ProSep®A Chromatography Resins: Virus Clearance and Sanitization
- Document Type:
- Technical Information
Prosep resins
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How do I choose between ProSep-vA Ultra versus ProSep-vA High Capacity?…
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Prosep-vA Ultra has a higher binding capacity than ProSep-vA High Capacity - ≥ 56mg/ml vs ≥ 40 mg/ml.
ProSep-vA High Capacity has a larger pore size and may perform better when purifying fusion proteins or antibody conjugates with molecular weights above 150 kD. - Document Type:
- FAQ
- Product Catalog Number:
- C7842
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Prosep-vA Ultra has a higher binding capacity than ProSep-vA High Capacity - ≥ 56mg/ml vs ≥ 40 mg/ml.
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Crystal structure of the glutamate receptor GluA1 N-terminal domain.
- The AMPA (α-amino-3-hydroxy-5-methylisoxazole-4-propionic acid) subfamily of iGluRs (ionotropic glutamate receptors) is essential for fast excitatory neurotransmission in the central nervous system. The malfunction of AMPARs (AMPA receptors) has been implicated in many neurological diseases, including Alzheimer's disease, Parkinson's disease and amyotrophic lateral sclerosis. The active channels of AMPARs and other iGluR subfamilies are tetramers formed exclusively by assembly of subunits within the same subfamily. It has been proposed that the assembly process is controlled mainly by the extracellular ATD (N-terminal domain) of iGluR. In addition, ATD has also been implicated in synaptogenesis, iGluR trafficking and trans-synaptic signalling, through unknown mechanisms. We report in the present study a 2.5 Å (1 Å=0.1 nm) resolution crystal structure of the ATD of GluA1. Comparative analyses of the structure of GluA1-ATD and other subunits sheds light on our understanding of how ATD drives subfamily-specific assembly of AMPARs. In addition, analysis of the crystal lattice of GluA1-ATD suggests a novel mechanism by which the ATD might participate in inter-tetramer AMPAR clustering, as well as in trans-synaptic protein-protein interactions.
- Document Type:
- Reference
- Product Catalog Number:
- MAB397
- Product Catalog Name:
- Anti-Glutamate Receptor 2 Antibody, extracellular, clone 6C4
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Amino acid mutagenesis of the ligand binding site and the dimer interface of the metabotropic glutamate receptor 1. Identification of crucial residues for setting the act ...
- Previously, we determined the crystal structures of the dimeric ligand binding region of the metabotropic glutamate receptor subtype 1. Each protomer binds l-glutamate within the crevice between the LB1 and LB2 domains. We proposed that the two different conformations of the dimer interface between the two LB1 domains define the activated and resting states of the receptor protein. In this study, the residues in the ligand-binding site and the dimer interface were mutated, and the effects were analyzed in the full-length and truncated soluble receptor forms. The variations in the ligand binding activities of the purified truncated receptors are comparable with those of the full-length form. The mutated full-length receptors were also analyzed by inositol phosphate production and Ca(2+) response. The magnitude of the ligand binding capacities and the amplitude of the intracellular signaling were almost correlated. Alanine substitutions of four residues, Thr(188), Asp(208), Tyr(236), and Asp(318), which interact with the alpha-amino group of glutamate in the crystal, abolished their responses both to glutamate and quisqualate. The mutations of the Tyr(74), Arg(78), and Gly(293) residues, which interact with the gamma-carboxyl group of glutamate, lost their responsiveness to glutamate but not to quisqualate. Furthermore, a mutant receptor containing alanine instead of isoleucine at position 120 located within an alpha helix constituting the dimer interface showed no intracellular response to ligand stimulation. The results demonstrate the crucial role of the dimer interface in receptor activation.
- Document Type:
- Reference
- Product Catalog Number:
- AB1551
- Product Catalog Name:
- Anti-Metabotropic Glutamate Receptor 1α Antibody, pain, CT