| Description | Non-specific monocyte binding remains a ubiquitous challenge in flow cytometry. Although the exact mechanism is undefined, literature implicates CD64 interactions with cyanine dyes. However, our data demonstrate that non-specific binding extends beyond cyanine-based fluorophores: certain non-cyanineNon-specific monocyte binding remains a ubiquitous challenge in flow cytometry. Although the exact mechanism is undefined, literature implicates CD64 interactions with cyanine dyes. However, our data demonstrate that non-specific binding extends beyond cyanine-based fluorophores: certain non-cyanine fluorescent dyes also exhibit this phenomenon. Crucially, we observed selective non-specific staining on monocytes for all tested PE and APC tandem dyes. Human Fc Receptor Blocking Solution is a non-antibody blocking solution and has been formulated to block non-specific binding of PE-Cy7, PE-Cy5, PE-Cy5.5, PE-APC, APC-Cy7, and AF647 which is also a cyanine dye commonly appeared on monocytes and macrophages.This buffer contains specialized human IgG containing 0.05% ProClin 300. It is not recommended to be used for staining human IgG. Handle as biohazard agent.Human peripheral blood leukocytes were either not preincubated (Upper Plots) or were preincubated (Lower Plots) with Human Fc Receptor Blocking Solution as indicated. The cells were then selectively stained with either Mouse IgG1-kappa (PE-Cy5.5), anti-E8L (Ab216584), Mouse IgG1-kappa (PE-Cy7), anti-E8L (Ab216583), Mouse IgG2b-kappa (PE-Cy5), anti-E8L (Ab216565), Mouse IgG2c-kappa (PE-Cy5), anti-HEL (Ab212231) or Mouse IgG2c-kappa (PE-Cy7), anti-HEL (Ab212232). Two-dimensional pseudocolor plots of SSC-A vs Mouse IgG show that the Human Fc Receptor Blocking Solution reduces non-specific binding compared to staining without any blocking reagent. Human peripheral blood leukocytes were either not preincubated any blocking reagent (Top Plots) or were preincubated with competitor Fc Receptor Blocking reagent (Middle Plots) or were preincubated with Human Fc Receptor Blocking Solution (Bottom Plots) as indicated. The cells were then selectively stained with either Mouse IgG (APC-Cy7) (Ab213860), Mouse IgG2b-kappa (PE-Cy5), anti-E8L (Ab216565) or Mouse IgG2c-kappa (PE-Cy5), anti-HEL (Ab212231). Two-dimensional pseudocolor plots of SSC-A vs Mouse IgG show that the Human Fc Receptor Blocking Solution reduces non-specific binding compared to staining without any blocking reagent or with competitor Fc Receptor Blocking reagent. ... 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 | Inquire | IRE1α kinase-IN-2 is a potent IRE1α kinase inhibitor, with an EC 50 of 0.82 µM. IRE1α kinase-IN-2 inhibits IRE1α kinase autophosphorylation (IC 50 =3.12 µM). IRE1α kinase-IN-2 inhibits XBP1 mRNA splicing in the WT cell lines.In VitroIRE1α kinase-IN-2 (compoundIRE1α kinase-IN-2 is a potent IRE1α kinase inhibitor, with an EC 50 of 0.82 µM. IRE1α kinase-IN-2 inhibits IRE1α kinase autophosphorylation (IC 50 =3.12 µM). IRE1α kinase-IN-2 inhibits XBP1 mRNA splicing in the WT cell lines.In VitroIRE1α kinase-IN-2 (compound 3) inhibits XBP1 mRNA splicing, even during ER stress. MCE has not independently confirmed the accuracy of these methods. They are for reference only.Form:Solid... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： 100B, previously called S100 beta, belongs to the S100 family within the EF-hand superfamily of Ca2+ binding proteins. S100 proteins contain two EF-hand motifs that differ in affinity, separated by a hingePurity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： 100B, previously called S100 beta, belongs to the S100 family within the EF-hand superfamily of Ca2+ binding proteins. S100 proteins contain two EF-hand motifs that differ in affinity, separated by a hinge region with a hydrophobic cleft that is exposed upon Ca2+ binding. S100B is a 91 amino acid (aa) protein, after removal of the initial methionine, and is found as homodimers of 10.4 kDa monomers. Human S100B shares 99%, 98%, 100%, 99% and 97% aa sequence identity with mouse, rat, rabbit, equine and bovine S100B, respectively. Within the S100 family, human S100B shows the highest aa identity (59%) with S100A1. S100B is expressed primarily by astrocytes and oligodendrocytes in the central nervous system, and by Schwann cells in the peripheral nervous system. Ca2+-bound S100B interacts in vitro with at least 20 cytoplasmic proteins, including several structural molecules such as tubulin and GFAP. It can inhibit the phosphorylation of these kinase substrates and others such as tau and neuromodulin. Astrocytes can secrete S100B, which then acts in a cytokine-like manner. Nanomolar concentrations of S100B are secreted constitutively, promote proliferation, and are neurotrophic and anti-apoptotic. Blood levels of S100B reflect extracellular concentrations within the nervous system, and are elevated in Down’s syndrome, Alzheimer’s disease and Tourette’s syndrome, metabolic stress, acute brain injury and brain tumors. Micromolar concentrations of S100B can be destructive and pro-apoptotic; they induce the expression of iNOS, COX-2, IL-1, IL‑6 and TNF-alpha by microglia, astrocytes or neurons. Most extracellular actions of S100B can be mediated by RAGE (receptor for advanced glycation end products), which is also a receptor for other S100 proteins... Read More |