| Description | C-Reactive Protein (CRP) is a homopentameric protein with a monomer size of ~24 kDa. It is a member of the pentraxin family, a family of proteins characterized by their calcium dependent ligand binding and unique ring-like structure. Like many other pentraxins, CRP is highly upregulated in the acuteC-Reactive Protein (CRP) is a homopentameric protein with a monomer size of ~24 kDa. It is a member of the pentraxin family, a family of proteins characterized by their calcium dependent ligand binding and unique ring-like structure. Like many other pentraxins, CRP is highly upregulated in the acute-phase response to bodily insults such as tissue injuries, infections and general inflammation. In normal, healthy individuals the concentration of CRP in blood is ~5 mg/ml. This number rises 5-10 fold in response to infection or other causes of inflammation. In severe cases, CRP levels can rise above 200 mg/L. CRP can be used as a biomarker for general inflammation or more specific issues such as certain cancers, diabetes, hypertension, cardiovascular disease (CVD) or Rheumatoid Arthritis (RA). On a cellular/molecular level, CRP activates the complement system of the immune response by binding to surface molecules on dead/dying cells or foreign/invading bacteria. Laboratories and companies investigating the diseases mentioned, complement system induction or the acute phase would find our CRP a useful reagent in their studies. Prepared from plasma shown to be non reactive for HBsAg, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA-required tests. Aladdin products are laboratory reagents and are not to be administered to humans or used for any drug purpose. For research or further manufacturing use only... Read More | Inquire | Inquire | 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 | Purity> 97 % by SDS-PAGE and HPLC analyses.FunctionReceptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation whichPurity> 97 % by SDS-PAGE and HPLC analyses.FunctionReceptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. Contributes to the induction of non-cytocidal TNF effects including anti-viral state and activation of the acid sphingomyelinase... Read More |