Proteasome Subunit Beta Type 7 (PSMB7), also known as 20S proteasome subunit beta-2, is a crucial component of the proteasome complex in humans. This protein is encoded by the PSMB7 gene and plays a significant role in the degradation of intracellular proteins, maintaining cellular homeostasis, and regulating various biological processes .
The proteasome is a multicatalytic proteinase complex with a highly ordered 20S core structure. This barrel-shaped core is composed of four axially stacked rings of 28 non-identical subunits: the two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. PSMB7 is one of these beta subunits and is essential for the proteolytic activity of the proteasome .
PSMB7, along with other beta subunits, assembles into two heptameric rings, forming a proteolytic chamber for substrate degradation. This protein exhibits “trypsin-like” activity, capable of cleaving after basic residues of peptides . The proteasome complex, including PSMB7, is involved in the ATP-dependent degradation of ubiquitinated proteins, which is crucial for protein quality control and the regulation of various cellular processes .
The proteasome complex, including PSMB7, plays a key role in maintaining protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions. It also degrades proteins whose functions are no longer required, thus regulating various biological processes. The 26S proteasome, formed by the association of the 20S core with two 19S regulatory particles, is involved in the ATP-dependent degradation of ubiquitinated proteins .
Recombinant Human Proteasome Subunit Beta Type 7 is a human full-length protein expressed in Escherichia coli. It is used in various applications, including mass spectrometry (MS) and SDS-PAGE, and is biologically active . The recombinant form of PSMB7 is essential for research and therapeutic purposes, providing insights into the protein’s structure, function, and role in various diseases.