Analytical Data
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Gene name
PADI4
- Application
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Alternative Names
PAD; PADI5; PDI4; PDI5; Peptidyl Arginine Deiminase Type V; Peptidylarginine deiminase IV
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q9UM07
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Expression Region
Met1~Pro300
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Molecular Weight
36kDa
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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
PADI4, or Peptidyl Arginine Deiminase type 4, is an enzyme that catalyzes the deimination process, converting arginine residues in proteins into citrulline. This post-translational modification has significant implications for various biological processes, including gene expression, protein function, and immune response. Research surrounding PADI4 has gained traction due to its role in autoimmune diseases, particularly rheumatoid arthritis, where its dysregulation is linked to the formation of antibodies against citrullinated proteins, contributing to disease pathology. Furthermore, PADI4 is involved in epigenetic regulation and inflammation, positioning it as a promising target for therapeutic interventions. The study of PADI4's recombinant protein has opened avenues for understanding its enzymatic mechanisms, substrate specificity, and potential interactions with other biomolecules. The structural and functional characterization of PADI4 can facilitate the development of inhibitors that may mitigate its deleterious effects in disease contexts. Consequently, advancements in recombinant PADI4 research not only enhance our understanding of the enzyme's biology but also pave the way for novel therapeutic strategies against associated disorders.
