Results 41 to 50 of about 15,564 (249)

Extended plasma half-life of albumin-binding domain fused human IgA upon pH-dependent albumin engagement of human FcRn in vitro and in vivo

open access: yesmAbs, 2021
Albumin has a serum half-life of 3 weeks in humans. This feature can be used to improve the pharmacokinetics of shorter-lived biologics. For instance, an albumin-binding domain (ABD) can be used to recruit albumin.
Simone Mester   +7 more
doaj   +1 more source

Dissection of the Neonatal Fc Receptor (FcRn)-Albumin Interface Using Mutagenesis and Anti-FcRn Albumin-blocking Antibodies [PDF]

open access: yesJournal of Biological Chemistry, 2014
Albumin is the most abundant protein in blood and plays a pivotal role as a multitransporter of a wide range of molecules such as fatty acids, metabolites, hormones, and toxins. In addition, it binds a variety of drugs. Its role as distributor is supported by its extraordinary serum half-life of 3 weeks.
Sand, Kine Marita Knudsen   +10 more
openaire   +4 more sources

Tissues Expression, Polymorphisms Identification of FcRn Gene and Its Relationship with Serum Classical Swine Fever Virus Antibody Level in Pigs [PDF]

open access: yesAsian-Australasian Journal of Animal Sciences, 2012
Neonatal Fc receptor (FcRn) gene encodes a receptor that binds the Fc region of monomeric immunoglobulin G (IgG) and is responsible for IgG transport and stabilization.
Liu Yang   +8 more
doaj   +1 more source

Abundant intracellular IgG in enterocytes and endoderm lacking FcRn.

open access: yesPLoS ONE, 2013
FcRn, a non-classical MHCI molecule, transports IgG from mother to young and regulates the rate of IgG degradation throughout life. Brambell proposed a mechanism that unified these two functions, saying that IgG was pinocytosed nonspecifically by the ...
Sudhasri Mohanty   +5 more
doaj   +1 more source

Forced Degradation Testing as Complementary Tool for Biosimilarity Assessment [PDF]

open access: yes, 2019
Oxidation of monoclonal antibodies (mAbs) can impact their efficacy and may therefore represent critical quality attributes (CQA) that require evaluation.
Dyck, Yan Felix Karl   +6 more
core   +1 more source

FcRn expression in cancer: Mechanistic basis and therapeutic opportunities

open access: yesJournal of Controlled Release, 2021
There is an urgent need to identify new cellular targets to expand the repertoire, potency and safety of cancer therapeutics. Neonatal Fc Receptor (FcRn)-driven cellular recycling plays a predominant role in the prolonged serum half-life of human serum albumin (HSA) and immunoglobulin G (IgG) exploited in long-acting cancer drug designs.
Rudnik-Jansen, Imke, Howard, Ken
openaire   +3 more sources

Hydrophobic Ligand Binding by Zn-α_2-glycoprotein, a Soluble Fat-depleting Factor Related to Major Histocompatibility Complex Proteins [PDF]

open access: yes, 2001
Zn-alpha2-glycoprotein (ZAG) is a member of the major histocompatibility complex (MHC) class I family of proteins and is identical in amino acid sequence to a tumor-derived lipid-mobilizing factor associated with cachexia in cancer patients.
Bjorkman, Pamela J.   +4 more
core   +1 more source

Effects of receptor dimerization on the interaction between the class I major histocompatibility complex-related Fc receptor and IgG [PDF]

open access: yes, 1995
The neonatal Fc receptor (FcRn) transports maternal IgG from ingested milk in the gut to the bloodstream of newborn mammals. An FcRn dimer was observed in crystals of the receptor alone and of an FcRn-Fc complex, but its biological relevance was unknown.
Bjorkman, Pamela J.   +2 more
core   +1 more source

Fully human monoclonal antibody inhibitors of the neonatal Fc receptor (FcRn) reduce circulating IgG in nonhuman primates

open access: yesFrontiers in Immunology, 2015
The therapeutic management of antibody mediated autoimmune disease typically involves immunosuppressant and immunomodulatory strategies. However, perturbing the fundamental role of the neonatal Fc receptor (FcRn) in salvaging IgG from lysosomal ...
Andrew E Nixon   +12 more
doaj   +1 more source

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