Recombinant Proteins

USD 585.00

2 Weeks

GroEL gene was amplified by PCR from E.coli and cloned into an expression vector. This protein was overexpressed in E.coli and was purified by using conventional chromatography techniques.

Tag Tag Free
Expression Host E.Coli

USD 270.00

2 Weeks

GroEL gene was amplified by PCR from E.coli and cloned into an expression vector. This protein was overexpressed in E.coli and was purified by using conventional chromatography techniques.

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Expression Host E.Coli

USD 340.00

2 Weeks

Recombinant E.coli SurA protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography.

Tag His-tag
Expression Host E.Coli

Recombinant E.coli ppiA protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.

Tag His-tag
Expression Host E.Coli

Recombinant E.coli ppiA protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.

Tag His-tag
Expression Host E.Coli

USD 585.00

2 Weeks

DnaK (amino acids 1-384) is N-terminal ATPase domain and ATP bound to the ATPase domain induces a conformational change in the substrate binding domain (residues 385-638). The protein coding region of the ATPase domain of DNAK (amino acids 1-384) was amplified by PCR and cloned into an E. coli expression vector. The ATPase domain of DNAK was overexpressed in E. coli and the recombinant protein was purified to apparent homogeneity by using conventional column chromatography techniques.

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Expression Host E.Coli

USD 270.00

2 Weeks

Recombinant DsbA (residues 20-208) was expressed in E. coli and purified by using conventional chromatography techniques.

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Expression Host E.Coli

The protein coding region of the substrate binding domain of DNAK (amino acids 385-546) was amplified by PCR and cloned into an E. coli expression vector. The substrate binding domain of DNAK was overexpressed in E. coli and the recombinant protein was purified to apparent homogeneity by using conventional column chromatography techniques. Additional amino acid (Met) is attached at N- terminus.

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Expression Host E.Coli

USD 585.00

2 Weeks

DnaJ(amino acids 1-376) was overexpressed in E. coli and purified to apparent homogeneity by using conventional column chromatography techniques.

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Expression Host E.Coli

USD 585.00

2 Weeks

Recombinant DsbA (residues 20-208) was expressed in E. coli and purified by using conventional chromatography techniques.

Tag Tag Free
Expression Host E.Coli

USD 585.00

2 Weeks

The protein coding region of the substrate binding domain of DNAK (amino acids 385-638) was amplified by PCR and cloned into an E. coli expression vector. The substrate binding domain of DNAK was overexpressed in E. coli and the recombinant protein was purified to apparent homogeneity by using conventional column chromatography techniques. Additional amino acid (Met) is attached at N-terminus.

Tag Tag Free
Expression Host E.Coli