Recombinant mTFPI160 (mature amino acids 1–160) was expressed and isolated using the pMAL system (New England Biolabs) and used to raise rabbit anti-mTFPI160 polyclonal IgG that was purified by protein A affinity (Captiva-PriMAB, Repligen) chromatography. Control, pre-immune rabbit IgG was isolated in the same manner.
Pmal system
Manufactured by New England Biolabs
The PMAL system is a versatile laboratory instrument designed for protein expression and purification. It utilizes a maltose-binding protein (MBP) fusion system to facilitate efficient isolation and purification of recombinant proteins. The core function of the PMAL system is to enable researchers to express and purify target proteins from bacterial or eukaryotic host cells.
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Lab products found in correlation
2 protocols using pmal system
1
Recombinant mTFPI160 Antibody Production
2
TAC102 Recombinant Protein Expression and Antibody Generation
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The recombinant version of TAC102 was expressed in E. coli BL21 strain as a fusion with the maltose-binding protein (MBP) at the N-terminus of TAC102, using the pMAL system (New England Biolabs). The fusion protein was purified on amylose resin and analyzed by mass-spectrometry. The purified product was used to generate polyclonal antibodies in rats (Eurogentec, Belgium). The monoclonal antibody was produced in mice (GenScript, USA) against a synthetic peptide that represented the 500−660 aa of TAC102. Specificity of both antibodies was confirmed by western blotting and immunofluorescence microscopy, in PCF and BSF cells (S2 Fig ).
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