Analytical Data
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Gene name
SHPK
- Application
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Alternative Names
SHPK；CARKL；Sedoheptulokinase
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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
Q9UHJ6
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Expression Region
2-478aa
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AA Sequence
AARPITLGI DLGTTSVKAA LLRAAPDDPS GFAVLASCAR AARAEAAVES AVAGPQGREQ DVSRILQALH ECLAALPRPQ LRSVVGIGVS GQMHGVVFWK TGQGCEWTEG GITPVFEPRA VSHLVTWQDG RCSSEFLASL PQPKSHLSVA TGFGCATIFW LLKYRPEFLK SYDAAGTIHD YVVAMLCGLP RPLMSDQNAA SWGYFNTQSQ SWNVETLRSS GFPVHLLPDI AEPGSVAGRT SHMWFEIPKG TQVGVALGDL QASVYSCMAQ RTDAVLNIST SVQLAASMPS GFQPAQTPDP TAPVAYFPYF NRTYLGVAAS LNGGNVLATF VHMLVQWMAD LGLEVEESTV YSRMIQAAVQ QRDTHLTITP TVLGERHLPD QLASVTRISS SDLSLGHVTR ALCRGIVQNL HSMLPIQQLQ DWGVERVMGS GSALSRNDVL KQEVQRAFPL PMSFGQDVDA AVGAALVMLR RHLNQKES
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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
SHPK (Sphingosine Phosphate Kinase) is a pivotal enzyme involved in sphingolipid metabolism, catalyzing the conversion of sphingosine to sphingosine-1-phosphate (S1P), a bioactive lipid mediator. The significance of SHPK in cellular processes has garnered attention due to its role in various physiological and pathological conditions, including cell growth, survival, migration, immune responses, and inflammation. Dysregulation of SHPK activity is associated with several diseases, such as cancer, cardiovascular disorders, and neurological diseases. As research progresses, the structural and functional characterization of SHPK is vital for understanding its complex regulatory mechanisms and interactions within cellular signaling pathways. The production of recombinant SHPK proteins allows for detailed studies of its enzymatic properties, substrate specificity, and potential as a therapeutic target. Utilizing molecular biology techniques to express and purify SHPK in heterologous systems has enabled researchers to investigate its role in sphingolipid signaling more effectively. Insights gained from SHPK studies could pave the way for novel therapeutic strategies aimed at modulating sphingosine-1-phosphate signaling in various diseases, making this line of research increasingly relevant in the fields of biochemistry, pharmacology, and biomedical research.
