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provides coniferyl ferulate(CAS#:5353-15-1) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate
There are distinctive areas of colocalization of matrix metalloproteinase (MMP)-2 and -14 on trabecular meshwork (TM) cells that resemble podosomes or invadopodia. Studies were conducted to determine whether TM cells exhibit podosome- or invadopodia-like structures (PILS) and whether they produce focal extracellular matrix (ECM) turnover.
Porcine and human TM cells and perfused anterior segment organ cultures were studied. Localization of PILS components on TM cells and in sections from anterior segments was determined by immunohistochemistry and confocal microscopy. Cells were grown on type I collagen labeled with fluorescein isothiocyanate (FITC) for degradation analysis. Confocal time lapse images were taken of labeled TM cells on FITC-collagen.
Immunostaining for MMP-2, MMP-14, and the typical PILS components cortactin, caldesmon, α-actinin, N-WASP, Arp-3, and cdc42 colocalized on these distinctive structures. Integrin-αV and -β1, fibronectin, and versican colocalized with PILS components. TM cells on FITC-conjugated collagen developed focal regions of degradation. Time-lapse imaging showed dramatic and controlled movement of TM cell processes during this ECM degradation and fragment internalization. MMP-2, MMP-14, and cortactin colocalized at regions that appear to be PILS on cells within the outflow pathway in sections of human anterior segments.
TM cells exhibit areas where PILS components colocalize with MMP-2 and -14. Similar structures are found in sections, suggesting that PILS occur in situ in the outflow pathway. The collagen degradation suggests that PILS may serve as focal sites for targeted ECM turnover, an event linked to modifications of aqueous outflow resistance and intraocular pressure homeostasis.
Specialized Podosome- or Invadopodia-like Structures (PILS) for Focal Trabecular Meshwork Extracellular Matrix Turnover
Mini Aga, John M. Bradley, Kate E. Keller, Mary J. Kelley, and Ted S. Acott
2009 Dec 1.
Coupling efficiencies for the covalent attachment of oligonucleotides (17-29 bases in length) to solid supports derivatized with alkyl-amino and -carboxylic functionalities have been determined. Attachment efficiencies of 60-80% were obtained for coated long-chain alkylamino controlled pore glass (CPG) supports. Similar efficiencies of immobilization were observed for carboxyl-bearing supports, which additionally exhibited lower levels of non-covalent binding. The extent of terminally linked oligonucleotide was determined to be 50-55% of the overall attachment in the carbodiimide-mediated coupling reaction of a 5′-aminohexyl phosphoramidate derivative of a 29-mer to Sephacryl carboxyl support. While lower overall efficiencies of attachment were obtained in the reaction with Sephacryl N-hydroxysuccinimide-activated carboxyl support, greater than 80% of this coupling results in end-attached oligonucleotides.
Covalent attachment of oligonucleotides to solid supports.
S S Ghosh and G F Musso
1987 Jul 10;
Pancreata of fetal, neonatal and adult cattle were studied immunohistochemically for galanin. The results revealed galanin-like immunoreactivity both in the endocrine cells and in the neural elements. The galanin-like immunoreactive endocrine cells (Gal-LIEC) were confined to the large islets, and were not observed in the islets of Langerhans and exocrine pancreas. They were first detected at the third prenatal month. Their developmental profile showed an increase from fetal to early neonatal stage with a subsequent decrease towards adulthood. The considerable number of Gal-LIEC from late prepartum to early postpartum stage may imply functional significance of galanin during the perinatal development of cattle. Coexistence of galanin and insulin was also observed which may suggest autocrine interaction between the 2 hormones.
Immunohistochemistry, insulin, large islets, cattle
Galanin-like immunoreactive endocrine cells in bovine pancreas
EMMANUEL T. BALTAZAR,1 NOBUO KITAMURA,1 EIICHI HONDO,1 ERLINDA C. NARRETO,2 and JUNZO YAMADA1