Recombinant human PADI1 / PAD1 protein is a Human Full Length protein, in the 1 to 663 aa range, expressed in Baculovirus infected Sf9, with >70% purity and suitable for SDS-PAGE, FuncS.
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Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
Catalyzes the deimination of arginine residues of proteins.
PAD1, PDI1, PADI1, Protein-arginine deiminase type-1, Peptidylarginine deiminase I, Protein-arginine deiminase type I
Recombinant human PADI1 / PAD1 protein is a Human Full Length protein, in the 1 to 663 aa range, expressed in Baculovirus infected Sf9, with >70% purity and suitable for SDS-PAGE, FuncS.
Assay Conditions: Enzyme reaction was performed in a buffer (50 mM Tris, pH 7.4, 50 mM NaCl, 10 mM CaCl2, and 2 mM DTT) containing ab196400 and 10 mM BAEE as a substrate for 25 min at 37°C. Amount of ammonia produced was measured and used for specific activity calculation.
pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 0.72% Sodium chloride, 0.71% Tris HCl, 0.05% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.02% Potassium chloride
Affinity purified.
Catalyzes the deimination of arginine residues of proteins.
Belongs to the protein arginine deiminase family.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.
PADI1 also known as PAD1 or PADIone is a protein of approximately 74 kDa that belongs to the peptidylarginine deiminase family. It catalyzes the conversion of arginine residues into citrulline in a calcium-dependent manner a process known as citrullination or deimination. The PADI1 expression is mainly in the epidermis hair follicles and other keratinizing tissues. The enzyme requires at least one Ca2+ ion for its activity and often associates with the nucleus and cytoplasm within cells.
PADI1 plays an important role in modulating structural changes in proteins involved in skin differentiation and hair formation. It is not known to form part of a larger protein complex but instead acts as a standalone enzyme in multiple cellular processes. The citrullination activity of PADI1 significantly affects the structural proteins like keratin and filaggrin influencing keratinocyte terminal differentiation and barrier function of the skin.
PADI1 is instrumental in the formation of the epidermal barrier by contributing to the terminal differentiation pathway of keratinocytes. This pathway ensures the proper development and maintenance of the skin layers. It associates with proteins such as keratin and filaggrin during this process. Furthermore PADI1 also links to pathways involved in the regulation of intracellular protein modification impacting the overall protein structure and function in tissues.
PADI1 has been linked to psoriasis and skin cancers. In psoriasis the aberrant expression or regulation of PADI1 can lead to improper protein citrullination affecting skin barrier function and immune responses. Moreover dysregulated activity of PADI1 connects to skin cancer progression through its impact on keratinocyte proliferation and differentiation. Research has shown interactions with other proteins like keratin as part of these disease processes relevant to its role in skin pathology.
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Example of specific activity of ab196400
10% SDS-PAGE analysis of ab196400 (5 μg) with Coomassie staining.
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