Recombinant Rat Vesicle-Associated Membrane Protein 2 (VAMP2) Protein (His)

Name: Recombinant Rat Vesicle-Associated Membrane Protein 2 (VAMP2) Protein (His)
Brand: Beta LifeScience
SKU: BLC-03469P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Rat Vesicle-Associated Membrane Protein 2 (VAMP2) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P63045
Target Symbol	VAMP2
Synonyms	Vamp2; Syb2; Vesicle-associated membrane protein 2; VAMP-2; Synaptobrevin-2
Species	Rattus norvegicus (Rat)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	SATAATVPPAAPAGEGGPPAPPPNLTSNRRLQQTQAQVDEVVDIMRVNVDKVLERDQKLSELDDRADALQAGASQFETSAAKLKRKYWWKNLK
Expression Range	2-94aa
Protein Length	Partial
Mol. Weight	14.1 kDa
Research Area	Cancer
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	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.
Subcellular Location	Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass type IV membrane protein. Cell membrane.
Protein Families	Synaptobrevin family
Database References	KEGG: rno:24803 STRING: 10116.ENSRNOP00000054114 UniGene: Rn.12939
Tissue Specificity	Nervous system specific. A higher level expression is seen in the brain as compared to the spinal cord. Expressed in hippocampal neurons.

Gene Functions References

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
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
Syp1 clears Syb2 from the presynaptic active zone to prevent short-term depression. PMID: 26854222
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
miR-206 regulates lung surfactant secretion by limiting the availability of VAMP-2 protein. PMID: 25481410
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
a novel interaction between SERT and a synaptic vesicle protein PMID: 24878716
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
We suggest that VAMP-2 is the v-SNARE (vesicle SNARE) involved in regulated surfactant secretion. PMID: 22571236
The Ca2+-dependent transition in syntaxin 1A (Syx) involves zippering between the membrane-proximal juxtamembrane regions of Syx and VAMP2. PMID: 23641074
Block of Synaptobrevin Inhibits Endocytosis Induced by boiled tetanus toxin. PMID: 23643538
SNAP23-VAMP2 interaction plays a key role in cAMP-mediated exocytosis from parotid glands. PMID: 23380067
Amyloid-beta acts as a regulator of neurotransmitter release disrupting the interaction between synaptophysin and VAMP2 PMID: 22905234
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
VAMP2, SNAP25b and syntaxin 1 characterize most cerebellar glutamatergic synapses and only one type of GABAergic synapse. PMID: 22094010
Dysregulation of SNARE complex and syt-1 in prefrontal cortex of adult-onset hypothyroidism can be restored by T(4) treatment. PMID: 21646859
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
Data show that most of the synaptobrevin SNARE motif has a remarkable reluctance to bind membranes. PMID: 21768342
Synaptophysin and synaptobrevin 2 were expressed in a dynamic manner during the development of rat cochlea PMID: 21556117
Data showv that complexin 2 interacts with vesicle-associated membrane protein (VAMP) 2, syntaxins 3 and 4. PMID: 20829354
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
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
tomosyn controls synaptic vesicle fusion positively by serving as a placeholder for VAMP2. PMID: 20633536
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
synaptobrevin 2 forms complexes with the plasma membrane-bound SNAREs syntaxin 1A and SNAP25 to initiate the fusion reaction. PMID: 12177041
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
VAMP2 mRNA is increased during nerve regeneration of the facial motor nucleus after axotomy. PMID: 12191731
Dimerization of synaptobrevin 2 in membranes is very weak, questioning any possible functional role for this association in vivo. PMID: 12501216
vesicle-associated membrane protein 2 is involved in secretion of polypeptides from the choroid plexus epithelium. PMID: 12559091
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
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
Homodimerization of Vamp2 is mediated by its transmembrane segment. PMID: 15109254
Data suggest that VAMP2-dependent exocytosis regulates plasma membrane insertion of TRPC3 channels and contributes to carbachol-stimulation of Ca2+ influx. PMID: 15327778
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
VAMP 2 is the most abundant isoform in the rat brain and is widely distributed PMID: 16169186
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
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
Individual pancreatic acinar cells express VAMP 2-specific populations of zymogen granules that orchestrate the constitutive and calcium(2+)-regulated secretory pathways. PMID: 17272274
VAMP2 is expressed in muscle satellite cells and up-regulated during muscle regeneration. PMID: 17468895
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
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
analysis of the substrate recognition mechanism of VAMP/synaptobrevin-cleaving clostridial neurotoxins PMID: 18511418
VAMP2 may contribute to the activity dependence of dense-core vesicles release PMID: 18542995
Findings suggest the involvement of VAMP2 in the development of skeletal muscles of somitic and non-somitic origins. PMID: 18570252
Results show that synaptophysin-containing cells co-expressed vesicular-associated membrane protein 2 and cholecystokinin. PMID: 19253017
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
VAMP2, VAMP5, and VAMP7 may be involved in translocation of GLUT4 during muscle contractions. PMID: 19675279
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
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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Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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