Analytical Data
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Gene name
VAMP1
- Application
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Alternative Names
SYB; Synaptobrevin 1
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Species
Human
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P23763
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Expression Region
Met1~Val111
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Molecular Weight
42kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
VAMP1, or Vesicle-Associated Membrane Protein 1, is a key component of the synaptic vesicle membrane and plays a crucial role in neurotransmitter release through its involvement in the SNARE (Soluble N-ethylmaleimide-sensitive factor Attachment Protein Receptor) complex formation. Understanding the structure and function of VAMP1 is pivotal for elucidating the mechanisms of synaptic transmission and plasticity, as aberrations in these processes are linked to various neurological disorders. The study of recombinant VAMP1 protein provides insight into its biochemical properties, interactions with other SNARE proteins such as Syntaxin and SNAP-25, and its role in vesicle fusion. Researchers have employed techniques such as X-ray crystallography, cryo-electron microscopy, and biophysical assays to investigate the conformational changes and dynamics of VAMP1 during neurotransmitter release. Furthermore, VAMP1's interactions with regulatory proteins and its involvement in pathways modulating neurotransmission are integral to understanding synaptic functionality. The ongoing research aims to develop potential therapeutic strategies targeting these molecular interactions to address synaptic dysfunction in neurodegenerative diseases and psychiatric disorders. Thus, VAMP1 serves not only as a critical player in neurotransmission but also as a relevant model for studying protein-protein interactions and cellular communication in the nervous system.
