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Citations & References (20)
Invitrogen™
CMAC, t-BOC-Leu-Met (7-Amino-4-Chloromethylcoumarin, t-BOC-L-Leucyl-L-Methionine amide)
CMACペプチダーゼ基質であるt-BOC-Leu-Metは、溶液中または生細胞中のペプチダーゼ活性の測定に使用できます。基質の最大励起波長／最大発光波長は約330/403です。この製品は、ペプチダーゼによる切断後に、最大励起波長／最大発光波長の約351/430で青色蛍光を生成します。詳細を見る
| 製品番号（カタログ番号） | 数量 |
|---|---|
| A6520 | 5 mg |
製品番号（カタログ番号） A6520
価格（JPY）お問い合わせください ›
64,800
Each
数量:
5 mg
CMACペプチダーゼ基質であるt-BOC-Leu-Metは、溶液中または生細胞中のペプチダーゼ活性の測定に使用できます。基質の最大励起波長／最大発光波長は約330/403です。この製品は、ペプチダーゼによる切断後に、最大励起波長／最大発光波長の約351/430で青色蛍光を生成します。
研究用にのみ使用できます。診断用には使用いただけません。
仕様
細胞透過性細胞透過性
数量5 mg
出荷条件室温
基質CMACペプチダーゼ基質
検出法蛍光
形状固体
Substrate Propertiesペプチドベースの基質
基質タイプペプチダーゼ基質
Target Enzymeカルパイン
Unit SizeEach
組成および保存条件
冷凍庫（-5～-30℃）に保存。
引用および参考文献 (20)
引用および参考文献
Abstract
Calpain-mediated X-linked inhibitor of apoptosis degradation in neutrophil apoptosis and its impairment in chronic neutrophilic leukemia.
Journal:J Biol Chem
PubMed ID:12121983
'The number of neutrophils in the blood and tissues is controlled by constitutive apoptotic programmed cell death and clearance by phagocytes such as macrophages. Here, we found that calpains cleave the X-linked inhibitor of apoptosis (XIAP) in vitro, producing fragments that are unable to inhibit caspase-3. These fragments were detected
Suppression of cancer cell migration and invasion by protein phosphatase 2A through dephosphorylation of mu- and m-calpains.
Journal:J Biol Chem
PubMed ID:16982626
'The mu- and m-calpains are major members of the calpain family that play an essential role in regulating cell motility. We have recently discovered that nicotine-activated protein kinase C iota enhances calpain phosphorylation in association with enhanced calpain activity and accelerated migration and invasion of human lung cancer cells. Here
Protein kinase Ciota promotes nicotine-induced migration and invasion of cancer cells via phosphorylation of micro- and m-calpains.
Journal:J Biol Chem
PubMed ID:16361262
'Nicotine is a major component in cigarette smoke that activates the growth-promoting pathways to facilitate the development of lung cancer. However, it is not clear whether nicotine affects cell motility to facilitate tumor metastasis. Here we discovered that nicotine potently induces phosphorylation of both mu- and m-calpains via activation of
Tumor necrosis factor-alpha-inducible IkappaBalpha proteolysis mediated by cytosolic m-calpain. A mechanism parallel to the ubiquitin-proteasome pathway for nuclear factor-kappab activation.
Journal:J Biol Chem
PubMed ID:9873017
'The cytokine tumor necrosis factor alpha (TNF-alpha) induces expression of inflammatory gene networks by activating cytoplasmic to nuclear translocation of the nuclear factor-kappaB (NF-kappaB) transcription factor. NF-kappaB activation results from sequential phosphorylation and hydrolysis of the cytoplasmic inhibitor, IkappaBalpha, through the 26 S proteasome. Here, we show a parallel proteasome-independent
Calpain is required for normal osteoclast function and is down-regulated by calcitonin.
Journal:J Biol Chem
PubMed ID:16461769
'Osteoclast motility is thought to depend on rapid podosome assembly and disassembly. Both mu-calpain and m-calpain, which promote the formation and disassembly of focal adhesions, were observed in the podosome belt of osteoclasts. Calpain inhibitors disrupted the podosome belt, blocked the constitutive cleavage of the calpain substrates filamin A, talin,