Analytical Data
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Gene name
RI
- Application
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Alternative Names
RI；Nuclear receptor-interacting 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
P12319
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Expression Region
26-205aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSVPQKPKV SLNPPWNRIF KGENVTLTCN GNNFFEVSST KWFHNGSLSE ETNSSLNIVN AKFEDSGEYK CQHQQVNESE PVYLEVFSDW LLLQASAEVV MEGQPLFLRC HGWRNWDVYK VIYYKDGEAL KYWYENHNIS ITNATVEDSG TYYCTGKVWQ LDYESEPLNI TVIKAPREKY WLQ
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Molecular Weight
23 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 Recombinant Immunoglobulin (RI) proteins has gained significant attention due to their pivotal role in therapeutic applications and in understanding immune responses. RIs are engineered antibodies produced through recombinant DNA technology, allowing for precise modifications in their structure and function. This adaptability enhances their ability to bind specific antigens, making them crucial tools in the development of targeted therapies for various diseases, including cancers, autoimmune disorders, and infectious diseases. The increasing prevalence of conditions that require personalized medicine underscores the importance of RIs, as they can be tailored for improved efficacy and reduced side effects. Additionally, the advancement in biotechnological methods, such as mammalian cell culture and microbial systems, has streamlined the production of these proteins, ensuring high yield and activity. Recent breakthroughs in antibody engineering, including bispecific antibodies and antibody-drug conjugates, highlight the potential of RIs in revolutionizing treatment paradigms. However, challenges remain in ensuring stability, solubility, and immunogenicity of engineered antibodies, driving ongoing research to improve these attributes. The integration of bioinformatics and computational modeling further aids in rational design, facilitating the identification of promising candidates for clinical development. Overall, the research on RI proteins not only enhances our understanding of the immune system but also paves the way for innovative therapeutic strategies, making it a rapidly evolving and impactful field in biotechnology and medicine.
