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一般說明
LysargiNase适于消化溶液或凝胶中的肽或蛋白。
赖氨酸精氨酸N端蛋白酶(LysargiNase)是从古菌嗜乙酸甲烷八叠球菌Methanosarcina acetivorans中发现的。 该酶特异地切割蛋白赖氨酸和精氨酸残基的N端。 与胰蛋白酶消化相比，得到的肽段分子量相近，但是产生的N端赖氨酸或精氨酸残基可用于b离子为主的谱学分析。 因此可促进C端肽段鉴定和富含精氨酸的磷酸化位点鉴定。 与胰蛋白酶不同的是，LysargiNase还可以切割甲基化修饰的精氨酸和赖氨酸，适合用于这类表观遗传学修饰的检测。
應用
LysargiNase适于消化溶液或凝胶中的肽或蛋白。
LysargiNase适于消化溶液或凝胶中的肽或蛋白。 可在多种溶剂中保持活性，包括5 mM TCEP、5%甲醇、5%乙腈、0.8 M尿素、0.1% RapiGest、1%脱氧胆酸、0.2% SDS和1% NP-40。 可耐受55°C，pH 6 – 9。LysargiNase可被1,10-菲咯啉、EDTA和其他钙、锌螯合剂可逆性抑制。 用于肽或蛋白消化时，建议酶：底物比为1:100至1:20(w/w)。
成分
每瓶含20 µg LysargiNase，通过大肠杆菌重组表达生产并由缓冲溶液冻干制成。
外觀
每瓶含20 µg LysargiNase，通过大肠杆菌重组表达生产并由缓冲溶液冻干制成。 用20 µL水复溶后，酶液含50 mM HEPES、5 mM CaCl2, pH 7.5。
儲存和穩定性
将冻干产品在-20°C下保存，最多可存放2年。重悬后，未用材料可分装保存在冰柜中。 应避免反复冻融循环。
其他說明
浓度：请参考特定批次的数据表。
免責聲明
除非我们的产品目录或产品附带的其他公司文档另有说明，否则我们的产品仅供研究使用，不得用于任何其他目的，包括但不限于未经授权的商业用途、体外诊断用途、离体或体内治疗用途或任何类型的消费或应用于人类或动物。
訊號詞
Danger
危險分類
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
標靶器官
Respiratory system
儲存類別代碼
11 - Combustible Solids
水污染物質分類（WGK）
WGK 1
Le Zhang et al.
ACS chemical biology, 16(11), 2595-2603 (2021-11-05)
Methods for the selective labeling of biogenic functional groups on peptides are being developed and used in the workflow of both current and emerging proteomics technologies, such as single-molecule fluorosequencing. To achieve successful labeling with any one method requires that
Cynthia Tallant et al.
The Journal of biological chemistry, 281(26), 17920-17928 (2006-04-22)
The metzincin clan encompasses several families of zinc-dependent metalloproteases with proven function both in physiology and pathology. They act either as broad spectrum protein degraders or as sheddases, operating through limited proteolysis. Among the structurally uncharacterized metzincin families are the
Pitter F Huesgen et al.
Nature methods, 12(1), 55-58 (2014-11-25)
To improve proteome coverage and protein C-terminal identification, we characterized the Methanosarcina acetivorans thermophilic proteinase LysargiNase, which cleaves before lysine and arginine up to 55 °C. Unlike trypsin, LysargiNase-generated peptides had N-terminal lysine or arginine residues and fragmented with b
Liana Tsiatsiani et al.
The FEBS journal, 282(14), 2612-2626 (2015-04-01)
Peptide-centered shotgun analysis of proteins has been the core technology in mass spectrometry based proteomics and has enabled numerous biological discoveries, such as the large-scale charting of protein-protein interaction networks, the quantitative analysis of protein post-translational modifications and even the
Kazuya Tsumagari et al.
STAR protocols, 2(3), 100682-100682 (2021-08-12)
Characterization of protein termini is essential for understanding how the proteome is generated through biological processes such as post-translational proteolytic events. Here, we introduce a practical protocol for terminomics to achieve simple and sensitive N- and C-terminal peptide enrichment. We
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