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Lysosomal Sorting of Amyloid-β by the SORLA Receptor Is Impaired by a Familial Alzheimer’s Disease Mutation includes the most recent citation for our HiLyte Fluor™ labeled β-amyloid peptide. With hundreds of product citations, AnaSpec's products and services have been revered as one of the best in the industry. See for yourself why our customers are so satisfied with the quality of our products and the exceptional services we offer.

  1. Caglayan S, et al. (2014). Lysosomal Sorting of Amyloid-β by the SORLA Receptor Is Impaired by a Familial Alzheimer’s Disease Mutation. Sci. Transl. Med. 6, 223ra20. DOI: 10.1126/scitranslmed.3007747

    SORLA/SORL1 is a neuronal sorting receptor for the amyloid precursor protein that has been implicated in both the sporadic and autosomal dominant forms of Alzheimer’s disease (AD). SORLA concentrations are inversely correlated with β-amyloid in mouse models and AD patents. Caglayan characterized a new mouse model in which SORLA is overexpressed and showed a decrease in β-amyloid concentration in mouse brain. β-amyloid concentration was determined using AnaSpec’s HiLyte Fluor™ labeled β-amyloid peptide.


  2. Zeng Y, et al. (2014). Sphingosine-1-phosphate protects endothelial glycocalyx by inhibiting syndecan-1 shedding. Am J Physiol Heart Circ Physiol. 306, H363-H372. DOI: 10.1152/ajpheart.00687.2013

    Sphingosine-1-phosphate (S1P) in albumin is thought to stabilize surface glycocalyx which is responsible for blood-tissue interface functions. The mechanism of protection from loss of glycocalyx components by S1P-dependent pathways is shown to suppress metalloproteinase (MMP) activity. MMP activity was measured using AnaSpec’s SensoLyte® 390 Generic MMP Assay kit. The researchers were able to conclude that S1P plays a critical role in protecting the glycocalyx via S1P receptors, and inhibits the protease activity-dependent shedding of CS, HS, and the syndecan-1 ectodomain.


  3. Kanda A, et al. (2013). Atp6ap2/(Pro)renin Receptor Interacts with Par3 as a Cell Polarity Determinant Required for Laminar Formation during Retinal Development in Mice. J Neurosci. 49, 19341-19351. DOI: 10.1523/JNEUROSCI.1362-13.2013

    (Pro)renin receptor also known as Atp6ap2, is a key molecule in the tissue renin-angiotensin system (RAS) that plays a role in tissue RAS activation and as a subunit for the vacuolar H+-ATPase proton pump. Kanda’s group studies the novel function of Atp6ap2 required for laminar formation during retinal development. Using AnaSpec’s HiLyte Fluor™ 647 fluorescent dye, they were able to perform IHC experiments to visualize their sections. They postulate that this cellular activity associated with the Par-aPKC system, in addition to the v-ATPase function and tissue RAS activation, is the third biological role of Atp6ap2.


  4. Hoffmann C, et al. (2014). Live cell imaging reveals actin-cytoskeleton-induced self-association of the actin-bundling protein WLIM1. J Cell Sci. 127, 582-598. DOI: 10.1242/jcs.134536

    Hoffmann’s team studies the crosslinking of actin filaments into bundles and the molecular mechanisms underlying actin bundle formation. Using our proprietary HiLyte Fluor™ 488 dye in conjunction with FLIM-FRET, the team was able to develop a model to see how actin binding promotes the formation and stabilization of NtWLIM1 complexes, which is hypothesized to drive the crosslinking of actin filaments.


  5. Quinn SD, et al. (2014). Real-time probing of β-amyloid self-assembly and inhibition using fluorescence self-quenching between neighbouring dyes. Mol. BioSyst. 10, 34-44. DOI: 10.1039/C3MB70272C

    Quinn's group characterized the fluorescence response of AnaSpec’s HiLyte Fluor™ 555-labelled Aβ peptides and demonstrated that Aβ self-assembly organizes the covalently attached probes in close proximity to trigger the self-quenching sensing process over a broad range of conditions. Additionally, they proved that N-terminal tagging of β-amyloid peptides does not alter the self-assembly kinetics or the resulting aggregated structures.


  6. Bush CO, et al. (2014). A Small-Molecule Inhibitor of Hepatitis C Virus Infectivity. Antimicrob. Agents Chemother. 58, 386-396. DOI: 10.1128/AAC.02083-13

    Bush C., et al. from Gilead Sciences, Inc. performs TR-FRET experiments using AnaSpec's NS3-4A europium substrate for Time-Resolved Fluorescence. NS3-4A protease activity was used to monitor intracellular HCV replication levels and was measured by using a europium-labeled NS3-4A protease substrate.


  7. Scruggs BA, et al. (2013). Age of the Donor Reduces the Ability of Human Adipose-Derived Stem Cells to Alleviate Symptoms in the Experimental Autoimmune Encephalomyelitis Mouse Model. Stem Cells Trans Med. 2, 797-807. DOI: 10.5966/sctm.2013-0026

    Mice were induced with chronic experimental autoimmune encephalomyelitis (EAE) using the myelin oligodendrocyte glycoprotein35–55 peptide and treated before disease onset with ASCs derived from younger (<35 years) or older (>60 years) donors. AnaSpec’s MOG 35–55 peptide was administered to the mice to induce chronic EAE, which models PPMS more than other MS forms.


  8. Semon JA, et al. (2013). Administration of Murine Stromal Vascular Fraction Ameliorates Chronic Experimental Autoimmune Encephalomyelitis. Stem Cells Trans Med. 2, 789-796. DOI: 10.5966/sctm.2013-0032

    The ability of murine SVF cells to treat myelin oligodendrocyte glycoprotein 35–55-induced experimental autoimmune encephalitis (EAE) was compared with that of culture-expanded ASCs in C57Bl/6J mice. Chronic EAE was induced in these animals by subcutaneous immunization using AnaSpec’s MOG 35–55 peptide.


  9. Somarowthu S, et al. (2013). Visualizing the ai5γ group IIB intron. Nucl. Acids Res. 1-12. DOI:

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