Analytical Data
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Gene name
PAD1
- Application
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Alternative Names
PDI; PAD1; HPAD10; PDI1; Peptidylarginine Deiminase Type I; Protein-Arginine Deiminase Type-1; hPAD-Colony 10
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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 90% as determined by SDS-PAGE.
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Uniprot
Q9ULC6
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Expression Region
Pro298~Arg556
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Molecular Weight
33kDa
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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
PAD1 (Peptidylarginine deiminase 1) is an enzyme that plays a critical role in the post-translational modification of proteins through a process known as citrullination, where the amino acid arginine is converted into citrulline. This modification significantly influences various biological processes, including gene regulation, protein interactions, and immune responses. PAD1 is particularly important in the context of autoimmune diseases, such as rheumatoid arthritis, where abnormal citrullination patterns can trigger inappropriate immune reactions. Research has shown that PAD1 is expressed in various tissues, including the skin and immune cells, and its dysregulation can be linked to inflammatory conditions. Scientists are actively investigating PAD1 not only to understand its fundamental biological roles but also to explore its potential as a therapeutic target. By studying PAD1 and its effects on protein function, researchers aim to develop new strategies for treating diseases characterized by pathological citrullination, paving the way for innovative treatments that could alleviate symptoms and modify disease progression. Advances in recombinant protein technology have further enabled the production of PAD1 for in-depth studies, facilitating biochemical assays and structural analyses that enhance our understanding of its mechanism of action. Thus, PAD1 continues to be a significant focus in biomedical research, particularly in elucidating its contributions to health and disease.
