| Description | HOXC13 Human Pre-designed siRNA Set A contains three designed siRNAs for HOXC13 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components HOXC13 siRNA-1: 5 nmol (HPLC) HOXC13 siRNA-2: 5 nmol (HPLC) HOXC13 siRNA-3: 5 nmol (HPLC) siRNA Negative HOXC13 Human Pre-designed siRNA Set A contains three designed siRNAs for HOXC13 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components HOXC13 siRNA-1: 5 nmol (HPLC) HOXC13 siRNA-2: 5 nmol (HPLC) HOXC13 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 | 4-Methylumbelliferyl α-L-iduronide (free acid) is a fluorogenic substrate for α-L-iduronidase. This is found in cell lysosomes, which is involved in the degradation of glycosaminoglycans. 4-Methylumbelliferyl-α-L-iduronide is cleaved by α-L-iduronidase to release the fluorescent 4-Methylumbelliferyl α-L-iduronide (free acid) is a fluorogenic substrate for α-L-iduronidase. This is found in cell lysosomes, which is involved in the degradation of glycosaminoglycans. 4-Methylumbelliferyl-α-L-iduronide is cleaved by α-L-iduronidase to release the fluorescent moiety 4-methylumbelliferyl (4-MU). This 4-Methylumbelliferyl α-L-iduronide form is the free acid, which offers a considerable weight for weight advantage over the 4-MU iduronide salt in terms of its application dose.:For further studies, use α-L-iduronidase gene silencing:siRNA and shRNA:reagents and α-L-iduronidase gene editing:CRISPR:knockout and activation products... 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 | Biochemical Test:SDS-PAGE (purity > 80%); Western blot with patient sample.Calculated Isoelectric Point:pH 5.68 | Biochemical Test:SDS-PAGE (purity > 80%); Western blot with patient sample.Calculated Isoelectric Point:pH 6.64 |