pEF6/V5-His A, B, & C Mammalian Expression Vectors - Citations

pEF6/V5-His A, B, & C Mammalian Expression Vectors - Citations

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Citations & References
Abstract
NOD2/CARD15 mediates induction of the antimicrobial peptide human beta-defensin-2.
AuthorsVoss E, Wehkamp J, Wehkamp K, Stange EF, Schröder JM, Harder J,
JournalJ Biol Chem
PubMed ID16319062
Production of inducible antimicrobial peptides offers a first and rapid defense response of epithelial cells against invading microbes. Human Beta-defensin-2 (hBD-2) is an antimicrobial peptide induced in various epithelia upon extracellular as well as intracellular bacterial challenge. Nucleotide-binding oligomerization domain protein 2 (NOD2/CARD15) is a cytosolic protein involved in intracellular ... More
Functional reconstitution of human FcRn in Madin-Darby canine kidney cells requires co-expressed human beta 2-microglobulin.
Authors Claypool Steven M; Dickinson Bonny L; Yoshida Masaru; Lencer Wayne I; Blumberg Richard S;
JournalJ Biol Chem
PubMed ID12023961
The major histocompatibility complex class I-related neonatal Fc receptor, FcRn, assembles as a heterodimer consisting of a heavy chain and beta(2)-microglobulin (beta(2)m), which is essential for FcRn function. We observed that, in Madin-Darby canine kidney (MDCK) cells, the function of human FcRn in mediating the bidirectional transport of IgG was ... More
Structural requirements for the recruitment of Gaa1 into a functional glycosylphosphatidylinositol transamidase complex.
Authors Vainauskas Saulius; Maeda Yusuke; Kurniawan Henry; Kinoshita Taroh; Menon Anant K;
JournalJ Biol Chem
PubMed ID12052837
Glycosylphosphatidylinositol (GPI)-anchored proteins are synthesized on membrane-bound ribosomes, translocated across the endoplasmic reticulum membrane, and GPI-anchored by GPI transamidase (GPIT). GPIT is a minimally heterotetrameric membrane protein complex composed of Gaa1, Gpi8, PIG-S and PIG-T. We describe structure-function analyses of Gaa1, the most hydrophobic of the GPIT subunits, with the ... More
Identification of amino acid residues critical for LD78beta, a variant of human macrophage inflammatory protein-1alpha, binding to CCR5 and inhibition of R5 human immunodeficiency virus type 1 replication.
Authors Miyakawa Toshikazu; Obaru Kenshi; Maeda Kenji; Harada Shigeyoshi; Mitsuya Hiroaki;
JournalJ Biol Chem
PubMed ID11734558
In an attempt to determine which amino acid(s) of LD78beta, a variant of human macrophage inflammatory protein-1alpha, plays a critical role in the interaction with CCR5, we generated six LD78beta variants with an amino acid substituted to Ala at the NH(2) terminus of LD78beta. There was no significant difference in ... More