Analytical Data
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Gene name
VSNL1
- Application
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Alternative Names
VSNL1；VISL1；Visinin-like Protein 1
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P62760
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Expression Region
1-191aa
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AA Sequence
MGKQNSKLAPEVMEDLVKSTEFNEHELKQWYKGFLKDCPSGRLNLEEFQQLYVKFFPYGDASKFAQHAFRTFDKNGDGTIDFREFICALSITSRGSFEQKLNWAFNMYDLDGDGKITRVEMLEIIEAIYKMVGTVIMMKMNEDGLTPEQRVDKIFSKMDKNKDDQITLDEFKEAAKSDPSIVLLLQCDIQK
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Molecular Weight
49.0kDa
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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
VSNL1, or Vesicle-associated membrane protein (VAMP)-like 1, is a member of the synaptobrevin/VAMP family, playing a critical role in synaptic transmission and vesicular transport in neurons. This protein is primarily expressed in the brain and is implicated in various neurophysiological processes, making it a subject of interest in neuroscience research. The functional mechanisms of VSNL1 involve its participation in the fusion of synaptic vesicles with the presynaptic membrane, facilitating the release of neurotransmitters. Dysregulation of VSNL1 has been associated with neurodegenerative diseases and synaptic dysfunctions, prompting investigations into its structural and functional characteristics. Understanding the recombinant protein's properties is crucial for elucidating its role in synaptic physiology and potential therapeutic targets for neurological disorders. Recent studies have focused on the production and characterization of recombinant VSNL1, utilizing techniques such as molecular cloning and expression in heterologous systems. The findings aim to provide insights into its biochemical properties, interaction with other synaptic proteins, and functional significance in neuronal communication. Hence, researching VSNL1 recombinant protein not only enhances our comprehension of synaptic mechanisms but also opens avenues for developing interventions in conditions linked to synaptic impairments.
