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Citations & References (20)
Invitrogen™
CMAC, t-BOC-Leu-Met (7-Amino-4-Chloromethylcoumarin, t-BOC-L-Leucyl-L-Methionine amide)
The CMAC peptidase substrate, t-BOC-Leu-Met can be used to measure peptidase activity in solution or in live cells. The substrateRead more
| Catalog Number | Quantity |
|---|---|
| A6520 | 5 mg |
Catalog number A6520
Price (CLP)
368.836
Each
Quantity:
5 mg
Price (CLP)
368.836
Each
The CMAC peptidase substrate, t-BOC-Leu-Met can be used to measure peptidase activity in solution or in live cells. The substrate has an excitation/emission maxima ∼330/403. After cleavage by peptidases, the product produces blue-fluorescence with excitation/emission maxima ∼351/430.
For Research Use Only. Not for use in diagnostic procedures.
Specifications
Cell PermeabilityCell-Permeant
Quantity5 mg
Shipping ConditionRoom Temperature
SubstrateCMAC peptidase substrate
Detection MethodFluorescence
FormSolid
Substrate PropertiesPeptide-Based Substrate
Substrate TypePeptidase Substrate
Target EnzymeCalpain
Unit SizeEach
Contents & Storage
Store in freezer (-5 to -30°C).
Citations & References (20)
Citations & References
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,