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These data provide a detailed specification of co-occurring C8 proteoforms, including experimental evidence on N-glycosylation, C-mannosylation, and O-glycosylation.
Binding of C8 gamma subunit to C8 beta is dependent on the thrombospondin type 1 module + low-density lipoprotein receptor class A module + membrane attack complex/perforin domain of C8 beta.
C8 alpha and C8 beta have correspondingly similar roles in MAC-mediated lysis of erythrocytes and bacterial killing. C8 gamma is not required for complement-mediated killing of Gram-negative bacteria.
results indicate that the principal binding site for C9 lies within the MACPF domain of C8alpha; they also suggest this site and the binding sites for C8beta and C8gamma are distinct
One can predict that the indel segment of C8alpha assumes a conformation that allows for multiple points of contact with C8gamma.
structure of a C8gamma.laurate complex revealed Y83 and Y131 can move to allow penetration of hydrocarbon chain of laurate into the lower cavity. A Y83W mutation blocked access but had no effect on the ability of C8gamma to enhance C8 cytolytic activity
Results describe the crystal structure of the human C8 alpha MACPF domain disulfide-linked to C8 gamma (alphaMACPF-gamma) at 2.15 A resolution.
C8gamma binds an indel peptide of C8alpha sequence and forms a non-covalent complex.
A review of the human C8 gamma ortholog.
This is a study of the human C8 orthologs. Binding of C8 gamma subunit to C8 beta is dependent on the thrombospondin type 1 module, low-density lipoprotein receptor class A module, and membrane attack complex/perforin domain of C8 beta.
This is a study of the human orthologs of C8 alpha, beta, and gamma. C8 gamma is not required for complement-mediated killing of Gram-negative bacteria.
Results describe the crystal structure of the human ortholog C8 alpha MACPF domain disulfide-linked to C8 gamma (alphaMACPF-gamma) at 2.15 A resolution.
The protein encoded by this gene belongs to the lipocalin family. It is one of the three subunits that constitutes complement component 8 (C8), which is composed of a disulfide-linked C8 alpha-gamma heterodimer and a non-covalently associated C8 beta chain. C8 participates in the formation of the membrane attack complex (MAC) on bacterial cell membranes. While subunits alpha and beta play a role in complement-mediated bacterial killing, the gamma subunit is not required for the bactericidal activity.
complement component C8 gamma chain
, complement component 8, gamma subunit
, novel lipocalin protein
, complement component C8 gamma subunit