| Description | C9orf78 Human Pre-designed siRNA Set A contains three designed siRNAs for C9orf78 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components C9orf78 siRNA-1: 5 nmol (HPLC) C9orf78 siRNA-2: 5 nmol (HPLC) C9orf78 siRNA-3: 5 nmol (HPLC) siRNA C9orf78 Human Pre-designed siRNA Set A contains three designed siRNAs for C9orf78 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components C9orf78 siRNA-1: 5 nmol (HPLC) C9orf78 siRNA-2: 5 nmol (HPLC) C9orf78 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 | Purity: >95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description:Cyclophilin B (SCYLP, CyPB, and peptidyl-prolyl cis-trans isomerase B) is a 24 kDa glycoprotein member of the B subfamily of the cyclophilin-type PPIase family of molecules. It is both secreted and retained in Purity: >95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description:Cyclophilin B (SCYLP, CyPB, and peptidyl-prolyl cis-trans isomerase B) is a 24 kDa glycoprotein member of the B subfamily of the cyclophilin-type PPIase family of molecules. It is both secreted and retained in the ER. When secreted, it mediates chemotaxis and T cell adhesion to fibronectin. This is likely due to its prolyl cis/trans isomerase activity. Intracellularly, Cyclophilin B appears to serve as a molecular chaperone for molecules destined for secretion. It does so via stabilization and facilitating the activity of additional chaperones. The human CyPB precursor is 216 amino acids (aa) in length. It contains a 25 aa signal sequence plus a 191 aa mature region. There is a partial heparin-binding sequence (aa 27‑34), a PPIase domain (aa 47‑204), and a C-terminal ER retention motif (aa 213‑216). Over aa 34‑216, the human and mouse sequences are 95% aa identical... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description:The HRV 3C Protease is a recombinant cysteine protease from human rhinovirus 3C (HRV 3C)expressed in and purified from Escherichia coli. HRV 3C Protease cleaves protein substrates with the recognition Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description:The HRV 3C Protease is a recombinant cysteine protease from human rhinovirus 3C (HRV 3C)expressed in and purified from Escherichia coli. HRV 3C Protease cleaves protein substrates with the recognition sequence Leu-Glu-Val-Leu-Phe-Gln-Gly-Pro between the Gln and Gly residues. The high specificity and affinity tags( 6xHis) of the protease make it an ideal choice for the removal of purification and detection tags on recombinant proteins and allows for flexibility in protease removal.Source:HRV 3C Protease is a recombinant cysteine protease from human rhinovirus 3C (HRV 3C) expressed in and purified from Escherichia coli.HRV 3C enzyme digestion of His-GST-IL33 protein, according to the mass ratio (HRV 3C: target protein) 1:25 and 1:50 enzyme digestion, overnight at 4℃ enzyme digestion results are as follows: completely clean enzyme digestion... Read More | Purity: >90%, by SDS-PAGE visualized with Coomassie® Blue Staining. Function:Actin cross-linking/gelling protein (By similarity). Involved in calcium interactions and contractile properties of the cell that may contribute to replicative senescence |