Analytical Data
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Gene name
ABCC1
- Application
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Alternative Names
ATP-binding cassette sub-family C member 1 Leukotriene C(4) transporter
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Species
Human
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P33527
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Expression Region
1248-1531aa
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Molecular Weight
35.9 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
ABCC1, also known as Multidrug Resistance Protein 1 (MRP1), is a member of the ATP-binding cassette (ABC) transporter superfamily, which plays a critical role in cellular detoxification and the efflux of various endogenous and exogenous compounds, including drugs and toxins. It is highly expressed in various tissues, including the lungs, liver, and brain, where it contributes to protecting cells from harmful substances. The clinical relevance of ABCC1 is underscored by its involvement in multidrug resistance (MDR) in cancer treatment, as its overexpression can lead to decreased efficacy of chemotherapy agents. Therefore, understanding its structure and function is crucial for developing strategies to overcome drug resistance. Research has focused on the purification and characterization of recombinant ABCC1 protein to study its functional mechanism and interaction with substrates. Techniques such as site-directed mutagenesis, X-ray crystallography, and cryo-electron microscopy have been utilized to elucidate the transport mechanism of ABCC1 and its substrate specificity. By exploring the conformational changes during the transport cycle, researchers aim to identify potential inhibitors that could enhance the effectiveness of chemotherapeutic agents in ABCC1-overexpressing tumors. Moreover, insights gained from these studies could lead to novel therapeutic approaches in designing drugs that evade efflux by ABCC1, ultimately improving patient outcomes in cancer therapy and other diseases associated with this transporter.
