Analytical Data
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Gene name
AIP
- Application
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Alternative Names
ARA9; XAP2; AH receptor-interacting protein; HBV X-associated protein 2; Immunophilin homolog ARA9
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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
O00170
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Expression Region
Ile63~Pro296
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Molecular Weight
30kDa
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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
AIP (Arrestin-Independent Pathway) recombinant proteins have gained prominence in recent years due to their potential in advancing therapeutic interventions and understanding cellular signaling mechanisms. The study of AIP is rooted in the intricate network of G protein-coupled receptor (GPCR) signaling, where traditional pathways often involve arrestin-mediated processes that regulate receptor desensitization and internalization. However, AIP represents a unique aspect of GPCR signaling that operates independently of arrestins, suggesting alternative pathways that could be exploited for novel drug development. Research has indicated that AIP can play a crucial role in diverse physiological functions and contribute to various diseases, including cancer, cardiovascular disorders, and neurological conditions. By utilizing recombinant protein techniques, scientists can create and study specific AIP variants, examining their structure, function, and interactions within cellular environments. This approach not only enhances our comprehension of GPCR signaling but also opens avenues for therapeutic strategies that target AIP-related mechanisms. Understanding AIP's role could lead to the development of more selective and effective pharmacological agents, minimizing side effects associated with traditional receptor targeting. As ongoing research continues to unveil the complexities of these pathways, the application of AIP recombinant proteins promises to revolutionize our approach to treating multifaceted diseases.
