Analytical Data
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Gene name
SNAP29
- Application
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Alternative Names
SNAP29；Synaptosomal-associated Protein 29
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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
O95721
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Expression Region
1-258aa
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AA Sequence
MSAYPKSYNPFDDDGEDEGARPAPWRDARDLPDGPDAPADRQQYLRQEVLRRAEATAASTSRSLALMYESEKVGVASSEELARQRGVLERTEKMVDKMDQDLKISQKHINSIKSVFGGLVNYFKSKPVETPPEQNGTLTSQPNNRLKEAISTSKEQEAKYQASHPNLRKLDDTDPVPRGAGSAMSTDAYPKNPHLRAYHQKIDSNLDELSMGLGRLKDIALGMQTEIEEQDDILDRLTTKVDKLDVNIKSTERKVRQL
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Molecular Weight
56.0 kDa
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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
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Protein Description
SNAP29, a member of the soluble N-ethylmaleimide-sensitive factor attachment protein (SNAP) family, plays a crucial role in intracellular membrane traffic and the fusion of vesicles. It is particularly noted for its involvement in autophagy and endosomal pathways. Research has indicated that SNAP29 is essential for the degradation of cellular debris and the recycling of membrane proteins, which is vital for cellular homeostasis and responses to stress. Mutations or dysregulation of SNAP29 have been associated with various pathological conditions, including neurodegenerative diseases and disorders related to impaired autophagy. Studies have shown that SNAP29 interacts with multiple proteins involved in membrane fusion, suggesting its role as a molecular hub in vesicular transport. Furthermore, exploring the structural and biochemical properties of SNAP29 has provided insights into its functional mechanisms, which are critical for understanding its involvement in essential cellular processes. This research is not only pivotal for elucidating the fundamental biology of SNAP29 but also holds therapeutic potential for targeting autophagy-related diseases. By better understanding the function and interactions of SNAP29, researchers aim to develop innovative strategies to manipulate its pathways for clinical applications. Overall, the study of SNAP29 is significant for unraveling the complexities of vesicular transport and autophagy, thereby contributing to advances in cellular biology and disease treatment.
