Analytical Data
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Gene name
PAG2
- Application
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Alternative Names
PAG2；PAGA；PAGB；TDPX2；Peroxiredoxin-1
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Species
Bovine
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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
Q28057
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Expression Region
22-376aa
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AA Sequence
KKMKTLRETLREKNLLNNFLEEQAYRLSKNDSKITIHPLRNYLDTAYVGNITIGTPPQEFRVVFDTGSANLWVPCITCTSPACYTHKTFNPQNSSSFREVGSPITIFYGSGIIQGFLGSDTVRIGNLVSPEQSFGLSLEEYGFDSLPFDGILGLAFPAMGIEDTIPIFDNLWSHGAFSEPVFAFYLNTNKPEGSVVMFGGVDHRYYKGELNWIPVSQTSHWQISMNNISMNGTVTACSCGCEALLDTGTSMIYGPTKLVTNIHKLMNARLENSEYVVSCDAVKTLPPVIFNINGIDYPLRPQAYIIKIQNSCRSVFQGGTENSSLNTWILGDIFLRQYFSVFDRKNRRIGLAPAV
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Molecular Weight
42.1 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
PAG2 (Pseudomonas aeruginosa Gain-of-Function Protein 2) has garnered significant attention in the field of molecular biology due to its pivotal role in the pathogenicity of Pseudomonas aeruginosa, a notorious opportunistic pathogen associated with various infections, particularly in immunocompromised patients. Research has shown that PAG2 is involved in the regulation of key virulence factors and may modulate the host immune response, making it a potential target for therapeutic interventions. In recent years, advances in recombinant protein technology have facilitated the production of PAG2 in various expression systems, enabling detailed structural and functional studies. These investigations aim to elucidate the protein’s mechanisms of action, its interactions with host cells, and its potential as a vaccine candidate. The understanding of PAG2's role in bacterial virulence not only sheds light on the pathogenic mechanisms of Pseudomonas aeruginosa but also opens avenues for novel strategies in combating infections and developing effective treatments against this resilient pathogen.
