Analytical Data
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Gene name
RHAG
- Application
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Alternative Names
CD241; RH2; RH50A; Rh50 GP; SLC42A1; Ammonium Transporter Rh Type A; Rhesus Blood Group-Associated Glycoprotein; Erythrocyte plasma membrane 50 kDa glycoprotein
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Species
Rat
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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
Q7TNK7
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Expression Region
Ala251~Val450
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Molecular Weight
25kDa
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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
RHAG (Rhesus-associated glycoprotein) is a member of the major facilitator superfamily (MFS) known for its role in facilitating the transport of ammonia and other small molecules across cellular membranes. The importance of RHAG extends to its involvement in the Rh blood group system, which is crucial for blood transfusion compatibility and has implications in hemolytic disease of the newborn. Research on RHAG has gained momentum due to its significant physiological roles in erythrocytes and other tissues, where it contributes to the maintenance of acid-base balance and the transport of nitrogenous waste. Additionally, its expression and function have been linked to various pathological conditions, including blood disorders and non-communicable diseases. Understanding the structure and functional mechanisms of RHAG through protein engineering and recombinant approaches can provide valuable insights into its transport capabilities and regulatory mechanisms. The generation of recombinant RHAG proteins allows for detailed studies on its transport kinetics, substrate specificity, and interaction with other membrane proteins, thus paving the way for potential therapeutic interventions in conditions related to RHAG dysregulation. As such, the exploration of RHAG is not only pivotal for fundamental biological research but also for clinical applications in transfusion medicine and beyond.
