Analytical Data
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Gene name
JN
- Application
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Alternative Names
JN；KIAA1189；Ermin
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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
Q8TAM6
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Expression Region
1-284aa
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AA Sequence
MTDVPATFTQ AECNGDKPPE NGQQTITKIS EELTDVDSPL PHYRVEPSLE GALTKGSQEE RRKLQGNMLL NSSMEDKMLK ENPEEKLFIV HKAITDLSLQ ETSADEMTFR EGHQWEKIPL SGSNQEIRRQ KERITEQPLK EEEDEDRKNK GHQAAEIEWL GFRKPSQADM LHSKHDEEQK VWDEEIDDDD DDNCNNDEDE VRVIEFKKKH EEVSQFKEEG DASEDSPLSS ASSQAVTPDE QPTLGKKSDI SRNAYSRYNT ISYRKIRKGN TKQRIDEFES MMHL
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Molecular Weight
32.7 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
Related Products
Protein Description
The study of JN recombinant proteins has emerged as a pivotal area in biomedical research, particularly due to their potential applications in therapeutic development and disease modeling. JN proteins are known for their unique structural and functional properties, which make them suitable candidates for a variety of biotechnological applications. These proteins can be engineered to exhibit enhanced stability, binding affinity, and specificity, thereby improving their utility in drug delivery systems, vaccines, and diagnostic tools. Recent advancements in genetic engineering and protein expression techniques have facilitated the high-yield production of JN recombinant proteins, allowing researchers to investigate their biochemical properties and interactions with other biomolecules in detail. As a result, they have garnered significant attention for their role in addressing complex challenges such as vaccine development for emerging infectious diseases, targeted cancer therapies, and the study of protein interactions in cellular pathways. Furthermore, the elucidation of their mechanisms of action could lead to novel insights into pathophysiological processes and contribute to the development of innovative therapeutic strategies. Overall, ongoing research into JN recombinant proteins holds promise for advancing our understanding of molecular biology and enhancing the efficacy of current medical interventions.
