Enhanced Stability of Detergent-Free Human Native STEAP1 Protein from Neoplastic Prostate Cancer Cells upon an Innovative Isolation Procedure.

ABSTRACT:

Background

The STEAP1 is a cell-surface antigen over-expressed in prostate cancer, which contributes to tumor progression and aggressiveness. However, the molecular mechanisms underlying STEAP1 and its structural determinants remain elusive.

Methods

The fraction capacity of Butyl- and Octyl-Sepharose matrices on LNCaP lysates was evaluated by manipulating the ionic strength of binding and elution phases, followed by a Co-Immunoprecipitation (Co-IP) polishing. Several potential stabilizing additives were assessed, and the melting temperature (Tm) values ranked the best/worst compounds. The secondary structure of STEAP1 was identified by circular dichroism.

Results

The STEAP1 was not fully captured with 1.375 M (Butyl), in contrast with interfering heterologous p

SUBMITTER: Barroca-Ferreira J 

PROVIDER: S-EPMC8472055 | biostudies-literature | 2021 Sep

REPOSITORIES: biostudies-literature