Analytical Data
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Gene name
purF
- Application
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Alternative Names
purF；GPAT；Amidophosphoribosyltransferase
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Species
Human
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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
P9WHQ6
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Expression Region
35-527aa
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AA Sequence
CGVFGVWAPGEDVAKLTYYGLYALQHRGQEAAGIAVADGSQVLVFKDLGLVSQVFDEQTLAAMQGHVAIGHCRYSTTGDTTWENAQPVFRNTAAGTGVALGHNGNLVNAAALAARARDAGLIATRCPAPATTDSDILGALLAHGAADSTLEQAALDLLPTVRGAFCLTFMDENTLYACRDPYGVRPLSLGRLDRGWVVASETAALDIVGASFVRDIEPGELLAIDADGVRSTRFANPTPKGCVFEYVYLARPDSTIAGRSVHAARVEIGRRLARECPVEADLVIGVPESGTPAAVGYAQESGVPYGQGLMKNAYVGRTFIQPSQTIRQLGIRLKLNPLKEVIRGKRLIVVDDSIVRGNTQRALVRMLREAGAVELHVRIASPPVKWPCFYGIDFPSPAELIANAVENEDEMLEAVRHAIGADTLGYISLRGMVAASEQPTSRLCTACFDGKYPIELPRETALGKNVIEHMLANAARGAALGELAADDEVPVGR
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Molecular Weight
56.5 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
Related Products
Protein Description
PurF, an essential enzyme involved in the purine biosynthetic pathway, plays a critical role in cellular metabolism by catalyzing the conversion of phosphoribosyl pyrophosphate (PRPP) and amino acids into purine nucleotides. The study of PurF recombinant protein has garnered significant interest in the fields of biochemistry and molecular biology due to its potential implications in understanding metabolic disorders, cancer, and microbial physiology. Research on PurF has highlighted its evolutionary conservation across various organisms, suggesting that it could serve as a promising target for the development of novel antimicrobial agents. Additionally, as an integral component of the purine biosynthesis pathway, PurF's activity directly influences DNA and RNA synthesis, making it a key player in cellular proliferation and function. Recombinant protein technology allows for the production of PurF in a controlled environment, enabling extensive characterization of its biochemical properties, structure-function relationships, and catalytic mechanisms. Such studies not only deepen our understanding of purine metabolism but also pave the way for innovative therapeutic strategies aimed at manipulating purine levels in pathological conditions. With the advent of advanced techniques like protein engineering and high-throughput screening, researchers are now more equipped than ever to explore the functional dynamics of PurF and its potential applications in biotechnology and medicine.
