Product: VAMP2 Antibody
Catalog: DF6381
Description: Rabbit polyclonal antibody to VAMP2
Application: WB IHC IF/ICC
Reactivity: Human, Mouse, Rat
Prediction: Pig, Bovine, Rabbit
Mol.Wt.: 18kDa; 13kD(Calculated).
Uniprot: P63027
RRID: AB_2838344

View similar products>>

   Size Price Inventory
 100ul $280 In stock
 200ul $350 In stock

Lead Time: Same day delivery

For pricing and ordering contact:
Local distributors

Product Info

Source:
Rabbit
Application:
WB 1:500-1:2000, IHC 1:50-1:200, IF/ICC 1:100-1:500
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human,Mouse,Rat
Prediction:
Pig(100%), Bovine(100%), Rabbit(100%)
Clonality:
Polyclonal
Specificity:
VAMP2 Antibody detects endogenous levels of total VAMP2.
RRID:
AB_2838344
Cite Format: Affinity Biosciences Cat# DF6381, RRID:AB_2838344.
Conjugate:
Unconjugated.
Purification:
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Storage:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

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;

Immunogens

Immunogen:
Uniprot:
Gene(ID):
Expression:
P63027 VAMP2_HUMAN:

Nervous system and skeletal muscle.

Description:
Vesicle-associated membrane protein 2 (VAMP2, also called synaptobrevin) is part of the R-soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex (1). The SNARE complex is involved in vesicular transport and membrane fusion, a process regulated by calcium (2). In neurons, VAMP2 is predominantly inserted in presynaptic vesicle membranes. Assembly of VAMP2 with the plasma membrane SNAREs syntaxin 1 and SNAP25 is a key event necessary for membrane fusion and neurotransmitter release (2). In addition to this important function, VAMP2 is also involved in granule exocytosis in neutrophils (3) and release of bioactive peptides from cardiac myocytes (4) and juxtaglomerular cells (5).
Sequence:
MSATAATAPPAAPAGEGGPPAPPPNLTSNRRLQQTQAQVDEVVDIMRVNVDKVLERDQKLSELDDRADALQAGASQFETSAAKLKRKYWWKNLKMMIILGVICAIILIIIIVYFST

Predictions

Predictions:

Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Species
Results
Score
Pig
100
Bovine
100
Rabbit
100
Zebrafish
73
Xenopus
50
Horse
0
Sheep
0
Dog
0
Chicken
0
Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - P63027 As Substrate

Site PTM Type Enzyme
K52 Ubiquitination
K59 Ubiquitination
S61 Phosphorylation
R66 Methylation
S75 Phosphorylation
T79 Phosphorylation
S80 Phosphorylation
K83 Ubiquitination
K85 Ubiquitination
K91 Ubiquitination

Research Backgrounds

Function:

Involved in the targeting and/or fusion of transport vesicles to their target membrane. Modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1.

PTMs:

Phosphorylated by PRKCZ in vitro and this phosphorylation is increased in the presence of WDFY2.

(Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type B (BoNT/B, botB) which hydrolyzes the 76-Gln-|-Phe-77 bond and probably inhibits neurotransmitter release.

(Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type D (BoNT/D, botD) which probably hydrolyzes the 59-Lys-|-Leu-60 bond and inhibits neurotransmitter release. Note that humans are not known to be infected by C.botulinum type D.

(Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type F (BoNT/F, botF) which hydrolyzes the 58-Gln-|-Lys-59 bond and probably inhibits neurotransmitter release.

(Microbial infection) Targeted and hydrolyzed by C.tetani tetanus toxin (tetX) which hydrolyzes the 76-Gln-|-Phe-77 bond and probably inhibits neurotransmitter release.

Subcellular Location:

Cytoplasmic vesicle>Secretory vesicle>Synaptic vesicle membrane>Single-pass type IV membrane protein. Cell junction>Synapse>Synaptosome. Cell membrane.
Note: Neuronal synaptic vesicles. Colocalizes with PRKCZ and WDFY2 in intracellular vesicles (PubMed:17313651).

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

Nervous system and skeletal muscle.

