Analytical Data
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Gene name
HYKK
- Application
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Alternative Names
HYKK;AGPHD1;Hydroxylysine kinase
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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
A2RU49
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Expression Region
1-373aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGS MSSGNYQ QSEALSKPTF SEEQASALVE SVFGLKVSKV RPLPSYDDQN FHVYVSKTKD GPTEYVLKIS NTKASKNPDL IEVQNHIIMF LKAAGFPTAS VCHTKGDNTA SLVSVDSGSE IKSYLVRLLT YLPGRPIAEL PVSPQLLYEI GKLAAKLDKT LQRFHHPK LS SLHRENFIWN LKNVPLLEKY LYALGQNRNR EIVEHVIHLF KEEVMTKLSH FRECINHGDL NDHNILIESS KSASGNAEYQ VSGILDFGDM SYGYYVFEVA ITIMYMMIES KSPIQVGGHV LAGFESITPL TAVEKGALFL LVCSRFCQSL VMAAYSCQLY PENKDYLMVT AKTGWKHLQQ MFDMGQKAVE EIWFETAKSY ESGIS
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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
Related Products
Protein Description
The research on HYKK recombinant protein is rooted in the exploration of its potential applications in biopharmaceuticals and therapeutic interventions. HYKK, a protein of interest, has shown promise due to its unique structural features and biological activities. Recombinant protein technology allows scientists to produce HYKK in a controlled environment using techniques such as genetic engineering and expression systems. This approach not only ensures a higher yield of the protein but also enables modifications that can enhance stability and functionality. The growing interest in HYKK is driven by its potential role in disease modulation, particularly in conditions where protein dysfunction is evident. Additionally, understanding the interactions and mechanisms of HYKK can lead to innovative treatments, contributing to advancements in personalized medicine. Continued research aims to elucidate the full range of biological activities of HYKK, paving the way for its application in diagnostics and therapeutics, as well as its integration into drug development pipelines. The collaborative efforts in this field highlight the significance of interdisciplinary approaches, merging molecular biology, bioinformatics, and pharmacology to unlock the full potential of HYKK as a valuable asset in modern medicine.
