Analytical Data
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Gene name
proA
- Application
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Alternative Names
proA；Gamma-glutamyl phosphate reductase
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Species
E.coli
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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
P07004
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Expression Region
1-417aa
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AA Sequence
MLEQMGIAAKQASYKLAQLSSREKNRVLEKIADELEAQSEIILNANAQDVADARANGLSEAMLDRLALTPARLKGIADDVRQVCNLADPVGQVIDGGVLDSGLRLERRRVPLGVIGVIYEARPNVTVDVASLCLKTGNAVILRGGKETCRTNAATVAVIQDALKSCGLPAGAVQAIDNPDRALVSEMLRMDKYIDMLIPRGGAGLHKLCREQSTIPVITGGIGVCHIYVDESVEIAEALKVIVNAKTQRPSTCNTVETLLVNKNIADSFLPALSKQMAESGVTLHADAAALAQLQAGPAKVVAVKAEEYDDEFLSLDLNVKIVSDLDDAIAHIREHGTQHSDAILTRDMRNAQRFVNEVDSSAVYVNASTRFTDGGQFGLGAEVAVSTQKLHARGPMGLEALTTYKWIGIGDYTIRA
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Molecular Weight
48.7 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
ProA, or Protein A, is a bacterial protein derived from Staphylococcus aureus, known for its ability to bind specifically to the Fc region of immunoglobulins. The study of ProA and its recombinant forms has gained considerable importance in various biotechnological and pharmaceutical applications, particularly in the field of antibody purification and characterization. Researchers have been investigating the structural and functional properties of ProA to enhance its efficiency and specificity in binding to antibodies. Recombinant approaches to produce ProA allow for the modification of its binding affinity and stability, making it a valuable tool in affinity chromatography. Additionally, the ability to generate chimeric proteins by fusing ProA with other functional domains has opened new avenues for targeted drug delivery and diagnostics. As the demand for high-purity antibodies grows in therapeutic and diagnostic settings, understanding the nuances of ProA's interactions and optimizing its recombinant variants remain critical in advancing antibody engineering and purification techniques. This research is pivotal for developing more efficient and cost-effective methods of isolating and producing monoclonal antibodies, ultimately contributing to better therapeutic outcomes in immunotherapy and other medical applications.
