Recombinant Rat Vesicle-associated membrane protein 2 (Vamp2), partial

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中文名稱：

大鼠Vamp2重組蛋白
品名簡稱：

Recombinant Rat Vamp2 protein, partial
貨號：

CSB-EP025781RA1
說明書：

MSDS Datasheet
規(guī)格：

￥1836
圖片：
(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
其他：

產(chǎn)品詳情
產(chǎn)品評價
相關產(chǎn)品
靶點詳情

產(chǎn)品詳情

純度：

Greater than 85% as determined by SDS-PAGE.
基因名：

Vamp2
Uniprot No.：

P63045
別名：

Vamp2; Syb2; Vesicle-associated membrane protein 2; VAMP-2; Synaptobrevin-2
種屬：

Rattus norvegicus (Rat)
蛋白長度：

Partial
來源：

E.coli
分子量：

14.1 kDa
表達區(qū)域：

2-94aa
氨基酸序列

SATAATVPPAAPAGEGGPPAPPPNLTSNRRLQQTQAQVDEVVDIMRVNVDKVLERDQKLSELDDRADALQAGASQFETSAAKLKRKYWWKNLK
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.
蛋白標簽：

N-terminal 6xHis-tagged
產(chǎn)品提供形式：

Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
緩沖液：

Tris-based buffer,50% glycerol
儲存條件：

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
保質(zhì)期：

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
貨期：

3-7 business days
注意事項：

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA：

Please contact us to get it.

