Anti-ADRM1 Antibody

The adhesion-regulating molecule 1 (ADRM1) is thought to be involved in protein recruitment and cell adhesion and functions as a proteasomal ubiquitin receptor (1) . ADRM1 promotes the activity of UCH-L5 and plays a role in lymphocyte homing. The carboxy-terminal domain of mammalian ADRM1 serves to bind and enhance the isopeptidase activity of UCHL5/UCH37, perhaps serving as a mechanism to accelerate ubiquitin chain disassembly (2,3) . ADRM1 expression is induced by IFN-gamma in some cancer cell lines and its expression is upregulated in other metastatic cells, suggesting a role in carcinogenesis (4,5) .

ADRM1 antibody was raised against a 19 amino acid peptide near the center of human ADRM1. The immunogen is located within amino acids 210 - 260 of ADRM1.

Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. Within the complex, functions as a proteasomal ubiquitin receptor. Engages and activates 19S-associated deubiquitinases UCHL5 and PSMD14 during protein degradation. UCHL5 reversibly associate with the 19S regulatory particle whereas PSMD14 is an intrinsic subunit of the proteasome lid subcomplex.