Analytical Data
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Gene name
Peptide deformylase
- Application
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Alternative Names
Polypeptide deformylase
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Species
Staphylococcus aureus
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Source
Yeast
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P68826
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Expression Region
1-183aa
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Molecular Weight
22.6 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
Peptide deformylase (PDF) is an essential bacterial enzyme that plays a crucial role in the co-translational processing of newly synthesized proteins by removing the N-formyl group from the N-terminus of formylmethionyl peptides. This enzymatic activity is vital for the maturation of proteins and is unique to prokaryotes, making PDF a potential target for antibiotic drug development. The increasing prevalence of antibiotic-resistant bacteria has intensified the search for novel therapeutic agents, with PDF emerging as a promising candidate due to its distinct mechanism of action. Research on recombinant PDF has gained momentum, focusing on its structure, function, and interaction with potential inhibitors. By producing recombinant PDF in suitable expression systems, researchers are able to study its catalytic properties in detail and assess the impact of various small molecules as inhibitors. This work not only deepens our understanding of bacterial protein synthesis but could also aid in the design of targeted inhibitors that circumvent existing resistance mechanisms. Overall, the exploration of recombinant peptide deformylase holds significant implications for microbiology and pharmaceutical development, offering new avenues for combating antibiotic resistance.
