Analytical Data
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Gene name
nth
- Application
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Alternative Names
NTHL1;NTH1;OCTS3;Endonuclease III-like Protein 1
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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
P78549
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Expression Region
1-312aa
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AA Sequence
MCSPQESGMT ALSARMLTRS RSLGPGAGPR GCREEPGPLR RREAAAEARK SHSPVKRPRK AQRLRVAYEG SDSEKGEGAE PLKVPVWEPQ DWQQQLVNIR AMRNKKDAPV DHLGTEHCYD SSAPPKVRRY QVLLSLMLSS QTKDQVTAGA MQRLRARGLT VDSILQTDDA TLGKLIYPVG FWRSKVKYIK QTSAILQQHY GGDIPASVAE LVALPGVGPK MAHLAMAVAW GTVSGIAVDT HVHRIANRLR WTKKATKSPE ETRAALEEWL PRELWHEING LLVGFGQQTC LPVHPRCHAC LNQALCPAAQ GL
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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 study of nth recombinant proteins has gained considerable attention in the field of molecular biology and biotechnology, primarily due to their pivotal role in various cellular processes and potential applications in medicine and industry. Nth proteins, characterized by their unique structural and functional properties, are often involved in vital processes such as DNA repair, replication, and transcription regulation. Understanding these proteins is critical because they can provide insights into fundamental biological mechanisms and the pathology of diseases, including cancer. Researchers have developed recombinant DNA technologies to express nth proteins in prokaryotic or eukaryotic systems, allowing for detailed studies of their functions and interactions. This methodological advancement has not only facilitated the investigation of nth proteins in vitro but also paved the way for therapeutic applications, such as enzyme replacement therapies or the development of novel biomolecules for drug delivery. Overall, the exploration of nth recombinant proteins encompasses a multidisciplinary approach, integrating genetics, biochemistry, and structural biology, which contributes to our understanding of life at the molecular level and holds promise for future innovations in health and biotechnology.
