Analytical Data
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Gene name
fpg
- Application
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Alternative Names
mutM;fpg;Formamidopyrimidine-DNA glycosylase
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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
P05523
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Expression Region
1-289aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MPELPEVETS RRGIEPHLVG ATILHAVVRN GRLRWPVSEE IYRLSDQPVL SVQRRAKYLL LELPEGWIII HLGMSGSLRI LPEELPPEKH DHVDLVMSNG KVLRYTDPRR FGAWLWTKEL EGHNVLTHLG PEPLSDDFNG EYLHQKCAKK KTAIKPWLMD NKLVVGVGNI YASESLFAAG IHPDRLASSL SLAECELLAR VIKAVLLRSI EQGGTTLKDF LQSDGKPGYF AQELQVYGRK GEPCRVCGTP IVATKHAQRA TFYCRQCQK
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Molecular Weight
32 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
The study of fibronectin type III domain-containing protein (FPG) recombinantly targets the intricate interplay between protein structure and function, particularly in the fields of biochemistry and molecular biology. FPGs are integral components of various cellular processes, including cell adhesion, migration, and tissue repair. The ability to produce FPGs through recombinant DNA technology allows researchers to generate large quantities of these proteins for detailed analysis. This research is pertinent not only for understanding fundamental biological mechanisms but also for potential applications in therapeutics and biotechnology. FPGs serve as models for investigating protein folding, interactions, and post-translational modifications, critical for drug development and engineering biomaterials. Recent advances in recombinant techniques, such as improved expression systems and purification methods, have enhanced the yield and functionality of these proteins, propelling further studies into their roles in disease pathology and regenerative medicine. Consequently, the exploration of FPGs provides insight into their potential as biomarkers and therapeutic agents, highlighting the relevance of recombinant protein research in advancing scientific knowledge and healthcare solutions.
