Recombinant Proteins

p53
LBP
CEA
HLA
TCL
TTC
NPM
MAF
Bax
BID

VAMP5 Human

Vesicle-associated membrane protein 5 Human Recombinant

Produced in E. coli, VAMP5 is a single, non-glycosylated polypeptide chain comprising 109 amino acids (amino acids 1-72) with a molecular mass of 12.7 kDa. It features a 37 amino acid His Tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5806
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

VAMP7 Human

Vesicle-Associated Membrane Protein 7 Human Recombinant

Recombinant human VAMP7, expressed in E. coli, is a single polypeptide chain. This protein consists of 211 amino acids, with a sequence encompassing residues 1-188 of the native protein, and has a molecular weight of 23.0 kDa. For purification purposes, a 23 amino acid His-tag is fused to the N-terminus of the protein. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5912
Source
E.coli.
Appearance
Clear, colorless solution, sterile-filtered.

VAMP8 Human

Endobrevin Human Recombinant

Recombinant Human VAMP8, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 96 amino acids (1-76 a.a.). It has a molecular weight of 10.9 kDa. The VAMP8 protein is fused to a 20 amino acid His Tag at the N-terminus and purified using proprietary chromatography techniques.
Shipped with Ice Packs
Cat. No.
BT6007
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

VAPA Human

VAMP Associated Protein A 33kDa Human Recombinant

Recombinant Human VAPA, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 264 amino acids (1-227 a.a.). With a molecular mass of 29.8 kDa, it is fused to a 37 amino acid His Tag and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT6051
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized through filtration.

VAPB Human

VAMP Associated Protein B and C Human Recombinant

Recombinant human VAPB, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It comprises 242 amino acids (1-222 a.a.) with a 20 amino acid His tag fused at the N-terminus, resulting in a molecular mass of 27.1 kDa. Note that the molecular size on SDS-PAGE may appear higher. The purification of VAPB is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT6137
Source
Escherichia Coli.
Appearance
A colorless solution that has been sterilized by filtration.

VAMP3 Human

Synaptobrevin-3 Human Recombinant

Recombinant human VAMP3, expressed in E. coli, is a single, non-glycosylated polypeptide chain with a molecular weight of 8.7 kDa, comprising 77 amino acids.
Shipped with Ice Packs
Cat. No.
BT5654
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

VAMP4 Human

Vesicle-associated membrane protein 4 Human Recombinant

Recombinant human VAMP4, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 123 amino acids (amino acids 1-115) with a molecular weight of 14.5 kDa. A His tag is fused to the C-terminus of VAMP4. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5725
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

VAMP2 Human

Synaptobrevin-2 Human Recombinant

Recombinant human VAMP2, produced in E. coli, is a single, non-glycosylated polypeptide chain of 126 amino acids (1-89) with a molecular weight of 13.8 kDa. It includes a 37 amino acid N-terminal His-Tag and is purified using standard chromatography techniques.
Shipped with Ice Packs
Cat. No.
BT5448
Source
Escherichia Coli.
Appearance
A sterile, colorless solution.

VAMP2 Human, (1-94)

Synaptobrevin-2 Human Recombinant, (1-94)

Recombinant Human VAMP2, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 118 amino acids (residues 1-94) with a molecular weight of 12.8 kDa. A 24 amino acid His-tag is fused to the N-terminus of VAMP2. The protein undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5506
Source

E.Coli

Appearance
A colorless solution that has been sterilized by filtration.

VAMP2 Mouse

Synaptobrevin-2 Recombinant Mouse

VAMP2 Mouse Recombinant, produced in E. coli, is a single, non-glycosylated polypeptide chain containing 118 amino acids (1-94 a.a). With a molecular mass of 12.8 kDa, it consists of VAMP2 fused to a 24 amino acid His-tag at its N-terminus. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5574
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.
Definition and Classification

Synaptobrevin, also known as vesicle-associated membrane protein (VAMP), is a small integral membrane protein found in secretory vesicles. It is a crucial component of the SNARE (soluble NSF attachment protein receptor) complex, which is essential for the fusion of vesicles with target membranes during exocytosis . Synaptobrevin is classified as an R-SNARE due to the presence of an arginine residue at a specific location within its primary sequence . In the V/T nomenclature, it is classified as a V-SNARE, indicating its localization to vesicles .

Biological Properties

Synaptobrevin is a protein with a molecular weight of approximately 18 kilodaltons (kDa) . It is predominantly expressed in neurons, where it is localized to synaptic vesicles . The protein is also found in other secretory cells, such as endocrine cells . Synaptobrevin’s expression is tightly regulated, and it is distributed throughout the nervous system, with high concentrations in the brain .

Biological Functions

The primary function of synaptobrevin is to mediate the fusion of synaptic vesicles with the presynaptic membrane, facilitating the release of neurotransmitters into the synaptic cleft . This process is critical for synaptic transmission and communication between neurons . Synaptobrevin also plays a role in the immune response by participating in the exocytosis of cytotoxic granules from immune cells . Additionally, it is involved in pathogen recognition and the immune response to infections .

Modes of Action

Synaptobrevin interacts with other SNARE proteins, such as syntaxin and SNAP-25, to form the SNARE complex . This complex undergoes a conformational change that brings the vesicle and target membranes into close proximity, allowing them to fuse . Synaptobrevin’s binding partners include synaptophysin, which regulates its trafficking and assembly into the SNARE complex . The downstream signaling cascades initiated by synaptobrevin-mediated vesicle fusion are essential for neurotransmitter release and synaptic plasticity .

Regulatory Mechanisms

The expression and activity of synaptobrevin are regulated at multiple levels. Transcriptional regulation involves various transcription factors that control the gene expression of synaptobrevin . Post-translational modifications, such as phosphorylation and ubiquitination, also play a role in modulating synaptobrevin’s function and stability . Additionally, synaptobrevin is subject to degradation by specific proteases, such as tetanospasmin and botulinum toxin, which cleave the protein and inhibit its function .

Applications

Synaptobrevin has several applications in biomedical research and clinical practice. It is used as a marker for synaptic vesicles in studies of synaptic transmission and neurodegenerative diseases . Synaptobrevin’s role in exocytosis makes it a target for therapeutic strategies aimed at modulating neurotransmitter release in conditions such as epilepsy and depression . Additionally, synaptobrevin-based diagnostic tools are being developed to detect and monitor neurological disorders .

Role in the Life Cycle

Throughout the life cycle, synaptobrevin plays a critical role in the development, function, and maintenance of the nervous system . During development, synaptobrevin is involved in the formation and maturation of synapses . In adulthood, it is essential for synaptic plasticity and memory formation . In aging and disease, alterations in synaptobrevin expression and function are associated with neurodegenerative conditions, such as Alzheimer’s disease and Parkinson’s disease .

© Copyright 2024 Thebiotek. All Rights Reserved.