ERP29 Protein, Human (GST)

Contrary to expectations, the ERP29 protein does not exhibit disulfide isomerase activity. Its function is critical in the processing of secreted proteins within the endoplasmic reticulum (ER) and may contribute to the folding of proteins in this cellular compartment. ERP29 Protein, Human (GST) is the recombinant human-derived ERP29 protein, expressed by E. coli , with N-GST labeled tag.

ERP29 protein, as per available information, does not appear to function as a disulfide isomerase, distinguishing it from certain enzymes involved in disulfide bond rearrangement. Instead, ERP29 plays a pivotal role in the processing of secretory proteins within the endoplasmic reticulum (ER), suggesting its involvement in the folding of proteins in this cellular compartment. It exists as a homodimer and is an integral part of a substantial chaperone multiprotein complex. This complex includes proteins like CABP1, DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PPIB, SDF2L1, and UGGT1. Notably, ERP29 is present in very small amounts within this complex, and it is intriguingly absent or present at very low levels of CALR and CANX. The detailed involvement of ERP29 in these protein interactions highlights its significance in the ER-related protein processing pathway.

Human

E. coli

N-GST

P30040-1 (P40-F251)

10961  [NCBI]

PLDTVTFYKVIPKSKFVLVKFDTQYPYGEKQDEFKRLAENSASSDDLLVAEVGISDYGDKLNMELSEKYKLDKESYPVFYLFRDGDFENPVPYTGAVKVGAIQRWLKGQGVYLGMPGCLPVYDALAGEFIRASGVEARQALLKQGQDNLSSVKETQKKWAEQYLKIMGKILDQGEDFPASEMTRIARLIEKNKMSDGKKEELQKSLNILTAF

Approximately 51.0 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.