| Type | Bioactive Small Molecules | Chelating Agents & Ligands | Chelating Agents & Ligands | Chelating Agents & Ligands | Chelating Agents & Ligands |
| Description | HOXA1 Human Pre-designed siRNA Set A contains three designed siRNAs for HOXA1 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components HOXA1 siRNA-1: 5 nmol (HPLC) HOXA1 siRNA-2: 5 nmol (HPLC) HOXA1 siRNA-3: 5 nmol (HPLC) siRNA Negative Control:HOXA1 Human Pre-designed siRNA Set A contains three designed siRNAs for HOXA1 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components HOXA1 siRNA-1: 5 nmol (HPLC) HOXA1 siRNA-2: 5 nmol (HPLC) HOXA1 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 | Inquire | Inquire | 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 | Trypsin is a member of the serine protease family. Trypsin cleaves peptides on the C-terminal end of lysine and arginine amino acid residues. The pH optimum of trypsin is pH 7 - 10. The enzyme is inhibited by serine protease inhibitors, e.g. PMSF, and by metal chelating agents, e.g., EDTA. Trypsin is a member of the serine protease family. Trypsin cleaves peptides on the C-terminal end of lysine and arginine amino acid residues. The pH optimum of trypsin is pH 7 - 10. The enzyme is inhibited by serine protease inhibitors, e.g. PMSF, and by metal chelating agents, e.g., EDTA. Recombinant Human Trypsin is a genetically engineered protein expressed in E.coli and purified by high pressure liquid chromatography. There are no contaminating enzyme activities such as carboxypeptidase A and chymotrypsin. No protease inhibitors such as PMSF are contained in the preparation.Animal origin free:The use of recombinant Human Trypsin eliminates the risk of virus presence, and of any other potential adventitious agents found in animal pancreas-derived trypsin. Recombinant human trypsin:The amino acid sequence is the same as the Human Trypsin 2.Stable:A sterile recombinant human trypsin lyophilized eliminates the contamination risks and decreases the chance of activity loss in the process of transport and storage.High purity:(1) Recombinant human trypsin provides increased specificity and eliminates contaminating activities found in lower purity enzymes.(2) No other contaminating proteases such as chymotrypsin or carboxypeptidase A... Read More |