產(chǎn)品評價

靶點詳情

功能：

Involved in the targeting and/or fusion of transport vesicles to their target membrane. Major SNARE protein of synaptic vesicles which mediates fusion of synaptic vesicles to release neurotransmitters. Essential for fast vesicular exocytosis and activity-dependent neurotransmitter release as well as fast endocytosis that mediates rapid reuse of synaptic vesicles. Modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1.
基因功能參考文獻：
1. our findings show an intimate interaction between the dynamics of the VAMP2 transmembrane domains via the central glycine and the fluidity of the lipid membrane. In turn, this interaction influences greatly the likelihood and speed of fusion pore opening and expansion. PMID: 28588281
2. The ternary complex of syntaxin1:SNAP25:Munc18-1binds synaptobrevin with fast kinetics, resulting in the rapid formation of a fully zippered SNARE complex to which Munc18-1 remains tethered by the N-terminal domain of syntaxin1. PMID: 28483813
3. Syp1 clears Syb2 from the presynaptic active zone to prevent short-term depression. PMID: 26854222
4. These effects weaken the integrity of the outer membrane layer and are attributed mainly to the highly charged linker and juxtamembrane regions of sybII PMID: 26851777
5. miR-206 regulates lung surfactant secretion by limiting the availability of VAMP-2 protein. PMID: 25481410
6. distribution of SNAP25, VAMP1 and VAMP2 in adult deep cerebellar nuclei differs significantly from that found in newborn DCN and administration of E2 in the newborn DCN affected synaptic density and also changed their distribution PMID: 24534378
7. a novel interaction between SERT and a synaptic vesicle protein PMID: 24878716
8. In vivo silencing of VAMP2 but not VAMP3 in TALs blunted cAMP-stimulated steady-state surface NKCC2 expression and completely blocked cAMP-stimulated NKCC2 exocytic delivery PMID: 25008321
9. We suggest that VAMP-2 is the v-SNARE (vesicle SNARE) involved in regulated surfactant secretion. PMID: 22571236
10. The Ca2+-dependent transition in syntaxin 1A (Syx) involves zippering between the membrane-proximal juxtamembrane regions of Syx and VAMP2. PMID: 23641074
11. Block of Synaptobrevin Inhibits Endocytosis Induced by boiled tetanus toxin. PMID: 23643538
12. SNAP23-VAMP2 interaction plays a key role in cAMP-mediated exocytosis from parotid glands. PMID: 23380067
13. Amyloid-beta acts as a regulator of neurotransmitter release disrupting the interaction between synaptophysin and VAMP2 PMID: 22905234
14. a mechanism whereby fusion pore formation is induced by movement of the charged syb2 C-terminus within the membrane in response to pulling and tilting force PMID: 23009845
15. VAMP2, SNAP25b and syntaxin 1 characterize most cerebellar glutamatergic synapses and only one type of GABAergic synapse. PMID: 22094010
16. Dysregulation of SNARE complex and syt-1 in prefrontal cortex of adult-onset hypothyroidism can be restored by T(4) treatment. PMID: 21646859
17. Munc18-1 and the neuronal SNAREs (t-SNARE (syntaxin 1.SNAP-25) and v-/t-SNARE (VAMP2.syntaxin 1.SNAP-25) complexes) already have the inherent capability to function as a basic stage-specific off/on switch to control membrane fusion PMID: 21730064
18. Data show that most of the synaptobrevin SNARE motif has a remarkable reluctance to bind membranes. PMID: 21768342
19. Synaptophysin and synaptobrevin 2 were expressed in a dynamic manner during the development of rat cochlea PMID: 21556117
20. Data showv that complexin 2 interacts with vesicle-associated membrane protein (VAMP) 2, syntaxins 3 and 4. PMID: 20829354
21. In the incisor dental pulp, all nerve fibers display immunoreactivity for syntaxin-1, synaptosomal-associated protein (SNAP)-25, and vesicle-associated membrane protein (VAMP)-2. PMID: 20186959
22. the ability of sybII to support exocytosis is inhibited by addition of one or two residues to the sybII C terminus depending on their energy of transfer from water to the membrane interface, following a Boltzmann distribution PMID: 20937897
23. tomosyn controls synaptic vesicle fusion positively by serving as a placeholder for VAMP2. PMID: 20633536
24. Recombinant VAMP2 could serve as a replacement for VAMP2 synthetic peptide, potentially useful in endopeptidase assays for replacement of the currently used mouse bioassay for clostridial neurotoxins contaminating biotherapeutic products. PMID: 20005125
25. synaptobrevin 2 forms complexes with the plasma membrane-bound SNAREs syntaxin 1A and SNAP25 to initiate the fusion reaction. PMID: 12177041
26. Data suggest that synaptophysin I has multiple roles in neurotransmitter release, regulating VAMP2 availability for the soluble N-ethylmaleimide-sensitive factor attachment protein receptor complex and participating in the late steps of exocytosis. PMID: 12181340
27. VAMP2 mRNA is increased during nerve regeneration of the facial motor nucleus after axotomy. PMID: 12191731
28. Dimerization of synaptobrevin 2 in membranes is very weak, questioning any possible functional role for this association in vivo. PMID: 12501216
29. vesicle-associated membrane protein 2 is involved in secretion of polypeptides from the choroid plexus epithelium. PMID: 12559091
30. cytoplasmic domain of VAMP2 was found to be necessary for both the formation of VAMP2-SypI hetero-dimers and for VAMP2 sorting to SVs PMID: 14528015
31. Synaptobrevin-2 is present in approximately 35% of the taste cells in rat circumvallate taste buds and colocalizes with SNAP-25, serotonin, protein gene product 9.5. and type III inositol 1,4,5-triphosphate receptor. PMID: 14983476
32. Homodimerization of Vamp2 is mediated by its transmembrane segment. PMID: 15109254
33. Data suggest that VAMP2-dependent exocytosis regulates plasma membrane insertion of TRPC3 channels and contributes to carbachol-stimulation of Ca2+ influx. PMID: 15327778
34. cAMP increases NKCC2 surface expression by a mechanism involving VAMP and that NKCC2 trafficking to the apical membrane is involved in the stimulation of Tkidney medulla NaCl absorption by cAMP. PMID: 16144963
35. VAMP 2 is the most abundant isoform in the rat brain and is widely distributed PMID: 16169186
36. in astrocytes, a subpopulation of vesicles (tagged with a synaptobrevin2-EGFP chimera) is highly mobile and can fuse with the plasma membrane, at the level of the astrocyte processes, in a Ca2+-dependent manner PMID: 16322057
37. results show SNARE nucleation restricted to N-terminal portion; zippering proceeds in an N- to C-terminal direction; synaptobrevin binds rapidly to syntaxin/SNAP-25 acceptor; stabilizing syntaxin/SNAP-25 acceptor by a peptide allowed fast liposome fusion PMID: 16888141
38. Individual pancreatic acinar cells express VAMP 2-specific populations of zymogen granules that orchestrate the constitutive and calcium(2+)-regulated secretory pathways. PMID: 17272274
39. VAMP2 is expressed in muscle satellite cells and up-regulated during muscle regeneration. PMID: 17468895
40. Cleavage of synaptobrevin 2 by tetanus toxin, known to reduce neurotransmission, did not affect the respiratory response to K+, whereas the general excitability of d PC12 cells increased PMID: 18086678
41. analysis of SNARE mutations that cause a decrease in the ability of botulinum toxin-resistant synaptobrevin 2 to rescue regulated exocytosis in toxin-treated neuroendocrine cells PMID: 18508917
42. analysis of the substrate recognition mechanism of VAMP/synaptobrevin-cleaving clostridial neurotoxins PMID: 18511418
43. VAMP2 may contribute to the activity dependence of dense-core vesicles release PMID: 18542995
44. Findings suggest the involvement of VAMP2 in the development of skeletal muscles of somitic and non-somitic origins. PMID: 18570252
45. Results show that synaptophysin-containing cells co-expressed vesicular-associated membrane protein 2 and cholecystokinin. PMID: 19253017
46. 30 mW/cm(2) (SAR 14.1 W/kg) microwave radiation can result in the perturbation of the synaptic vesicles associated proteins: synapsin I, synaptophysin, VAMP-2, and syntaxin. PMID: 19603498
47. VAMP2, VAMP5, and VAMP7 may be involved in translocation of GLUT4 during muscle contractions. PMID: 19675279
48. Data suggest that VAMP2 modulates Kv2.1 inactivation by interfering with the interaction between the docking loop and C1a, a mechanism for gating regulation that may pertain also to other Kv channels. PMID: 19690160
49. Under appropriate conditions a docked state, mediated by trans-SNARE interactions, can be isolated that constitutes an intermediate in the fusion pathway. PMID: 19843696
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亞細胞定位：

Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass type IV membrane protein. Cell membrane.
蛋白家族：

Synaptobrevin family
組織特異性：

Nervous system specific. A higher level expression is seen in the brain as compared to the spinal cord. Expressed in hippocampal neurons.
數(shù)據(jù)庫鏈接：

KEGG: rno:24803

STRING: 10116.ENSRNOP00000054114

UniGene: Rn.12939