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Cocktails, tablets, capsules, and individual purified formulations of protease inhibitors and phosphatase inhibitors designed to protect proteins from degradation during cell lysis and extraction.
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A potent cathepsin L inhibitor (IC50 = 0.85 nM); selective for cathepsin L over calpain II and cathepsin B (IC50s = 184, and 85.1 nM, respectively); trypanocidal against T. brucei (ED50 = 45 nM); completely suppresses osteoclastic pit formation on femur slices isolated from bovine cortical bone at a concentration of 1 μg/ml; inhibits bone loss in a mouse model of osteoporosis in a dose-dependent manner
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These Serine Protease Assay Kits enable researchers to detect intracellular chymotrypsin-like serine protease activity in vitro without lysing the cell.
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R406 (free base) is a potent Syk inhibitor with IC50 of 41 nM in a cell-free assay, strongly inhibits Syk but not Lyn, 5-fold less potent to Flt3. R406 (free base) triggers apoptosis. Phase 1. *For Research & Development use only. Product is not intended for drug, household, or human consumption.
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MF: C21H24NNaO8S, MW: 473.47, Synonyms: ON-01910, Estybon. Solubility: 23.65mg/mL in DMSO. Rigosertib (ON-01910,Estybon) is a potent, specific PLK1 inhibitor with IC50 value of 9nM.
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Competitive serine protease inhibitor which forms stable complexes with and blocks the active sites of enzymes. The binding is reversible, and most aprotinin-protease complexes dissociate at a pH>10 or <3.2. Target enzumes include trypsin, chymatrypsin, kalikrein and plasmin.
Activity: >4500 KIU/mg
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EGFR inhibitor. Potent and selective inhibitor of EGFR (IC50 = 3nM). Reduces EGF-stimulated DNA synthesis in Rat-1 fibroblasts by ~75% at 0.25μM. Blocks EGF-dependent src-family kinase activation and p21/Cip 1/WAF1 induction in A431 cells. Also inhibits H2O2-induced stimulation of amphiregulin expression in rat gastric epithelium (RGM 1) cells. Alternative name: 4-(3-Chloroanilino)-6,7-dimethoxyquinazoline. Formula: C16H14ClN3O2. MW: 315.8. Purity: ≥98% (HPLC). Appearance: White to light yellow solid. Solubility: Soluble in DMSO (10mg/ml). Long Term Storage: -20°C. Handling: Protect from light. Packaged under inert gas.
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SUMO proteases are a general class of enzymes that specifically remove the post-translational protein modification (PTM) known as small ubiquitin-related modifier (SUMO) which falls into the PTM class of ubiquitin and/or ubiquitin-like proteins (UBL). The enzyme commonly referred to as SUMO protease is the Ubl-specific protease 1 (Ulp1) from Saccharomyces cerevisiae. This was the first of this class of enzymes to be isolated. SUMO protease specifically cleaves the SUMO moiety in a scarless manner. SUMO protease recognizes the tertiary structure of the Ubiquitin-like SUMO domain and hydrolyzes the peptide bond in the x-Gly-Gly-x sequence after the Gly-Gly bond at the C-terminus of the SUMO domain. In addition to cleavage of natural SUMO-modified proteins SUMO protease is used to cleave recombinant SUMO fusion proteins. The SUMO domain is a known solubility-enhancing fusion tag used in recombinant protein expression. A histidine tag can also be added at the N-terminus of the SUMO doma
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A potent inhibitor of Aurora A kinase (IC50 = 42 nM); selective for Aurora A over BMX, BTK, IGF-1R, c-Src, TRKB, SYK, and EGFR (IC50s = 386, 3,550, 591, 1,980, 2,510, 887, and >10,000 nM, respectively)
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