Subunit Structure:

Interacts (via N-terminus) with KCNB1 (via N-terminus and C-terminus); stimulates the channel inactivation rate of KCNB1 (By similarity). Part of the SNARE core complex containing SNAP25, VAMP2 and STX1A. This complex binds to CPLX1. Interacts with BVES and STX4 (By similarity). Interacts with VAPA and VAPB. Interacts with WDFY2, PRKCZ and PRKCI. Forms a complex with WDFY2 and PRKCZ. Interacts with SEPT8; the interaction inhibits interaction of VAMP2 with SYP. Interacts with SYP; the interaction is inhibited by interaction with SEPT8 (By similarity). Interacts with PICALM. Interacts with alpha-synuclein/SNCA. Interacts with STX3 (By similarity).

Family&Domains:

Belongs to the synaptobrevin family.

Research Fields

· Genetic Information Processing > Folding, sorting and degradation > SNARE interactions in vesicular transport.

· Organismal Systems > Nervous system > Synaptic vesicle cycle.

· Organismal Systems > Endocrine system > Insulin secretion.   (View pathway)

· Organismal Systems > Excretory system > Vasopressin-regulated water reabsorption.

· Organismal Systems > Digestive system > Salivary secretion.

References

1). An artificial protein modulator reprogramming neuronal protein functions. Nature communications, 2024 (PubMed: 38448420) [IF=16.6]

Application: IF/ICC    Species: Mouse    Sample:

Fig. 5 APROM2 reprograms neuronal protein functions via de novo PTMs to fuel synaptic function. a Schematic illustration of the de novo PTM strategy of neuronal proteins using APROM2. APROM2 with protein phosphatase-like characteristics can dephosphorylate phospho-proteins, and thus restore the function of neuronal proteins. Created with BioRender.com. b Top, representative confocal laser scanning microscopy (CLSM) images of p-α-syn in primary neurons after different treatments. Bottom, 3D mapping of intracellular fluorescence. c Mean fluorescence intensity of p-α-syn in primary neurons after different treatments (n = 5 biologically independent cultures). Quantitative analysis (d) and representative CLSM images (e) of synaptic vesicle function indicated by FM1-43 after different treatments (n = 5 biologically independent cultures). Immunofluorescence and quantification analysis of the colocalization of α-syn with VMAT2 (f, h) or VAMP2 (g, i) in primary neurons after different treatments (n = 5 biologically independent cultures). j Microscopy images showing the neurite branches and neuronal connectivity of primary neurons after different treatments. k Intracellular ROS levels in primary neurons after different treatments. l, m Mitochondrial membrane potential (∆ψ) is indicated by JC-1 staining (l) and quantified by normalized JC-1 aggregates/monomers ratio (m) (n = 3 biologically independent cultures). JC-1 monomers (green) represent low ∆ψ, and JC-1 aggregates (red) represent high ∆ψ. n Protective effect of APROM2 and CeNPs on MPP+ treated cells (n = 5 biologically independent cultures). o Schematic illustration of APROM2 that reprograms α-syn function by the de novo PTM strategy and protects mitochondria for fueling synaptic function. APROM2 directly modulates p-α-syn by cleaving the phosphate monoester bond, thus, α-syn regains biological functions of binding to VMAT2 and VAMP2. In addition, APROM2 protects mitochondria against ROS to maintain presynaptic energy homeostasis. All the data are presented as means ± s.e.m. Statistical significance was analyzed by one-way ANOVA with multiple comparisons test. Source data are provided as a Source Data file.

Restrictive clause

 

Affinity Biosciences tests all products strictly. Citations are provided as a resource for additional applications that have not been validated by Affinity Biosciences. Please choose the appropriate format for each application and consult Materials and Methods sections for additional details about the use of any product in these publications.

For Research Use Only.
Not for use in diagnostic or therapeutic procedures. Not for resale. Not for distribution without written consent. Affinity Biosciences will not be held responsible for patent infringement or other violations that may occur with the use of our products. Affinity Biosciences, Affinity Biosciences Logo and all other trademarks are the property of Affinity Biosciences LTD.