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Experimental Spinal Fusion With Recombinant Human Bone Morphogenetic Protein-2

Spine, 1995
Lumbar intertransverse process arthrodesis using recombinant human bone morphogenetic protein-2 was performed in a previously established rabbit model for posterolateral spinal fusion and compared with fusions achieved using autogenous bone graft.To qualitatively compare different recombinant human bone morphogenetic protein-2 dosages and carriers and ...
J H, Schimandle, S D, Boden, W C, Hutton
openaire   +2 more sources

Recombinant rubella E1 fusion proteins for antibody screening and diagnosis

Clinical and Diagnostic Virology, 1994
Until rubella is eradicated there will be a continuing need for rubella antibody surveillance. Antigen production using recombinant DNA technology may be a viable alternative to traditional techniques of producing antigens for enzyme immunoassays (EIAs).To investigate the potential of bacterial fusion proteins containing rubella E1 protein sequences ...
J, Newcombe   +5 more
openaire   +2 more sources

The Use of Recombinant Fusion Proteases in the Affinity Purification of Recombinant Proteins

Molecular Biotechnology, 1999
In the affinity purification of recombinant fusion proteins, the rate-limiting step is usually the efficient proteolytic cleavage and removal of the affinity tail and the protease from the purified recombinant protein. We have developed a rapid, convenient, and efficient method of affinity purification that can overcome this limitation.
openaire   +3 more sources

Production of Recombinant Oxytocin Through Sulfitolysis of Inteincontaining Fusion Protein

Protein & Peptide Letters, 2012
An artificial gene consisting of seven copies of an oxytocinoyl-lysine encoding sequence arranged in a tandem was synthesized and inserted downstream of the SspDnaB intein gene in a pTWIN1 plasmid. The corresponding fusion protein Dnab-7oxy contained 16 cysteine residues and formed inclusion bodies when expressed in E. coli.
Roman S, Esipov   +3 more
openaire   +2 more sources

Fusion tails for the recovery and purification of recombinant proteins

Protein Expression and Purification, 1991
Several fusion tail systems have been developed to promote efficient recovery and purification of recombinant proteins from crude cell extracts or culture media. In these systems, a target protein is genetically engineered to contain a C- or N-terminal polypeptide tail, which provides the biochemical basis for specificity in recovery and purification ...
C F, Ford, I, Suominen, C E, Glatz
openaire   +2 more sources

Tag Removal by Site-Specific Cleavage of Recombinant Fusion Proteins

2010
Where an affinity tag has served its purpose it may become desirable to remove it from the protein of interest. This chapter describes the removal of such fusion partners from the intended protein product by cleavage with site-specific endoproteases. Methods to achieve proteolytic cleavage of the fusion proteins are provided, along with techniques for ...
Adam, Charlton, Michael, Zachariou
openaire   +2 more sources

Expression, Purification, and Immobilization of Recombinant Tamavidin 2 Fusion Proteins

2014
Tamavidin 2 is a fungal avidin-like protein that binds biotin with high affinity. Unlike avidin or streptavidin, tamavidin 2 in soluble form is produced at high levels in Escherichia coli. In this chapter, we describe a method for immobilization and purification of recombinant proteins with the use of tamavidin 2 as an affinity tag.
Yoshimitsu, Takakura   +2 more
openaire   +2 more sources

Recombinant TLR-MD-2 fusion proteins

2006
The present invention provides recombinant TLR-MD-2 fusion proteins capable of binding to lipopolysaccharide (LPS) containing a TLR-moiety comprising the extracellular domain of a Toll-like receptor (TLR) or a functional derivative thereof, fused with a MD-2-moiety comprising MD-2 or a functional derivative thereof.
openaire   +1 more source

Integrative oncology: Addressing the global challenges of cancer prevention and treatment

Ca-A Cancer Journal for Clinicians, 2022
Jun J Mao,, Msce   +2 more
exaly  

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