|Detection of Human, Mouse, and Rat PSMA2 by Western Blot. Western blot shows lysates of A172 human glioblastoma cell line, NIH‑3T3 mouse embryonic fibroblast cell line, RAW 264.7 mouse monocyte/macrophage cell line, and NRK rat normal kidney cell line. PVDF membrane was probed with 0.2 µg/mL of Sheep Anti-Human/Mouse/Rat PSMA2 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF7639) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). A specific band was detected for PSMA2 at approximately 25 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
PSMA2 (Proteasome subunit alpha type 2; also proteasome component C3 and Macropain subunit C3) is an intracellular 25-27 kDa member of the peptidase T1A family of molecules. It is ubiquitously expressed, and participates in the formation of the 700 kDa 20S proteasomal complex. This complex contains four stacked rings, forming a barrel. The top and bottom rings are made of seven alpha -subunits, while the two central rings are composed of seven catalytic beta -subunits. The complex degrades 80-90% of all intracellular proteins through both a ubiquitin-dependent and -independent process. PSMA2 may modulate the activity of select beta -subunits. Human PSMA2 is 234 amino acids (aa) in length. It contains at least five utilized phosphorylation sites plus one nitrated tyrosine. Full-length human PSMA2 shares 99% aa sequence identity with mouse PSMA2.
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