Erratum to: Prokaryotic expression, purification and functional characterization of recombinant human RIP2
نویسندگان
چکیده
منابع مشابه
Cloning, Expression, Purification and CD Analysis of Recombinant Human Betatrophin
Betatrophin is a member of the angiopoietin-like (ANGPTL) family that has been implicated in both triglyceride and glucose metabolism. The physiological functions and molecular targets of this protein remain largely unknown; hence, a purified available protein would aid study of the exact role of betatrophin in lipid or glucose metabolism. In this study, we cloned the full-length cDNA of betatr...
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Background: Over the past century, the areas of genomics, proteomics and lipids have captured the attention of investigators worldwide. Carbohydrates, have recently received increased attention through the expanding field of glycobiology; probably because they are very complex and not encoded in the genome. Objectives: The purpose of this study was to express and purify recombinant human galec...
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Background: Rabies virus (RABV) is a deadly neurotropic virus that causes the disease of rabies in humans and animals. L protein is one of the large structural protein of rabies virus, which displays multiple enzymatic activities, and is required for viral transcription and replication. Objectives: A truncated L protein of Rabies virus is being cloned, expressed and purified to produce relevant...
متن کاملProkaryotic expression, purification and characterization of human cyclooxygenase-2
Cyclooxygenase-2 (COX-2) is a key enzyme which catalyzes the conversion of arachidonic acid (AA) into prostaglandins (PGs). It plays an important role in pathophysiological processes, such as tumorigenesis, angiogenesis, inflammation and tumor cell drug resistance. Therefore, COX-2 has been viewed as an important target for cancer therapy. The preparation of COX-2 protein is an important initia...
متن کاملExpression, purification, and characterization of recombinant human glutamine synthetase.
A bacterial expression system has been engineered for human glutamine synthetase (EC 6.3.1.2) that produces approximately 60 mg of enzyme (20% of the bacterial soluble protein) and yields approx. 8 mg of purified enzyme per litre of culture. The recombinant enzyme was purified 5-fold to apparent homogeneity and characterized. It has a subunit molecular mass of approx. 45000 Da. The Vmax value o...
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ژورنال
عنوان ژورنال: Molecular Biology Reports
سال: 2012
ISSN: 0301-4851,1573-4978
DOI: 10.1007/s11033-012-2335-z