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1 Citations 7 Q&As
Facts about Synaptosomal-associated protein 23.
Human | |
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Gene Name: | SNAP23 |
Uniprot: | O00161 |
Entrez: | 8773 |
Belongs to: |
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SNAP-25 family |
HsT17016; SNAP23; SNAP-23; SNAP23A; SNAP23B; synaptosomal-associated protein 23; synaptosomal-associated protein, 23kD; synaptosomal-associated protein, 23kDa; Vesicle-membrane fusion protein SNAP-23
Mass (kDA):
23.354 kDA
Human | |
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Location: | 15q15.1-q15.2 |
Sequence: | 15; NC_000015.10 (42491244..42533061) |
Ubiquitous. Highest levels where found in placenta.
Cell membrane; Peripheral membrane protein. Cell membrane; Lipid-anchor. Cell junction, synapse, synaptosome. Mainly localized to the plasma membrane.
The SNAP23 Marker has been validated by Boster on multiple platforms with both known positive and negative samples. This confirms its high affinity and specificity. As an added incentive, Boster offers rewards for the first person to review the product and receive a product credit. Boster rewards scientists world-wide for their product reviews and feedback. In the end, the boster SNAP23 Marker is an excellent choice for your next study.
SNAP23 is a novel target in cellular signaling. It is a component of the general membrane fusion machinery, a family of SNAP proteins that play important roles in transport vesicle docking. It interacts with other proteins such as DOC2alpha, kinesin 5B, and rootletin, which help regulate vesicle docking and transport in cells.
The SNAP23 gene has two versions, one of which lacks an internal exon. The variant 2 retains the same reading frame as variant one, but lacks an internal exon six. The missing region is required for nonspecific binding of the protein to plasma membranes. The SNAP-23 gene is also a part of the SNAP-23 gene family.
SNAP-23 is a nonneuronal homologue of SNAP25, which is a target SNARE found in the plasma membrane and intracellular membranes. SNAP23 has been implicated in exocytosis, whereas SNAP25 is primarily found in neuronal cells. Its role in exocytosis is unknown, but it is known to play a role in docking and fusion of transport vesicles.
SNAP23 is a key regulator of synaptin and syntaxin fusion, and is required for the association of SNAP-25 with syntaxin. This fusion requires a membrane-proximal region of syntaxin. A soluble GST fusion protein that lacks this region was not able to bind SNAP-23. This result is consistent with the hypothesis that synaptotagmin may trigger fusion of SNAP-23 and syntaxin-23.
The expression of SNAP23 is closely associated with the activity of OGT. In order to investigate this relationship, we studied the effect of OGT on the secretion of exosomes in a cancer cell line. In the model, OGT decreased the release of exosomes, which was found to be correlated with the level of SNAP-23. To determine whether this association between SNAP23 and OGT is causal, we transfected SKOV3 cells with NC or SNAP-23 siRNA. We also assessed the effects of cisplatin treatment on exosome release in the OGT sh group.
These results indicate that SNAP23 is downregulated by OGD. This phenomenon is likely related to the decreased levels of SNAP-23, a gene that is found in neutrophilic granulocytes that are attracted to skin wounds. In addition, these cells express higher levels of ALIX than normal, which suggests that the overexpression of SNAP-23 is related to cancer progression.
Downregulation of OGT increases the efflux of chemotherapy drugs, including cisplatin. This increases drug efflux, which reduces the cell's damage from chemotherapy. Accordingly, the expression of SNAP23 in serum of drug-resistant patients was higher than that of drug-sensitive patients. Furthermore, downregulation of OGT increased cisplatin efflux and reduced the intracellular concentration in OGT-knocked-down cells. Furthermore, cisplatin resistance in OGT-knocked-down cells was higher than that of drug-sensitive patients. As a result, the efflux of cisplatin seems to be faster and more direct, despite the increased toxicity in the drug-resistant cell line.
SNAP23 is a key mediator of autophagosome-lysosome fusion. It also associates with intracellular compartments rich in PE and is anchored to the PM. In response to pancreatitis stimuli, SNAP23 is relocalized to autolysosomes. It also participates in the formation of the SNAP23-STX17 SNARE complex and is involved in basolateral exocytosis.
SNAP23 is a ubiquitous SNAP25 isoform that mediates exocytosis in many non-neuronal cells, including pancreatic acini. It interacts with Stx-3 and Stx-4 on SGs and PMs to form distinct SM/SNARE complexes that regulate basal exocytosis and SG-SG fusion.
In addition, Stx-1A and Stx-3 colocalize with SNAP23. Moreover, the receptor for insulin was found in the SNAP23-Stx4-VAMP8 complex. Interestingly, the SNAP23-mCherry protein surfaced to its native location in the PM when incubated with 16.7 mM glucose plus 10 nM GLP-1. Moreover, it was not trapped inside the Golgi complex.
Stx-1A and Stx-3 inhibit the formation of SM/SNARE complexes by preventing SNAP23 from translocating to intracellular vesicles. Both SNAP25 and SNAP23 inhibit autophagy. The results of these experiments support the hypothesis that SNAP23 and SNAP25 are co-targeted and compete for autophagy.
The Boster Bio company offers high-affinity primary antibodies. Boster antibodies have been extensively cited in the scientific literature over the last 25 years and are a reputable source of antibodies in the research community. Their antibodies are validated for use in Western Blotting (WB) as well as immunohistochemistry and ELISA. In addition to their ubiquitin-conjugated and monoclonal antibodies, Boster also offers a specialized line of antibodies, as well as custom services.
The Boster company offers over 16,000 monoclonal antibodies, and more than 10,000 IHC and WB-validated polyclonal antibodies. All Boster antibodies have undergone rigorous testing against a panel of 250 tissues and cells to ensure high affinity and specificity. They are also validated quantitatively against recombinant proteins and untransfected cell lines. Boster Bio also rewards the first reviewer with product credits.
Boster Bio has been manufacturing antibodies for 25 years. Their products have a Boster Quality Guarantee that ensures they will work as advertised. Additionally, the Boster Bio Anti-Rap 2C antibody is validated on WB and ELISA. The company's products have received over 23,000 citations and are covered by Boster's quality guarantee. The company's product line is growing each month.
During the validation, we evaluated a set of tissues fixed in formalin, embedded in paraffin, and stained with the SNAP23 marker. Positive staining in these tissues was confirmed by IHC. We also tested the immunofluorescence of MSI2 and HMGA2.
The Boster Bio SNAP23 marker is based on human syndet, a gene that encodes a transcription factor involved in neuronal cell death. The marker has been validated on Immunofluorescence. To validate the SNAP23 marker, cell lysates were fixed, permeabilized with 0.1% Triton X-100 for 15 min, and incubated with anti-LC3, anti-HMG-ABC, and anti-S100b/MSI2. The fixed cells were then analysed by confocal microscopy. The cells were also subjected to TUNEL assays.
PMID: 8663154 by Ravichandran V., et al. Identification of a novel syntaxin- and synaptobrevin/VAMP-binding protein, SNAP-23, expressed in non-neuronal tissues.
PMID: 9070898 by Mollinedo F., et al. Identification of two isoforms of the vesicle-membrane fusion protein SNAP-23 in human neutrophils and HL-60 cells.
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