| Description | ERLIN2 Human Pre-designed siRNA Set A contains three designed siRNAs for ERLIN2 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components ERLIN2 siRNA-1: 5 nmol (HPLC) ERLIN2 siRNA-2: 5 nmol (HPLC) ERLIN2 siRNA-3: 5 nmol (HPLC) siRNA Negative ERLIN2 Human Pre-designed siRNA Set A contains three designed siRNAs for ERLIN2 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components ERLIN2 siRNA-1: 5 nmol (HPLC) ERLIN2 siRNA-2: 5 nmol (HPLC) ERLIN2 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 | Amyloid β-Protein Fragment 25-35 (Aβ25-35) is derived from the amyloid-β protein.amyloid-β protein, which is mapped to human chromosome 21q21.Aβ25-35 lacks the N-terminal domain and the metal binding site and is majorly generated by proteolytic cleavage of Aβ(1−40Amyloid β-Protein Fragment 25-35 (Aβ25-35) is derived from the amyloid-β protein.amyloid-β protein, which is mapped to human chromosome 21q21.Aβ25-35 lacks the N-terminal domain and the metal binding site and is majorly generated by proteolytic cleavage of Aβ(1−40) peptides. It has a β-sheet and β-turn structure. Amino Acid Sequence Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-MetFunctional domain of Aβ required for both neurotrophic and neurotoxic effects... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description: This protein is a cell adhesion molecule involved in neuron-neuron adhesion, neurite fasciculation, outgrowth of neurites, etc | 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 |