Analytical Data
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Gene name
OPI
- Application
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Alternative Names
OPI；OPRK；Kappa-type opioid receptor
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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
P41145
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Expression Region
1-380aa
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AA Sequence
MDSPIQIFRGEPGPTCAPSACLPPNSSAWFPGWAEPDSNGSAGSEDAQLEPAHISPAIPVIITAVYSVVFVVGLVGNSLVMFVIIRYTKMKTATNIYIFNLALADALVTTTMPFQSTVYLMNSWPFGDVLCKIVISIDYYNMFTSIFTLTMMSVDRYIAVCHPVKALDFRTPLKAKIINICIWLLSSSVGISAIVLGGTKVREDVDVIECSLQFPDDDYSWWDLFMKICVFIFAFVIPVLIIIVCYTLMILRLKSVRLLSGSREKDRNLRRITRLVLVVVAVFVVCWTPIHIFILVEALGSTSHSTAALSSYYFCIALGYTNSSLNPILYAFLDENFKRCFRDFCFPLKMRMERQSTSRVRNTVQDPAYLRDIDGMNKPV
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Molecular Weight
42.6 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
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Protein Description
OPI (Oligomeric Protein Inhibitor) recombinant proteins have garnered significant attention in the field of molecular biology and therapeutic development due to their potential applications in various biomedical areas. The research surrounding OPI proteins focuses on their role as powerful inhibitors that can modulate protein interactions and cellular functions. These recombinant proteins are engineered to mimic natural inhibitors, providing a promising approach for therapeutic interventions in diseases characterized by abnormal protein interactions, such as cancer, neurodegenerative disorders, and infectious diseases. Advances in recombinant DNA technology have allowed for the high-yield production of these proteins, facilitating detailed studies into their structure-function relationships and mechanisms of action. Ongoing research aims to enhance the specificity and efficacy of OPI proteins, exploring their use in drug design, targeted therapies, and as diagnostic tools. Additionally, the interdisciplinary nature of this research brings together biochemistry, structural biology, and pharmacology, highlighting the importance of OPI proteins in developing innovative solutions for complex health challenges.
