Analytical Data
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Gene name
skg
- Application
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Alternative Names
skg；Basigin
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Species
E.coli
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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
P10519
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Expression Region
27-440aa
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AA Sequence
IAGPEWLLDR PSVNNSQLVV SVAGTVEGTN QDISLKFFEI DLTSRPAHGG KTEQGLSPKS KLFATDSGAM PHKLEKADLL KAIQEQLIAN VHSNDDYFEV IDFASDATIT DRNGKVYFAD KDGSVTLPIQ PVQEFLLKGH VRVRPYKEKP VQNQAKSVDV EYTVQFTPLN PDDDFRPALK DTKLLKTLAI GDTITSQELL AQAQSILNKN HPGYTIYERD SSIVTHDNDI FRTILPMDQE FTYHVKNREQ AYRINKKSGL NEEINNTDLI SEKYYVLKKG EKPYDPFDRS HLKLFTIKYV DVNTNELLKS EQLLTASERN LDFRDLYDPR DKAKLLYNNL DAFGIMDYTL TGKVEDNHDD TNRIITVYMG KRPEGENASY HLAYDKDRYT EEEREVYSYL RYTGTPIPDN PNDK
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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
SKG (Sphingosine Kinase Gyrolase) recombinant protein research has gained significant attention due to its crucial role in cellular signaling and metabolism. Sphingosine kinases are enzymes that catalyze the phosphorylation of sphingosine to produce sphingosine-1-phosphate (S1P), a bioactive lipid that regulates various physiological processes, including cell growth, migration, apoptosis, and immune responses. Dysregulation of this pathway has been implicated in various diseases, including cancer, cardiovascular disorders, and neurodegenerative conditions. The production of SKG recombinant protein enables researchers to investigate the enzyme's structure-function relationships, its interactions with other cellular proteins, and its potential as a therapeutic target. By employing advanced techniques such as recombinant DNA technology and protein purification methods, scientists aim to produce large quantities of SKG protein for further studies. Understanding the molecular mechanisms mediated by SKG could pave the way for novel therapeutic strategies aimed at modulating the sphingolipid metabolism pathway, thereby enhancing the treatment options for a wide range of diseases. This research not only contributes to fundamental knowledge in biochemistry and molecular biology but also holds promise for translational applications in drug development and regenerative medicine.
