Analytical Data
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Gene name
SNAP23
- Application
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Alternative Names
SNAP23;Synaptosomal-associated Protein 23
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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
O00161
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Expression Region
1-211aa
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AA Sequence
MDNLSSEEIQQRAHQITDESLESTRRILGLAIESQDAGIKTITMLDEQKEQLNRIEEGLDQINKDMRETEKTLTELNKCCGLCVCPCNRTKNFESGKAYKTTWGDGGENSPCNVVSKQPGPVTNGQLQQPTTGAASGGYIKRITNDAREDEMEENLTQVGSILGNLKDMALNIGNEIDAQNPQIKRITDKADTNRDRIDIANARAKKLIDS
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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
SNAP23, a member of the soluble N-ethylmaleimide-sensitive factor attachment protein (SNAP) family, is a crucial protein involved in the regulation of vesicular transport and membrane fusion processes within neurons and other cell types. Its primary role is to facilitate exocytosis, a vital mechanism for the release of neurotransmitters, hormones, and various signaling molecules. Research indicates that SNAP23 interacts with other SNARE proteins, contributing to the formation of snare complexes that initiate membrane fusion events. Alterations in SNAP23 function or expression have been implicated in several pathological conditions, including neurodegenerative diseases and metabolic disorders. Given its essential role in cellular communication and transport, SNAP23 has become a target for research focused on understanding its mechanisms in health and disease. Investigating SNAP23 through the development of recombinant proteins offers insights into its structure-function relationships, potentially aiding in the identification of novel therapeutic strategies for diseases linked to impaired vesicular trafficking. Understanding the biochemical properties and interactions of SNAP23 in greater detail could pave the way for innovations in drug design and therapeutic approaches, particularly in conditions characterized by dysfunctional exocytosis or synaptic transmission.
