Analytical Data
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Gene name
SYP
- Application
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Alternative Names
SYP；Synaptophysin
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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
P08247
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Expression Region
1-313aa
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AA Sequence
MLLLADMDVVNQLVAGGQFRVVKEPLGFVKVLQWVFAIFAFATCGSYS GELQLNVDCANKTESDLSIEVEFEYPFRLHQVYFDAPTCRGGTTKVFLVG DYSSSAEFFVTVAVFAFLYSMGALATYIFLQNKYRENNKGPMLDFLATAV FAFMWLVSSSAWAKGLSDVKMATDPENIIKEMPVCRQTGNTCKELRDLVT SGLNTSVVFGFLNLVLWVGNLWFVFKETGWAAPFLRAPPGAPEKQPAPGD AYGDAGYGQGPGGYGPQDSYGPQGGYQPDYGQPAGSGGSGYGPQGDYGQQ GYGPQGAPTSFSNQM
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Molecular Weight
61 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
In recent years, the study of SYP (Synaptophysin) recombinant proteins has gained significant attention due to their crucial role in synaptic function and neurobiology. SYP is a synaptic vesicle protein that is predominantly found in the presynaptic terminals of neurons, where it plays an essential role in neurotransmitter release and synaptic plasticity. Abnormalities in SYP expression have been implicated in various neurological disorders, including schizophrenia, Alzheimer's disease, and other neurodegenerative conditions. The recombinant production of SYP proteins allows researchers to investigate their structural and functional properties in detail, providing insights into their mechanisms of action within synaptic transmission. Furthermore, these studies facilitate the development of potential therapeutic strategies to target synaptic dysfunction in neurological disorders. By utilizing advanced techniques such as molecular cloning and protein expression systems, scientists are now able to produce large quantities of functional SYP protein for biochemical assays, structural analyses, and potential drug development. The ongoing research into SYP recombinant proteins is essential for expanding our understanding of neuronal communication and the molecular underpinnings of synaptic diseases, ultimately contributing to the advancement of targeted therapies.
