Results 301 to 310 of about 6,607,627 (360)
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Expression and Assay of Recombinant ATM

2003
A variety of genetic disorders involve genome instability and abnormal response to DNA damaging agents. Investigation of these disorders has revealed different metabolic pathways responsible for damage repair on one hand, and for signaling the presence of the damage to cellular regulatory systems on the other hand.
Ziv, Y Ziv, Yael   +5 more
openaire   +2 more sources

Recombinant RNA expression

Nature Methods, 2007
A new method for expressing functional RNA molecules in vivo opens a route to easy RNA sample preparation, and establishes a set of tools for studies of RNA structure, interactions and function in vitro and in vivo.
Dunham, Christine M., Conn, Graeme L.
openaire   +1 more source

Expression, purification, and characterization of recombinant apoPholasin

Protein Expression and Purification, 2020
Pholasin is a reactive oxygen-sensitive photoprotein that consists of an apoprotein (apoPholasin) and an unknown chromophore. The preferred human codon-optimized apoPholasin gene was transiently expressed in mammalian cells and apoPholasin was detected using an anti-recombinant apoPholasin antibody.
Satoshi, Inouye   +3 more
openaire   +2 more sources

Recombinant Protein Expression in Nicotiana

2010
Recombinant protein pharmaceuticals are now widely used in treatment of chronic diseases, and several recombinant protein subunit vaccines are approved for human and veterinary use. With growing demand for complex protein pharmaceuticals, such as monoclonal antibodies, manufacturing capacity is becoming limited.
Nobuyuki, Matoba   +2 more
openaire   +2 more sources

The expression of recombinant proteins in yeasts

Current Opinion in Biotechnology, 1996
The methylotrophic yeasts Hansenula polymorpha and Pichia pastoris are rapidly becoming the systems of choice for the expression of recombinant proteins in yeast. However, the powerful genetic techniques available in Saccharomyces cerevisiae and the fission yeast Schizosaccharomyces pombe are still exploited to establish models to study medically ...
openaire   +2 more sources

Expression and isolation of recombinant tau

2017
In this chapter, we describe methods for the purification of both untagged and polyhistidine-tagged tau protein. These protocols utilize a bacterial expression system to produce the tau isoform of interest, followed by heat treatment and column chromatography to separate tau from impurities.
Rebecca L, Best   +6 more
openaire   +2 more sources

Expression of recombinant myeloperoxidase using a baculovirus expression system

Biochemical and Biophysical Research Communications, 1992
Myeloperoxidase (MPO) is a glycosylated heme-containing enzyme present in the azurophilic granules of normal human polymorphonuclear neutrophils. This enzyme plays a major role in the microbicidal activity of the host defense system by catalyzing the formation of the potent oxidant, hypochlorous acid.
K L, Taylor, D J, Uhlinger, J M, Kinkade
openaire   +2 more sources

Expression and bioactivity of recombinant canine erythropoietin

American Journal of Veterinary Research, 1998
Abstract Objective To produce recombinant canine erythropoietin (rcEPO) and compare its biological activity with that of recombinant human EPO (rhEPO). Animals C57BL/6J mice. Procedure The gene encoding cEPO was isolated from a genomic library and subcloned into an eucaryotic expression vector.
J N, MacLeod   +3 more
openaire   +2 more sources

Cloning and expression of recombinant rabbit fertilin

Molecular Reproduction and Development, 1996
Fertilin is a sperm surface protein complex which is reported to play an essential role in sperm-egg fusion in mammals. It is comprised of two related subunits, alpha and beta, both of which are glycosylated and have cytoplasmic and extracellular domains. This protein has been reported to play an essential role in sperm-egg fusion in mammals. We report
C M, Hardy, M K, Holland
openaire   +2 more sources

Expression and processing of recombinant human galactosylceramidase

Clinica Chimica Acta, 1998
Stable transformants of CHO cells that overexpress human galactosylceramidase (GALC) were established. The GALC within the cell consisted of 50- and 30-kDa proteins. The active GALC secreted into the culture medium in large amounts consisted of the 80-kDa precursor enzyme.
S, Nagano   +5 more
openaire   +2 more sources

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