Analytical Data
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Gene name
ON
- Application
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Alternative Names
ON；Triggering receptor expressed on myeloid cells 2
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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
P13725
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Expression Region
26-221aa
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AA Sequence
AAIGSCSKEY RVLLGQLQKQ TDLMQDTSRL LDPYIRIQGL DVPKLREHCR ERPGAFPSEE TLRGLGRRGF LQTLNATLGC VLHRLADLEQ RLPKAQDLER SGLNIEDLEK LQMARPNILG LRNNIYCMAQ LLDNSDTAEP TKAGRGASQP PTPTPASDAF QRKLEGCRFL HGYHRFMHSV GRVFSKWGES PNRSRR
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Molecular Weight
22 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
ON-recombinant proteins have garnered significant attention in the field of biotechnology and pharmaceutical research due to their potential applications in various therapeutic and diagnostic processes. These proteins, derived from engineered organisms, offer enhanced functionality and specificity compared to their natural counterparts. The advent of genetic engineering and molecular biology techniques has enabled scientists to modify the amino acid sequences of proteins, leading to improved properties such as stability, solubility, and binding affinity. This has propelled the development of ON-recombinant proteins for use in drug delivery systems, vaccine formulations, and enzyme replacement therapies. Furthermore, their unique ability to mimic or enhance biological functions makes them invaluable in research settings, where they serve as tools for elucidating cellular mechanisms or validating drug targets. As the demand for more effective and safer biological products rises, the investigation of ON-recombinant proteins continues to be a dynamic and rapidly evolving area of study, promising advancements in personalized medicine and therapeutic interventions. Thus, ongoing research aims to optimize the production processes, enhance purification methods, and explore novel applications, ensuring ON-recombinant proteins remain at the forefront of biotechnological innovation.
