Analytical Data
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Gene name
SYT11
- Application
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Alternative Names
SYT11；KIAA0080；Synaptotagmin-11
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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
Q9BT88
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Expression Region
37-431aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSWSCCHQQAEKKQKNPPYKFIHMLKGIS IYPETLSNKKKIIKVRRDKDGPGREGGRRNLLVDAAEAGLLSRDKDPRGP SSGSCIDQLPIKMDYGEELRSPITSLTPGESKTTSPSSPEEDVMLGSLTF SVDYNFPKKALVVTIQEAHGLPVMDDQTQGSDPYIKMTILPDKRHRVKTR VLRKTLDPVFDETFTFYGIPYSQLQDLVLHFLVLSFDRFSRDDVIGEVMV PLAGVDPSTGKVQLTRDIIKRNIQKCISRGELQVSLSYQPVAQRMTVVVL KARHLPKMDITGLSGNPYVKVNVYYGRKRIAKKKTHVKKCTLNPIFNESF IYDIPTDLLPDISIEFLVIDFDRTTKNEVVGRLILGAHSVTASGAEHWRE VCESPRKPVAKWHSLSEY
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Molecular Weight
47 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
SYT11 (Synaptotagmin 11) is a member of the synaptotagmin family of proteins, which are primarily known for their roles in synaptic transmission and neurotransmitter release. Recent research has highlighted its significance in various neurological processes and potential implications in neurodegenerative diseases. The protein is characterized by its ability to bind calcium ions, which modulates its interactions with membrane surfaces and other proteins, potentially influencing membrane fusion events critical for synaptic efficiency. Understanding the structure and function of SYT11 can shed light on synaptic plasticity, a key mechanism underlying learning and memory. Additionally, aberrations in SYT11 function may be linked to conditions such as autism and schizophrenia, making it a target of increasing interest in neurobiological research. Therefore, the development of recombinant SYT11 protein is essential for elucidating its biochemical properties, determining its precise role in cellular signaling pathways, and exploring its potential as a therapeutic target. By producing and studying this recombinant protein, researchers aim to advance knowledge in neurobiology and potentially inform novel approaches to treating neurodevelopmental and neurodegenerative disorders.
