Journal: Journal of immunology (Baltimore, Md. : 1950)

Article Title: Immunoregulatory activity of the natural product laminarin varies widely as a result lt of its physical properties 1

doi: 10.4049/jimmunol.1701258

Figure Lengend Snippet: Saturation binding curves for rh and rm-Dectin-1 and two of the laminarins are shown. N=6 replicates for each laminarin and each receptor. At minimum a three log concentration range was employed with at least 10 data points for each analysis.

Article Snippet: Samples were analyzed for binding to recombinant human or mouse Dectin-1 (R&D Systems cat #1859-DC-050 and 1756-DC-050 respectively; both are C-terminal, extracellular truncated versions containing a 10 His N terminal tag) with an Octet Ks bio-layer interferometry instrument manufactured by ForteBio (Fremont CA).

Techniques: Binding Assay, Concentration Assay

Journal: Journal of immunology (Baltimore, Md. : 1950)

Article Title: Immunoregulatory activity of the natural product laminarin varies widely as a result lt of its physical properties 1

doi: 10.4049/jimmunol.1701258

Figure Lengend Snippet: A. Dectin-1 in RAW or THP-1 cells was silenced using lentiviral particles containing shRNA targeted against the murine and human Clec7a gene. Control cells were also lentivirally transduced with a non-targeting shRNA against GFP. After antibiotic selection, single cell clones were propagated and screened for loss of Dectin-1 mRNA expression using qPCR (left) or protein expression (right). For protein analysis in RAWs, cells were pretreated with 30 μg/ml zymosan. Numbers under blots represent relative level of Dectin-1 protein vs. control cells as determined by quantification using the software ImageJ and normalization to actin protein levels. Dashed lines indicate image splicing to remove irrelevant lanes. B. TNFα production in response to 24 h treatment of the indicated cells, control (red) or Dectin-1 knockdown (black; clone 6 and clone 3 for RAW and THP-1, respectively), with increasing concentrations of indicated laminarin. Graphs are one representative experiment of at least three replicates.

Article Snippet: Samples were analyzed for binding to recombinant human or mouse Dectin-1 (R&D Systems cat #1859-DC-050 and 1756-DC-050 respectively; both are C-terminal, extracellular truncated versions containing a 10 His N terminal tag) with an Octet Ks bio-layer interferometry instrument manufactured by ForteBio (Fremont CA).

Techniques: shRNA, Transduction, Selection, Clone Assay, Expressing, Software

Journal: Glycovirology Protocols

Article Title: The C Type Lectins DC-SIGN and L-SIGN

doi: 10.1007/978-1-59745-393-6_4

Figure Lengend Snippet: Structure of DC-SIGN and L-SIGN proteins. The C-type lectins DC-SIGN and L-SIGN are type II transmembrane proteins. Their cytoplasmic tails contain internalization signals (di-leucine, tyrosine, and tri-acidic) which are involved in internalization of the lectin. The extracellular domain is composed of a carbohydrate recognition domain (CRD) and a neck domain (conserved in the case of DC-SIGN, variable for L-SIGN) implicated in the oligomerization of these lectins. The oligomerization is probably important for the orientation and subsequently for the function of the CRDs.

Article Snippet: Phycoerythrin (PE)-conjugated mouse monoclonal antibodies (mAbs) directed against DC-SIGN (FAb161P), L-SIGN (FAb162P), or both lectins (FAb1621P) were purchased from R&D Systems.

Techniques: