| Quantity | 1Set | 100mg, 5mg, 2mg, 1mg, 25mg | 1ml | 100g, 500mg, 25g, 25mg, 100mg, 1g, 5g | 100µg, 10µg, 50µg, 1mg |
| Description | ILVBL Human Pre-designed siRNA Set A contains three designed siRNAs for ILVBL gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components ILVBL siRNA-1: 5 nmol (HPLC) ILVBL siRNA-2: 5 nmol (HPLC) ILVBL siRNA-3: 5 nmol (HPLC) siRNA Negative Control:ILVBL Human Pre-designed siRNA Set A contains three designed siRNAs for ILVBL gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components ILVBL siRNA-1: 5 nmol (HPLC) ILVBL siRNA-2: 5 nmol (HPLC) ILVBL 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 | 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 | InformationMyelin Oligodendrocyte Glycoprotein 35-55, mouse, rat (MOG 35-55) is a minor component of CNS myelin that induces experimental autoimmune encephalomyelitis in C57BL/6 mice by an encephalitogenic T cell response | Product IntroduceProteinase K, originally isolated from the mold Tritirachium album, is a serine protease with broad substrate specificity and relatively high proteolytic activity. It preferentially cleaves ester and peptide bonds adjacent to the C-termini of hydrophobic, aliphatic, or aromatic Product IntroduceProteinase K, originally isolated from the mold Tritirachium album, is a serine protease with broad substrate specificity and relatively high proteolytic activity. It preferentially cleaves ester and peptide bonds adjacent to the C-termini of hydrophobic, aliphatic, or aromatic amino acids. aladdin's proteinase K is characterized by high purity, sterility, no bio-burden, and no presence of DNAse, RNAse, DNA, and RNA contaminants. It is a good partner in DNA and RNA extraction for you.Features1、According to the SDS-PAGE image,the purity of Proteinase K is more than 95% and the molecular weight is 28.9 kDa.2、Detect DNase residue by agarose gel electrophores.3、Detect Nucleic acid residue by agarose gel electrophores.4、Detect RNase residue by agarose gel electrophores.5、Using the absorbance A275 as the vertical axis and different concentrations of tyrosine as the horizontal axis, a standard curve was drawn, and the enzyme activity was calculated>30U/mg... Read More | purity>97% by SDS-PAGE and HPLC analysesFunctionFunctionElicits growth inhibition on melanoma cells in vitro as well as some other neuroectodermal tumors, including gliomas.Post-translationalMay possess two intramolecular disulfide bonds |