Analytical Data
-
Gene name
purD
- Application
-
Alternative Names
purD；PGFT；PRGS；Trifunctional purine biosynthetic Protein adenosine-3
-
Species
E.coli
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q8X612
-
Expression Region
1-429aa
-
AA Sequence
MKVLVIGNGGREHALAWKAAQSPLVETVFVAPGNAGTALEPTLQNVAIGVTDIPALLDFAQNEKVDLTIVGPEAPLVKGVVDTFRAAGMKIFGPTAGAAQLEGSKAFTKDFLARHNIPTAEYQNFTEVEPALAYLREKGAPIVIKADGLAAGKGVIVAMTLEEAEAAVHDMLAGNAFGDAGHRIVIEEFLDGEEASFIVMVDGEHVLPMATSQDHKRVGDKDTGPNTGGMGAYSPAPVVTDDVHQRTMERIIWPTVKGMASEGNTYTGFLYAGLMIDKQGNPKVIEFNCRFGDPETQPIMLRMKSDLVELCLAACEGKLDEKTSEWDERASLGVVMAAGGYPGDYRTGDVIHGLPLEEVEDGKVFHAGTKLADDEQVVTSGGRVLCVTALGHTVAEAQKRAYALMTDIHWDDCFCRKDIGWRAIEREQN
-
Molecular Weight
62.0 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
The purD gene encodes an enzyme involved in the de novo synthesis of purines, specifically catalyzing the conversion of phosphoribosylamine to 5-amino-1-(5-phospho-D-ribosyl)imidazole. Research on purD recombinant protein has gained significant attention due to its essential role in the purine biosynthetic pathway, which is crucial for nucleotide production and cellular function in various organisms. Understanding the structure and function of purD can provide insights into the regulation of purine metabolism and its implications in microbial growth and pathogenicity. Moreover, purD and its associated pathways present potential targets for the development of antimicrobial agents, as inhibiting purine synthesis can effectively stifle the growth of pathogenic bacteria and protozoa. Studies have focused not only on characterizing the enzyme's kinetic properties and substrate specificity but also on developing expression systems for large-scale production of the recombinant protein. Molecular techniques, including site-directed mutagenesis, have been employed to dissect the enzyme's functional domains, contributing to a deeper understanding of the mechanisms governing purine metabolism. Furthermore, by utilizing purD as a model, researchers aim to elucidate broader metabolic networks and their regulatory mechanisms, fostering advances in biochemistry, pharmacology, and synthetic biology. Overall, recombinant purD protein research holds promise for both theoretical insights and practical applications in health and disease.
