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           Search results for: Recombinant Human TFF3 [from E. coli] Proteins    

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[Expression of human TFF3 in Escherichia coli].

To construct recombinant human TFF3 prokaryotic expressing plasmid, express it in E. coli and identify the expressed protein.

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Recombinant Human Inhibin Human, Trefoil factor 3 ( Recombinant Human TFF3 [f Recombinant Human Inhibin Recombinant Human TFF3 [f Human, Interleukin 6, E.c Recombinant Human Inhibin Human, Allograft Inflamma Recombinant Mn SOD (Human Goat Anti-Human Lactopero Goat Anti-Human NOVA1, (i Inflammation (Human) Anti

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High-level expression of human TFF3 in Escherichia coli.

A strategy for expression and purification of recombinant N-terminal human trefoil factor family-domain peptide 3 (hTFF3) in Escherichia coli was established. The gene of hTFF3 was synthesized to substitute the low-usage condons with corresponding high-usage synonymous condons. At the same time, the signal peptide of DsbC was added to the N-terminus of the hTFF3 gene. The mature recombinant hTFF3 was located in the periplasm of E. coli, which can be released by sonication. The protein was further purified by a two-step cation exchange chromatography mentod. The yield is about 14-15 mg/l of culture. The biological activity of purified hTFF3 was analyzed by cell-based apoptosis assay, which shows that the recombinant hTFF3 is biologically active.

1048 related Products with: High-level expression of human TFF3 in Escherichia coli.

Recombinant Mn SOD (Human Recombinant Human Inhibin ELISA Human , Interleukin Human, Interleukin 6, E.c ElISA Human , Interleukin Recombinant Human TFF3 [f Human, Allograft Inflamma Recombinant Human Inhibin Human high sensitivity in ElISA Human , Interleukin Human, Trefoil factor 3 ( Recombinant Human TFF3 [f

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Bacterial expression and purification of biologically active human TFF3.

A glutathione S-transferase (GST) fusion protein expression system for the production and purification of recombinant human trefoil factor family-domain peptide 3 (hTFF3) was established. The hTFF3 gene, prepared by PCR, was cloned into a pBluescript KS(+) plasmid, and inserted into a pGEX-4T-1 GST fusion vector. The GST-hTFF3 fusion protein was expressed in Escherichia coli, and hTFF3 was purified with Glutathione Sepharose 4B affinity chromatography, yielding about 3-4 mg of pure hTFF3 in one liter of culture broth. The biological activity of purified hTFF3 was tested in two previously reported rat gastric ulcer models. Oral administration of recombinant hTFF3 has a dose dependent protective effect against ethanol-induced or pylorus ligation-induced gastric mucosa injury in rat, which indicates that our recombinant hTFF3 is biologically active.

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CAR,CAR,Constitutive acti Active Human uPA Function Protein Purification Bea Active Human Caspase 925 Noggin Active Human Recom Rabbit Anti-Human Androge Active Human Caspase 325 Active Human Caspases Set pCAMBIA0380 Vector (No Re Recombinant Human TFF3 [f Active Human Caspase 41 u Fibroblast Growth Factor

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Homodimerization and hetero-oligomerization of the single-domain trefoil protein pNR-2/pS2 through cysteine 58.

The single-domain human trefoil proteins [pNR-2/pS2 and human intestinal trefoil factor (hITF)] have seven cysteine residues, of which six are involved in maintaining the structure of the trefoil domain. The seventh does not form part of the trefoil domain and is located three residues from the C-terminus. The ability of the pNR-2/pS2 single trefoil domain protein to dimerize was examined by using recombinant protein with either a cysteine or a serine residue at this position by equilibrium ultracentrifugation, laser-assisted desorption MS, gel filtration and PAGE. pNR-2/pS2 Cys58 formed dimers, whereas pNR-2/pS2 Ser58 did not. Experiments in which the dimer was treated with thiol agents demonstrated that the dimer was linked via a disulphide bond and that the intermolecular disulphide bond was more susceptible to reduction than the intramolecular disulphide bonds. To examine whether dimeric pNR-2/pS2 was secreted by oestrogen-responsive breast cancer cells, which are known to express pNR-2/pS2 mRNA, conditioned medium was separated on non-denaturing polyacrylamide gels, transferred to PVDF membrane and reacted with antiserum against pNR-2/pS2. Monomeric and dimeric pNR-2/pS2 were detected but the majority of the protein reactivity was associated with a larger protein. Treatment of this protein with thiol agents suggested that it is an oligomer containing pNR-2/pS2 linked to another protein by a disulphide bond. These studies suggest that the biological action of pNR-2/pS2 single-domain trefoil protein might involve the formation of homodimers or oligomers with other proteins.

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