| Description | IRBP (1-20), human contains a major epitope for the H-2 b haplotype. IRBP (1-20), human induces experimental autoimmune uveoretinitis (EAU) in H-2 b mice.In VivoIRBP (1-20), human TFA induces EAU. For determination of proliferative and cytokine responses, lymph node and spleen cells are collected 21IRBP (1-20), human contains a major epitope for the H-2 b haplotype. IRBP (1-20), human induces experimental autoimmune uveoretinitis (EAU) in H-2 b mice.In VivoIRBP (1-20), human TFA induces EAU. For determination of proliferative and cytokine responses, lymph node and spleen cells are collected 21 days after immunization and are stimulated in culture with the appropriate antigen. Cells of C57BL/6 mice and 129/J mice immunized with IRBP (1-20), human TFA proliferated in response to the peptide. MCE has not independently confirmed the accuracy of these methods. They are for reference only. Animal Model: C57BL/6 (H-2 bbDosage: 200, 300 µg Administration: I.h.; After 21 days Result: C57BL/6 (H-2 bb ) also developed disease, albeit with a lower average score than C57BL/6.Form:Solid... 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 6.10 | Format:1-ComponentEnzyme:Horseradish peroxidase | Trypsin is a pancreatic serine protease with substrate specificity based upon positively charged lysine and arginine side chains. It is derived from a 34 kDa inactive precursor zymogen, trypsinogen, after enzymatic removal of an N-terminal 6-amino acid leader sequence resulting in the 23.8 kDa Trypsin is a pancreatic serine protease with substrate specificity based upon positively charged lysine and arginine side chains. It is derived from a 34 kDa inactive precursor zymogen, trypsinogen, after enzymatic removal of an N-terminal 6-amino acid leader sequence resulting in the 23.8 kDa trypsin molecule. The optimum pH is 8.0. Trypsin is inhibited by organophosphorus compounds such as diisopropylfluorophosphate and natural inhibitors from pancreas. Soybean, lima bean, and egg white are also sources of natural inhibitors. Trypsin cleaves amide and ester bonds of Arg and Lys. The Aladdin Sequencing Grade Trypsin has been further purified to remove trace contaminating proteases and autolysis products which could interfere in trypsin digestion experiments, and exhibits a single band on PAGE.Trypsin is a serine protease used to hydrolyze proteins. Trypsin from bovine pancreas has a molecular weight of 23.8 kDa. Trypsins are used for the re-suspension of cells during cell culture and in proteomics research for the digestion of various proteins... Read More |