure of the N-terminal domain of this protein
- studies show that synaptosomal-associated protein-23 is phosphorylated in platelets during cell activation through a protein kinase C-related mechanism at two or more sites
- Because SNAP-23 plays a central role in SNAREs complex formation, it was chosen to examine possible functional implications of the SNARE system in plasma cell Ig secretion.
- expression of SNAP-23 and syntaxin-2 on the extracellular surface of the platelet plasma membrane.
- SNAP-23 is not essential for constitutive exocytosis of secreted alkaline phosphatase
- The expression of the SNARE protein SNAP-25 and its cellular homologue SNAP-23, as well as syntaxin1 and VAMP (vesicle-associated membrane protein) in samples of normal parathyroid tissue, chief cell adenoma, and parathyroid carcinoma, was examined.
- Overexpression of a dominant negative SNAP-23 mutant suppressed expression of P-selectin, CD40L, CD41, CD61, release from dense granules and platelet aggregation
