Recombinant Human Vesicle-Associated Membrane Protein 2 (VAMP2) Protein (GST)

Name: Recombinant Human Vesicle-Associated Membrane Protein 2 (VAMP2) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-09470P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) VAMP2.

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Product Overview

Description	Recombinant Human Vesicle-Associated Membrane Protein 2 (VAMP2) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P63027
Target Symbol	VAMP2
Synonyms	FLJ11460; RATVAMPB; RATVAMPIR; SYB; SYB2; Synaptobrevin 2; Synaptobrevin-2; VAMP 2; VAMP-2; Vamp2; VAMP2_HUMAN; Vesicle associated membrane protein 2; Vesicle-associated membrane protein 2 (synaptobrevin 2); Vesicle-associated membrane protein 2
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MSATAATAPPAAPAGEGGPPAPPPNLTSNRRLQQTQAQVDEVVDIMRVNVDKVLERDQKLSELDDRADALQAGASQFETSAAKLKRKYWWKNLKMMIILGVICAIILIIIIVYFST
Expression Range	1-116aa
Protein Length	Full Length
Mol. Weight	39.7kDa
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	HGNC: 12643 OMIM: 185881 KEGG: hsa:6844 STRING: 9606.ENSP00000314214 UniGene: Hs.25348
Tissue Specificity	Nervous system and skeletal muscle.

Gene Functions References

miR-493-5p overexpression promotes cell apoptosis and inhibits the proliferation and migration of liver cancer cells by negatively regulating the expression of VAMP. PMID: 29328362
VAMP2 is a promising new plasma cell marker PMID: 27247366
VAMP2 is involved in Porphyromonas gingivalis recycling pathway.VAMP2 is localized in early endosomes in gingival epithelial cells. PMID: 26617273
The present study addressed for the first time the unique substrate recognition mechanism of LC/F5 substrate cleavage of VAMP-2 by Botulinum Neurotoxin subtype F5. PMID: 26794648
This study showed that decreased Levels of VAMP2 correlate with Duration of Dementia. PMID: 26639969
VAMP2-NRG1 is a novel oncogenic fusion gene representing a new addition to the list of NRG1 fusion genes, which together may form an important diagnostic and clinical category of lung adenocarcinoma cases PMID: 26134228
A large vesicular pool of VAMP2 maintained by AP180 is crucial to sustain efficient neurotransmission. PMID: 26412491
miR-206 regulates lung surfactant secretion by limiting the availability of VAMP-2 protein. PMID: 25481410
The genetic variations of VAMP2, Synaptotagmin XI might be indication of the relationship between these genes and idiopathic generalized epilepsy PMID: 24164654
BoNT/F5 cleaves substrate synaptobrevin-2 in a different location than the other BoNT/F subtypes, between (54)L and (55)E. PMID: 22172278
unique mechanism of SNARE motif-dependent endocytic sorting and identify the ANTH domain proteins AP180 and CALM as cargo-specific adaptors for synaptobrevin 2 endocytosis PMID: 21808019
VAMP2 mediates the trafficking of alpha5beta1 integrin to the plasma membrane and VAMP2-dependent integrin trafficking is critical in cell adhesion, migration and survival. PMID: 19822142
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 PMID: 11842301
VAMP-2 mediates exocytosis of specific and tertiary granules of neutrophils through its interaction with Q-SNARE/R-SNARE complexes located at the neutrophil plasma membrane. PMID: 12517971
VAMP-2 can be one of the v-SNAREs for constitutive exocytosis PMID: 16195891
addition of PIP2 to Stx4/SNAP23 vesicles inhibited the fusion reaction, and its addition to VAMP2 vesicles was stimulatory PMID: 17001002
The vesicular distribution may be attributed in part to the direct interaction between PKD3 and vesicle-associated membrane protein VAMP2, through which PKD3 may regulate VAMP2 vesicle trafficking by facilitating its recruitment to the target membrane. PMID: 17196367
VAMP2 can be phosphorylated by activated PKCzeta in vitro and the presence of ProF increases the PKCzeta-dependent phosphorylation of VAMP2 in vitro PMID: 17313651
Results indicate that the sorting determinants of synaptic vesicle proteins can operate independently of a neuronal context and implicate the association of VAMP2 with synaptophysin I in the specification of the pathway of synaptic vesicle biogenesis. PMID: 17331077
Overexpression of CALM leads to the reduction of cell surface VAMP2, whereas knockdown of CALM by RNA interference results in the accumulation of surface VAMP2. PMID: 18182011
BoNT/B and TeNT possess similar organization but have unique residues to recognize and cleave VAMP-2 PMID: 18511417
analysis of the substrate recognition mechanism of VAMP/synaptobrevin-cleaving clostridial neurotoxins PMID: 18511418
These results do not suggest that a common genetic variant at VAMP2 or VAMP3 contributes to the development of bipolar affective disorder in German patients. PMID: 18628682

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.