| Description | Frozen in 20 mM Malonate, pH 5.5, 1 mM EDTA, 400 mM NaCl.The most powerful of the lysosomal proteases. It has a higher specific activity than cathepsin B and H in the degradation of a variety of physiological protein substrates. The level of cathepsin L is a strong predictor of relapse and survival Frozen in 20 mM Malonate, pH 5.5, 1 mM EDTA, 400 mM NaCl.The most powerful of the lysosomal proteases. It has a higher specific activity than cathepsin B and H in the degradation of a variety of physiological protein substrates. The level of cathepsin L is a strong predictor of relapse and survival following treatment of a primary breast tumor.Activity: > 1 unit/mg of protein. One unit is defined as the amount of enzyme that hydrolyzes one micromole of Z-Phe-Arg-AFC per minute at 25oC using 400 mM Na Acetate, pH 5.5 with 4 mM EDTA and 8 mM DTT as the activation buffer in the presence of Brij.Product Citations:Armstrong, Andrea, Niklas Mattsson, Hanna Appelqvist, Camilla Janefjord, Linnea Sandin, Lotta Agholme, Bob Olsson et al. "Lysosomal Network Proteins as Potential Novel CSF Biomarkers for Alzheimer’s Disease." Neuromolecular medicine (2013): 1-11Miller, Bailey, Aaron J. Friedman, Hyukjae Choi, James Hogan, J. Andrew McCammon, Vivian Hook, and William H. Gerwick. "The Marine Cyanobacterial Metabolite Gallinamide A Is a Potent and Selective Inhibitor of Human Cathepsin L." Journal of natural products (2013).References:Mason, R.W., Green, G.D.J. and Barrett, A.J. 1985. Biochem. J. 226, 233.Klijn et al. 1998. J. Clin. Onc.16, 1013.Barrett, A.J. and Kirschke, H. 1981. Methods Enzoymol. 80, 535.Tchope, J.R. et al. 1991. Biochem. Biophys. Acta. 1076. 149... Read More | Inquire | Product Application：KNK437 has been used: as a heat shock factor 1 (HSF1) inhibitor to study its effects on the inhibition of viability and apoptosis activation in chemoresistant mice cells as an HSF1 inhibitor to study its effects on viability and apoptosis of colorectal cancer cells as a Product Application：KNK437 has been used: as a heat shock factor 1 (HSF1) inhibitor to study its effects on the inhibition of viability and apoptosis activation in chemoresistant mice cells as an HSF1 inhibitor to study its effects on viability and apoptosis of colorectal cancer cells as a heat shock protein 70 (HSP70) inhibitor to study its effects on glutamine-induced HSP70 and inflammatory mediator release... Read More | Purity>95% SDS-PAGE.FunctionReceptor with high affinity for TNFSF2/TNF-alpha and approximately 5-fold lower affinity for homotrimeric TNFSF1/lymphotoxin-alpha. The TRAF1/TRAF2 complex recruits the apoptotic suppressors BIRC2 and BIRC3 to TNFRSF1B/TNFR2. This receptor mediates most of the Purity>95% SDS-PAGE.FunctionReceptor with high affinity for TNFSF2/TNF-alpha and approximately 5-fold lower affinity for homotrimeric TNFSF1/lymphotoxin-alpha. The TRAF1/TRAF2 complex recruits the apoptotic suppressors BIRC2 and BIRC3 to TNFRSF1B/TNFR2. This receptor mediates most of the metabolic effects of TNF-alpha. Isoform 2 blocks TNF-alpha-induced apoptosis, which suggests that it regulates TNF-alpha function by antagonizing its biological activity... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description:Monkeypox is a zoonotic disease caused by monkeypox virus (MPXV), which is a member of orthopoxvirus genus. A35R gene is highly conserved among poxviruses and encodes a previously uncharacterized hydrophobic acidicPurity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description:Monkeypox is a zoonotic disease caused by monkeypox virus (MPXV), which is a member of orthopoxvirus genus. A35R gene is highly conserved among poxviruses and encodes a previously uncharacterized hydrophobic acidic protein. The A35R has little homology to any protein outside of poxviruses, suggesting a novel virulence Monkeypox is a zoonotic disease caused by monkeypox virus (MPXV), which is a member of orthopoxvirus genus. A35R gene is highly conserved among poxviruses and encodes a previously uncharacterized hydrophobic acidic protein. The A35R has little homology to any protein outside of poxviruses, suggesting a novel virulence mechanism.A35R could block some stage of antigen processing or presentation in infected cells or interfere with regulation of apoptosis. In addition, the A35R function may be required for growth in certain cell types, e.g., macrophage, in vivo. It localizes to factories where viral DNA is located and it was shown to be a constitutive transcriptional activator in a large-scale yeast two-hybrid study... Read More |