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引用和文献 (20)
Invitrogen™
CMAC，t-BOC-Leu-Met（7-氨基-4-氯甲基香豆素，t-BOC-L-亮氨酰-L-蛋氨酰胺）
CMAC 肽酶底物 t-BOC-Leu-Met 可用于测量溶液或活细胞中的肽酶活性。底物的最大激发/发射波长为 ∼330/403。经过肽酶切割后，产物会产生蓝色荧光，最大激发/发射波长约为 ∼351/430。了解更多信息
| 货号 | 数量 |
|---|---|
| A6520 | 5 mg |
货号 A6520
价格（CNY)
3,327.00
Online Exclusive
Ends: 31-Dec-2025
4,393.00共减 1,066.00 (24%)
Each
数量:
5 mg
价格（CNY)
3,327.00
Online Exclusive
Ends: 31-Dec-2025
4,393.00共减 1,066.00 (24%)
Each
CMAC 肽酶底物 t-BOC-Leu-Met 可用于测量溶液或活细胞中的肽酶活性。底物的最大激发/发射波长为 ∼330/403。经过肽酶切割后，产物会产生蓝色荧光，最大激发/发射波长约为 ∼351/430。
仅供科研使用。不可用于诊断程序。
规格
细胞渗透性细胞通透性
数量5 mg
运输条件室温
底物CMAC 肽酶底物
检测方法荧光
形式实心
底物属性基于肽的底物
底物类型肽酶底物
目标酶钙蛋白酶
Unit SizeEach
内容与储存
在冰箱（-5 至 -30°C）中储存。
引用和文献 (20)
引用和文献
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,