Analytical Data
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Gene name
SYNGR1
- Application
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Alternative Names
SYNGR1；Synaptogyrin-1
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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
O43759
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Expression Region
1-191aa
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AA Sequence
MEGGAYGAGKAGGAFDPYTLVRQPHTILRVVSWLFSIVVFGSIVNEGYLNSASEGEEFCIYNRNPNACSYGVAVGVLAFLTCLLYLALDVYFPQISSVKDRKKAVLSDIGVSAFWAFLWFVGFCYLANQWQVSKPKDNPLNEGTDAARAAIAFSFFSIFTWSLTAALAVRRFKDLSFQEEYSTLFPASAQP
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Molecular Weight
48.0 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
SYNGR1, or Synaptogyrin 1, is a protein that plays a critical role in synaptic function and neural communication. Its expression is predominantly found in the brain, where it is involved in neurotransmitter release and synaptic plasticity. Recent studies have highlighted the potential implications of SYNGR1 in neuropsychiatric disorders, including schizophrenia and autism spectrum disorders, suggesting that alterations in its function may contribute to the pathophysiology of these conditions. The recombinant versions of SYNGR1 are being explored for a variety of applications, including the investigation of its interactions with other synaptic proteins and the characterization of its role in synaptic vesicle trafficking. By producing SYNGR1 as a recombinant protein, researchers can facilitate the development of assays to study its biochemical properties, cellular localization, and functionality in vitro. This research is not only important for understanding fundamental neural mechanisms but may also pave the way for novel therapeutic strategies targeting synaptic dysfunction, offering hope for improved treatment options for individuals affected by synaptic-related neurodevelopmental disorders. As a result, SYNGR1 continues to be a focus of active research, appealing to both neuroscientists and clinicians interested in the molecular basis of brain function and mental health.
