PDI1 ER and Nuclear Envelope Marker Antibody (38H8): sc-57963

PDI1 ER and Nuclear Envelope Marker Antibody (38H8) is a mouse monoclonal IgG1 antibody that detects the PDI1 ER and Nuclear Envelope Marker protein of S. cerevisiae origin by western blotting (WB), immunoprecipitation (IP), and immunofluorescence (IF). PDI1 ER and Nuclear Envelope Marker (38H8) antibody is available as the non-conjugated anti-PDI1 ER and Nuclear Envelope Marker antibody. The protein disulfide isomerase (PDI1) plays a crucial role in the formation and rearrangement of disulfide bonds in secretory proteins, which is essential for maintaining protein quality control during their translocation into the endoplasmic reticulum (ER). This process is vital because improperly folded proteins can lead to cellular stress and disease; thus, PDI1 ensures that only correctly folded proteins are transported to their final destinations. Additionally, PDI1 is an integral component of the yeast ER′s disulfide bond formation pathway, contributing both oxidase and isomerase activities. When proteins are misfolded, PDI1 facilitates their targeting to the export channel in the ER membrane, thereby preventing the accumulation of dysfunctional proteins. The nuclear envelope, which surrounds the nucleus in yeast cells, not only protects genetic material but also plays a significant role in the organization of chromatin within the nucleus. The unique proteins associated with the nuclear envelope can be instrumental in studying the dynamics of nuclear processes in yeast, making anti-PDI1 ER and Nuclear Envelope Marker antibody (38H8) a valuable tool for researchers investigating these cellular mechanisms.

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PDI1 ER and Nuclear Envelope Marker Antibody (38H8) References:

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