| Description | Endothelin-1 (1-31) (Human) TFA is a potent vasoconstrictor and hypertensive agent. Endothelin-1 (1-31) (Human) TFA is derived from the selective hydrolysis of big ET-1 by chymase.Appearance:SolidIn Vitro:Endothelin-1 (1-31) (Human) (100 pM-100 nM; 24 h) TFA induces human mesangial cells Endothelin-1 (1-31) (Human) TFA is a potent vasoconstrictor and hypertensive agent. Endothelin-1 (1-31) (Human) TFA is derived from the selective hydrolysis of big ET-1 by chymase.Appearance:SolidIn Vitro:Endothelin-1 (1-31) (Human) (100 pM-100 nM; 24 h) TFA induces human mesangial cells proliferation. Endothelin-1 (1-31) (Human) (100 nM; 0-10 min) TFA induces ERK activation in human mesangial cells. MCE has not independently confirmed the accuraIn Vivo:ET-1 (1-31) (100 nM; single dose) TFA induces contraction in the mouse mesenteric artery. The contraction may be mediated by the ET A receptor and may be increased by aging. A clear difference exists between males and females in the present chronic diabetBiological Activity:Endothelin-1 (1-31) (Human) TFA is a potent vasoconstrictor and hypertensive agent. Endothelin-1 (1-31) (Human) TFA is derived from the selective hydrolysis of big ET-1 by chymase... Read More | Inquire | Mammalian lactate dehydrogenases (LDH) exist as five tetrameric isozymes composed of combinations of two different subunits. The H subunit predominates in heart muscle, which is geared for aerobic oxidation of pyruvate. The M subunit predominates in skeletal muscle and is concerned more with Mammalian lactate dehydrogenases (LDH) exist as five tetrameric isozymes composed of combinations of two different subunits. The H subunit predominates in heart muscle, which is geared for aerobic oxidation of pyruvate. The M subunit predominates in skeletal muscle and is concerned more with anaerobic metabolism and pyruvate reduction.Catalyzes the interconversion of pyruvate and lactate with concomitant interconversion of NADH and NAD+Recombinant rabbit muscle Lactate Dehydrogenase produced in E.Coli. Chromatographically purified. A lyophilized powder... Read More | TEV Protease is the 241 amino acid (aa), 27 kDa catalytic domain of the nuclear inclusion a (NIa) protein encoded by the potyvirus, tobacco etch virus (TEV). It may be used in biotechnology to cleave affinity tags from recombinant proteins, either co-translationally orin vitrofollowing purification.TEV Protease is the 241 amino acid (aa), 27 kDa catalytic domain of the nuclear inclusion a (NIa) protein encoded by the potyvirus, tobacco etch virus (TEV). It may be used in biotechnology to cleave affinity tags from recombinant proteins, either co-translationally orin vitrofollowing purification. Its high specificity and activity at a wide range of pH and ionic strength make TEV Protease more versatile than many other proteases used for the same purpose. Unlike factor Xa, enteropeptidase or thrombin, TEV Protease has not been found to cleave at unintended sites, even when present at a high concentration. TEV Protease is a 3C-type protease that cleaves substrates with a consensus sequence of ENLYFQG. Cleavage occurs between Q and G. Since the final aa remains on the cleaved protein where it could potentially affect structure or function, substitution of a variety of aa have been tested. In order of efficiency, S, A, M, Y, D, N, E, K or L may be effectively used in place of G. Several of the remaining aa may also vary, giving a final consensus sequence of ExxYF(M)Q(E)/G(S, A or others) where aa in parenthesis are alternatives and x is any aa. The autocatalytic site of NIa at S2256 has been mutated to an N for improved stability of the protease.Tobacco Etch Virus Protease is a highly site-specific cysteine protease that is found in the tags from fusion proteins. The optimal temperature for cleavage is 30°C. It is recommended that the cleavage for each fusion protein be optimized by varying the amount of recombinant viral TEV protease, reaction time, or incubation temperature. It can be removed by Ni2+ affinity resin... Read More | Inquire |