Analytical Data
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Gene name
SNAPAP
- Application
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Alternative Names
SNAPIN; SNAP-25-Binding Protein; Biogenesis of lysosome-related organelles complex 1 subunit 7; Synaptosomal-associated protein 25-binding protein
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O95295
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Expression Region
Ala2~Lys136
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Molecular Weight
18kDa
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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
SNAPAP (Synergistic Neuronal Antigenic Protein) is a recombinant protein that has garnered attention in the field of neuroscience due to its potential roles in synaptic plasticity and neuronal signaling. The research surrounding SNAPAP is primarily driven by the need to understand the molecular mechanisms underlying neuronal communication and the factors contributing to neurodegenerative diseases. Recent studies indicate that SNAPAP may participate in crucial processes such as synaptic transmission, neuronal development, and the regulation of protein interactions within the synaptic environment. Furthermore, the exploration of SNAPAP at the molecular level could provide insights into synaptic dysfunction, a hallmark of various neurological disorders. As a recombinant protein, SNAPAP offers the advantage of being produced in controlled laboratory conditions, allowing researchers to investigate its structure-function relationships and interaction with other proteins in vitro. The integration of SNAPAP into various experimental models may also pave the way for the development of therapeutic strategies aimed at mitigating synaptic impairments. Given the complexity of neuronal networks and the multifaceted nature of synaptic interactions, the study of SNAPAP is not only relevant for basic neuroscience research but also holds promise for translational applications in understanding and treating neurodegenerative conditions.
