877617-46-4 Usage
Uses
Peptidyl arginine deiminase 4 (PAD4, Protein arginine deiminase 4) catalyzes the post-translational modification of arginine residues on histones to form citrulline, which plays a large role in regulating gene expression. Dysregulated PAD4 activity has been implicated in cancer and rheumatoid arthritis. F-amidine inhibits PAD4 activity with an IC50 value of 21.6 μM in an in vitro activity assay. It irreversibly inactivates (kinact/KI = 3,000 M-1min-1) PAD4 by covalently modifying an active site cysteine that is important for its catalytic activity. F-amidine also inhibits PAD1 and PAD3 with IC50 values of 29.5 and 350 μM, respectively. F-amidine is cytotoxic to HL-60, MCF-7, and HT-29 cancer cell lines (IC50s = 0.5, 0.5 and 1 μM, respectively).[Cayman Chemical]
Check Digit Verification of cas no
The CAS Registry Mumber 877617-46-4 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 8,7,7,6,1 and 7 respectively; the second part has 2 digits, 4 and 6 respectively.
Calculate Digit Verification of CAS Registry Number 877617-46:
(8*8)+(7*7)+(6*7)+(5*6)+(4*1)+(3*7)+(2*4)+(1*6)=224
224 % 10 = 4
So 877617-46-4 is a valid CAS Registry Number.
877617-46-4Relevant articles and documents
A fluoroacetamidine-based inactivator of protein arginine deiminase 4: Design, synthesis, and in vitro and in vivo evaluation
Luo, Yuan,Knuckley, Bryan,Lee, Young-Ho,Stallcup, Michael R.,Thompson, Paul R.
, p. 1092 - 1093 (2006)
Protein arginine deiminase 4 (PAD4) is a calcium-dependent transcriptional corepressor that has been implicated in the onset and progression of rheumatoid arthritis. Herein we describe the synthesis and in vitro evaluation of a fluoroacetamidine-containing compound, N-α-benzoyl-N5-(2-fluoro-1-iminoethyl)-l-ornithine amide, 1, hereafter referred to as F-amidine, that is the most potent PAD4 inhibitor ever described. Additional studies described herein indicate that F-amidine can also inhibit PAD4 activity in vivo. The bioavailability of this compound suggests that F-amidine will be a powerful chemical probe of PAD4 function that can be used to dissect the roles of this enzyme in both rheumatoid arthritis and transcriptional control. The fact that inhibition is of an irreversible nature suggests that, with appropriate functionalization, F-amidine analogues will be robust activity-based protein-profiling and proteomic capture reagents. Copyright