Analytical Data
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Gene name
Syntaphilin
- Application
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Alternative Names
Syntaphilin；KIAA0374；Syntaphilin
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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
O15079
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Expression Region
1-424aa
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AA Sequence
MAMSLPGSRRTSAGSRRRTSPPVSVRDAYGTSSLSSSSNSGSYKGSDSSPTPRRSMKYTLCSDNHGIKPPTPEQYLTPLQQKEVCIRHLKARLKDTQDRLQDRDTEIDDLKTQLSRMQEDWIEEECHRVEAQLALKEARKEIKQLKQVIDTVKNNLIDKDKGLQKYFVDINIQNKKLETLLHSMEVAQNGMAKEDGTGESAGGSPARSLTRSSTYTKLSDPAVCGDRQPGDPSSGSAEDGADSGFAAADDTLSRTDALEASSLLSSGVDCGTEETSLHSSFGLGPRFPASNTYEKLLCGMEAGVQASCMQERAIQTDFVQYQPDLDTILEKVTQAQVCGTDPESGDRCPELDAHPSGPRDPNSAVVVTVGDELEAPEPITRGPTPQRPGANPNPGQSVSVVCPMEEEEEAAVAEKEPKSYWSRH
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Molecular Weight
62.0kDa
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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
Syntaphilin is a protein that plays a crucial role in the regulation of mitochondrial dynamics and is primarily known for its function in tethering mitochondria to the cytoskeleton. This tethering is essential for maintaining mitochondrial morphology, facilitating mitochondrial transport, and optimizing energy production and distribution within cells. The interest in Syntaphilin has grown in recent years due to its implications in various neurological disorders, metabolic diseases, and aging. Dysfunctional mitochondrial dynamics are often linked to pathologies such as Alzheimer's disease, Parkinson's disease, and other neurodegenerative conditions, highlighting the importance of understanding Syntaphilin's mechanisms. Researchers have focused on the recombinant expression of Syntaphilin to elucidate its structure-function relationships, to identify potential post-translational modifications, and to explore its interactions with other mitochondrial and cytoskeletal proteins. By producing and characterizing recombinant Syntaphilin, scientists aim to develop therapeutic strategies that target mitochondrial dysfunction, thereby opening new avenues for treating diseases associated with impaired energy metabolism. This research not only enhances our understanding of mitochondrial biology but also provides potential pathways for developing novel interventions in mitochondrial-related diseases.
