| Description | Cecr2 Mouse Pre-designed siRNA Set A contains three designed siRNAs for Cecr2 gene (Mouse), as well as a negative control, a positive control, and a FAM-labeled negative control. Components Cecr2 siRNA-1: 5 nmol (HPLC) Cecr2 siRNA-2: 5 nmol (HPLC) Cecr2 siRNA-3: 5 nmol (HPLC) siRNA Negative Control:Cecr2 Mouse Pre-designed siRNA Set A contains three designed siRNAs for Cecr2 gene (Mouse), as well as a negative control, a positive control, and a FAM-labeled negative control. Components Cecr2 siRNA-1: 5 nmol (HPLC) Cecr2 siRNA-2: 5 nmol (HPLC) Cecr2 siRNA-3: 5 nmol (HPLC) siRNA Negative Control: 5 nmol (HPLC) FAM-labeled siRNA Negative Control: 5 nmol (HPLC) GAPDH siRNA Positive Control:5 nmol (HPLC)... Read More | Amine-Reactive probe which passively diffuse into cells and it is nonfluorescent until the acetate groups are cleaved by intracellular esterases to yield the highly fluorescent, amine-reactive fluorophore. Upon reaction with amine-containing residues of intracellular proteins, these probes form dye Amine-Reactive probe which passively diffuse into cells and it is nonfluorescent until the acetate groups are cleaved by intracellular esterases to yield the highly fluorescent, amine-reactive fluorophore. Upon reaction with amine-containing residues of intracellular proteins, these probes form dye protein adducts that are well retained in cells as they move and divide during embryonic development.A Non-fluorescent cell permeant amine-reactive probe for long term tracing of cell... Read More | Lipase PS is generally used in the enantioselective transesterification and hydrolysis. Applications include: 1.Lipase catalyzed transesterification of prochiral pyrimidine acyclonucleoside. 2.Lipase catalyzed hydrolysis of diacetylated pyrimidine acyclonucleosides. 3. Enantiomer selective acylationLipase PS is generally used in the enantioselective transesterification and hydrolysis. Applications include: 1.Lipase catalyzed transesterification of prochiral pyrimidine acyclonucleoside. 2.Lipase catalyzed hydrolysis of diacetylated pyrimidine acyclonucleosides. 3. Enantiomer selective acylation of racemic alcohols in continuous-flow bioreactors... 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 | Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description:Neural cell adhesion molecule 1 (NCAM-1) is a multifunctional member of the Ig superfamily. It belongs to a family of membrane-bound glycoproteins that are involved in Ca++ independent cell matrix and homophilic orPurity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description:Neural cell adhesion molecule 1 (NCAM-1) is a multifunctional member of the Ig superfamily. It belongs to a family of membrane-bound glycoproteins that are involved in Ca++ independent cell matrix and homophilic or heterophilic cell-cell interactions. NCAM-1 specifically binds to heparan sulfate proteoglycans, the extracellular matrix protein agrin, and several chondroitin sulfate proteoglycans that include neurocan and phosphocan. There are three main forms of human NCAM-1 that arise by alternate splicing. These are designated NCAM-120/NCAM-1 (761 amino acids [aa]), NCAM‑140 (848 aa), and NCAM-180 (1120 aa). NCAM-120 is GPI-linked, while NCAM‑140 and NCAM-180 are type I transmembrane glycoproteins. Additional alternate splicing adds considerable diversity to all three forms, and extracellular proteolytic processing is possible for NCAM-180. NCAM-1 is synthesized as a 761 aa preproprecursor that contains a 19 aa signal sequence, a 722 aa GPI-linked mature region, and a 20 aa C-terminal prosegment. The molecule contains five C-2 type Ig-like domains and two fibronectin type-III domains. Human to mouse, NCAM-1 is 93% aa identical. NCAM-1 appears to be highly sialylated. The polysialyation of NCAM-1 reduces its adhesive property and increases its neurite outgrowth promoting features. NCAM-1 in the adult brain shows a decline of sialylation relative to earlier developmental periods. In regions that retain a high degree of neuronal plasticity, however, the adult brain continues to express polysialylation-NCAM-1, suggesting sialylation of NCAM-1 is involved in regenerative processes and synaptic plasticity... Read More |