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一般描述
肽基精氨酸脱亚胺酶是将精氨酸转化为瓜氨酸的酶。
应用
肽基精氨酸脱亚胺酶已被用于一项评估了有前途的新型生物标志物,用于类风湿性关节炎的早期诊断的研究。 也有研究用于探讨牙周炎和类风湿关节炎的自身致病相关性。
生化/生理作用
在体外,钙是肽酰精氨酸脱亚胺酶活性所必需的。
单位定义
一个单位将在55°C,pH 7.2下每小时从BAEE产生 1μN-α 摩尔苯甲酰瓜氨酸乙酯。
外形
溶液溶于 20 mM Tris-HCl,pH 7.4,含 10 mM 2-巯基乙醇、1 mM EDTA 和 10% 甘油
警示用语:
Danger
危险声明
预防措施声明
危险分类
Resp. Sens. 1
储存分类代码
10 - Combustible liquids
WGK
WGK 2
闪点(°F)
Not applicable
闪点(°C)
Not applicable
法规信息
动植物源性产品
历史批次信息供参考:
分析证书(COA)
Cytokine, 61(1), 161-167 (2012-10-19)
Citrullination, a posttranslational modification (PTM) recently discovered on inflammatory chemokines such as interleukin-8 (IL-8/CXCL8) and interferon-γ-inducible protein-10 (IP-10/CXCL10), seriously influences their biological activity. Citrullination or the deimination of arginine to citrulline is dependent on peptidylarginine deiminases (PADs) and has been
Journal of molecular biology, 367(4), 1118-1129 (2007-02-17)
Peptidylarginine deiminase (PAD) enzymes catalyze the conversion of arginine residues in proteins to citrulline residues. Citrulline is a non-standard amino acid that is not incorporated in proteins during translation, but can be generated post-translationally by the PAD enzymes. Although the
PloS one, 17(3), e0265687-e0265687 (2022-03-24)
The immune response to citrullinated peptides in the mucosa has been suggested to play an important role in the transition from pre-onset rheumatoid arthritis (RA) to clinically evident RA. Although there are reports indicating the presence of anti-citrullinated peptide antibodies
Circulation research, 114(6), 947-956 (2014-01-16)
Neutrophil extracellular trap (NET) formation promotes vascular damage, thrombosis, and activation of interferon-α-producing plasmacytoid dendritic cells in diseased arteries. Peptidylarginine deiminase inhibition is a strategy that can decrease in vivo NET formation. To test whether peptidylarginine deiminase inhibition, a novel
Journal of biochemistry, 89(1), 257-263 (1981-01-01)
An enzyme which catalyzes the coversion of arginyl residues to citrullyl residues in protein was obtained from the extract of the epidermis of newborn rats. The enzyme required Ca2+ for its activity. The enzyme activity was enhanced in the presence
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