| Description | NeutrAvidin Protein is a specially-prepared form of avidin that decreases background in biotin-binding.Features include:• Near-neutral isoelectric point—pI = 6.3, more neutral than native avidin• Nearly devoid of glycosylation—decreased possibility of lectin binding compared NeutrAvidin Protein is a specially-prepared form of avidin that decreases background in biotin-binding.Features include:• Near-neutral isoelectric point—pI = 6.3, more neutral than native avidin• Nearly devoid of glycosylation—decreased possibility of lectin binding compared to native avidin• No RYD recognition sequence—no known off-target binding domains like streptavidin• Affordable—significantly less expensive than streptavidinNeutrAvidin Protein is deglycosylated native avidin from egg whites. Removal of the excess carbohydrate by an exclusive process yields a protein with a more neutral isoelectric point and less nonspecific binding properties. Purified NeutrAvidin Protein provides exceptional performance in western blot, ELISA, and IHC applications that require biotin-binding probes. Assay specificity, sensitivity, and signal-to-noise ratios with NeutrAvidin Protein are generally equivalent or better than with the significantly more expensive streptavidin.Avidin is a glycoprotein found in the egg white and tissues of birds, reptiles, and amphibia. The biotin-binding protein contains four identical subunits having a combined mass of 67,000-68,000 daltons. Removing the glycosylation from avidin yields NeutrAvidin Protein with a mass of 60,000 daltons. Carbohydrate-based lectin binding is reduced to undetectable levels, yet biotin-binding affinity is retained. NeutrAvidin Protein offers the advantages of a neutral pI to minimize nonspecific adsorption, along with lysine residues that remain available for derivatization or other customized conjugation. NeutrAvidin Protein yields the lowest nonspecific binding among the known biotin-binding proteins. The specific activity for biotin binding is approximately 14 µg/mg of protein, which is near the theoretical maximum activity... Read More | Inquire | Nucleoprotein (396-404) is the 396 to 404 fragment of lymphocytic choriomeningitis virus (LCMV). Nucleoprotein (396-404) is the H-2D(b)-restricted immunodominant epitope and can be used as a molecular model of viral antigen.Form:Solid | Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：IL12 is a cytokine that acts on T and natural killer cells, and has a broad array of biological activities. It is a disulfide-linked heterodimer composed of the 40 kD cytokine receptor like subunit and a 35 Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：IL12 is a cytokine that acts on T and natural killer cells, and has a broad array of biological activities. It is a disulfide-linked heterodimer composed of the 40 kD cytokine receptor like subunit and a 35 kD subunit. This cytokine is expressed by activated macrophages that serve as an essential inducer of Th1 cells development. IL12 has been found to be important for sustaining a sufficient number of memory/effector Th1 cells to mediate long-term protection to an intracellular pathogen. Recombinant human IL12 protein, fused to His-tag at C-terminus, was expressed in insect cells using baculovirus expression system and purified by using conventional chromatography techniques... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TREPurity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD3/SMAD4 complex, activates transcription. Also can form a SMAD3/SMAD4/JUN/FOS complex at the AP-1/SMAD site to regulate TGF-beta-mediated transcription. Has an inhibitory effect on wound healing probably by modulating both growth and migration of primary keratinocytes and by altering the TGF-mediated chemotaxis of monocytes. This effect on wound healing appears to be hormone-sensitive. Regulator of chondrogenesis and osteogenesis and inhibits early healing of bone fractures. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator... Read More |