Analytical Data
-
Gene name
SNAP23
- Application
-
Alternative Names
SNAP23A; SNAP23B; Vesicle-membrane fusion protein SNAP-23
-
Species
Mouse
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 95% as determined by SDS-PAGE.
-
Uniprot
O09044
-
Expression Region
Met1~Ser210
-
Molecular Weight
27kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
SNAP23 (Synaptosomal-associated protein of 23 kDa) is a member of the SNARE (Soluble N-ethylmaleimide-sensitive factor attachment protein receptor) protein family, which plays a crucial role in mediating membrane fusion processes in various cellular functions, including neurotransmitter release, insulin secretion, and endocytosis. Research on SNAP23 has gained significant interest due to its involvement in exocytosis in different cell types, and its ability to interact with other SNARE proteins and accessory factors that regulate synaptic transmission and secretion. The study of SNAP23 is important as it provides insights into the molecular mechanisms underlying essential physiological processes and the potential dysregulation associated with various diseases. For instance, aberrations in SNAP23 function are implicated in disorders such as diabetes and neurological conditions. Investigating SNAP23 through protein recombination techniques enables researchers to analyze its structure, interaction with other proteins, and functional roles in detail. Recombinant SNAP23 proteins facilitate the understanding of its role in membrane dynamics and cellular communication, paving the way for potential therapeutic interventions targeting SNAP23-related pathways in disease contexts. Consequently, the ongoing research aims to elucidate the precise mechanisms by which SNAP23 contributes to cellular functionality, with an eye toward developing novel strategies for disease treatment and management.
