Understanding the role of microperimetry in glaucoma
Ligand-Directed GPCR Antibody Discovery
Developing affinity reagents recognizing and modulating G-protein coupled receptors (GPCR) function by traditional animal immunization or in vitro screening methods is challenging. Some anti-GPCR antibodies exist on the market, but the success rate of development is still poor compared with antibodies targeting soluble or peripherally anchored proteins.
- More importantly, most of these antibodies do not modulate GPCR function. The current pipeline for antibody development primarily screens for overall affinity rather than functional epitope recognition. We developed a new strategy utilizing natural ligand affinity to generate a library of antibody variants with an inherent bias toward the active site of the GPCR.
- Instead of using phage libraries displaying antibodies with random CDR sequences at polymorphism sites observed in natural immune repertoire sequences, we generated focused antibody libraries with a natural ligand encoded within or conjugated to one of the CDRs or the N-terminus.
- To tailor antibody binding to the active site, we limited the sequence randomization of the antibody in regions holstering the ligand while leaving the ligand-carrying part unaltered in the first round of randomization. With hits from the successful first round, the second round of randomization of the ligand-carrying part was then performed to eliminate the bias of the ligand.
- Based on our results on three different GPCR targets, the proposed pipeline will enable the rapid generation of functional antibodies (both agonists and antagonists) against high-value targets with poor function epitope exposures including GPCR, channels, transporters as well as cell surface targets whose binding site is heavily masked by glycosylation.
endohedral trihedral metallo-borospherenes with spherical aromaticity
It is well-known that transition-metal-doping induces dramatic changes in the structures and bonding of small boron clusters, as demonstrated by the newly observed perfect inverse sandwich D8h [La(η8-B8)La] and D9h [La(η9-B9)La]–. Based on extensive global minimum searches and first-principles theory calculations, we predict herein the possibility of perfect endohedral trihedral metallo-borospherene D3h La@[La5&B30] (1, 3A’1) and its monoanion Cs La@[La5&B30]– (2, 2A’) and dianion D3h La@[La5&B30]2- (3, 1A’1).
These La-doped boron clusters are composed of three inverse sandwich La(η8-B8)La on the waist and two inverse sandwich La(η9-B9)La on the top and bottom which share one apex La atom at the center and six periphery B2 units between neighboring η8-B8 and η9-B9 rings, with three octo-coordinate La atoms and two nona-coordinate La atoms as integrated parts of the cage surface.
Detailed adaptive natural density partitioning (AdNDP) and iso-chemical shielding surface (ICSS) analyses indicate that La@[La5&B30]0/-/2- (1/2/3) are spherically aromatic in nature. The one-dimensional nanowire La4B21 (4, Pm) constructed from D3h La@[La5&B30] (1) along the C3 axis of the system appears to be metallic. The IR and Raman spectra of La@[La5&B30] (1) and photoelectron spectroscopy of the slightly distorted Cs La@[La5&B30]– (2) are theoretically simulated to facilitate their spectroscopic characterizations.
Towards the saving of global rainforests
Recombinant Human Serine racemase |
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0.02mg(E-Coli) | 320 EUR |
Recombinant Human Serine racemase |
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0.1mg(E-Coli) | 520 EUR |
Recombinant Human Serine racemase |
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1mg(E-Coli) | 1925 EUR |
Recombinant Human Serine racemase |
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5x1mg(E-Coli) | 8405 EUR |
Recombinant Human Serine Racemase |
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0.001mg | 240 EUR |
Recombinant Human Serine Racemase |
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0.005mg | 310 EUR |
Recombinant Human Serine Racemase |
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0.05mg | 1260 EUR |
Recombinant Human Serine Racemase |
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5x0.05mg | 5345 EUR |
Recombinant Human Serine racemase |
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0.05mg | 405 EUR |
Recombinant Human Serine racemase |
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0.2mg | 760 EUR |