A highly purified protein for fatty acid research

Source: recombinant N-terminal hexahistidine-tagged protein expressed in E. coli · M_r: 18.3 kDa ·

A highly purified protein for fatty acid research

Source: recombinant N-terminal hexahistidine-tagged protein expressed in E. coli · M_r: 18.3 kDa · Protein concentration: 0.5 mg/ml · Fatty acid binding protein 1 (FABP1) is one of nine known cytosolic FABPs ranging in size from 14-15 kDa containing 127-132 amino acids. FABP1 is composed of ten antiparallel β strands that form a barrel with a bigger binding pocket than the other FABPs allowing it to accommodate two fatty acids. Expression of FABP1 is decreased in hepatoblastoma and hepatocellular carcinoma making the protein a potential tumor marker. Moreover, studies have suggested FABP1 as a potential biomarker for both liver and kidney injury. Cayman’s FABP1 has been functionally characterized by a fluorescence displacement assay using the fluorescent fatty acid analogue 11-(dansyl amino)undecanoic acid (DAUDA). Both arachidonic acid and oleic acid effectively displace DAUDA from the FABP binding pocket in a concentration-dependent manner.

Pure inactive precursor of renin

Source: recombinant enzyme expressed in HEK cells · M_r: 45 kDa · Prorenin is the inactive precursor of renin, which is a key enzyme in the regulation of blood pressure and electrolyte balance. In renal juxtaglomerular cells, sequential cleavage of the N-terminal 20 and 46 amino acids of preprorenin produces prorenin and active renin, respectively. Renin catalyzes the conversion of angiotensinogen to angiotensin I. Prorenin exhibits 5-10% of the proteolytic activity of renin, however, the blood circulating levels are 10 times higher.

Pure active enzyme for drug discovery research

Renin is an aspartyl protease of approximately 40 kDa produced in the kidney by juxtaglomerular cells of the macula densa. Renin converts angiotensinogen into angiotensin I, activating a major arm of renal sodium and volume auto-regulation. The enzyme provided by Cayman Chemical is the active, 340 amino acid protease produced in HEK cells transfected with a human renin expression construct.

Source: recombinant C-terminal FLAG-tagged protein expressed in E. coli · M_r: 76.3 kDa ·