Recombinant Proteins

USD 600.00

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.

Expression Host E. coli

USD 250.00

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.

Expression Host E. coli

USD 320.00

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

USD 600.00

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.

Expression Host E. coli

USD 250.00

2 Weeks

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

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.

Expression Host E. coli

USD 600.00

2 Weeks

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

Expression Host E. coli

USD 600.00

2 Weeks

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

Expression Host E. coli

USD 600.00

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.

Expression Host E. coli

USD 600.00

2 Weeks

DnaK (amino acids 1-638) was amplified by PCR and cloned into an E. coli expression vector. DnaK 1-638 was overexpressed in E. coli and was purified to apparent homogeneity by using conventional column chromatography techniques.

Expression Host E. coli

USD 250.00

2 Weeks

Dnak (residues 508-638) of the substrate binding domain is a-helical and appears to act as a lid covering the substrate binding cleft. DnaK (amino acid 508-638) was overexpressed in E. coli and purified to apparent homogeneity by using conventional column chromatography techniques. Additional amino acid (Met) is attached at N-terminus.

Expression Host E. coli

USD 250.00

2 Weeks

DnaK (amino acids 1-638) was amplified by PCR and cloned into an E. coli expression vector. DnaK 1-638 was overexpressed in E. coli and was purified to apparent homogeneity by using conventional column chromatography techniques.

Expression Host E. coli

USD 250.00

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.

Expression Host E. coli