UBE2W Antibody / Ubiquitin-conjugating enzyme E2 W

UBE2W antibody detects Ubiquitin-conjugating enzyme E2 W, a cytoplasmic and nuclear enzyme encoded by the UBE2W gene on chromosome 8q24.3. UBE2W is a member of the E2 ubiquitin-conjugating enzyme family that plays a central role in the ubiquitination pathway, transferring ubiquitin from E1 activating enzymes to target substrates via E3 ligases. It is expressed in most tissues, with particularly high expression in testis, brain, and muscle, where it contributes to protein homeostasis and stress response regulation. UBE2W is unique among E2 enzymes in its ability to monoubiquitinate the N-terminal amino group of substrates rather than internal lysine residues, providing a specialized mechanism for protein modification.

UBE2W functions within the ubiquitin-proteasome system (UPS), a critical pathway for protein degradation, signal transduction, and DNA repair. It interacts with multiple E3 ligases, including BRCA1-BARD1, RNF4, and CHIP, and is involved in the ubiquitination of substrates associated with DNA damage repair, stress responses, and proteostasis. This enzyme participates in pathways that maintain genomic stability and cellular adaptation to oxidative and proteotoxic stress.

Structurally, UBE2W contains a conserved catalytic core domain typical of E2 enzymes, with a cysteine residue in its active site that forms a transient thioester bond with ubiquitin. The enzyme�s N-terminal helix contributes to substrate specificity and interaction with distinct E3 ligases. UBE2W�s ability to initiate ubiquitin chain formation on protein N-termini distinguishes it from other E2 enzymes and positions it as a key regulator of ubiquitin signaling complexity.

In DNA damage response, UBE2W assists in monoubiquitination of repair factors, facilitating recruitment of downstream effectors involved in homologous recombination and chromatin remodeling. It also plays a role in protein quality control by tagging misfolded or damaged proteins for degradation. Dysregulation of UBE2W activity has been implicated in carcinogenesis, neurodegeneration, and defective DNA repair syndromes. Altered UBE2W expression is observed in several cancer types, where its activity may influence genomic integrity and tumor cell survival.

At the pathway level, UBE2W functions in ubiquitin-mediated proteolysis, DNA damage repair signaling, and protein turnover. It interacts with the BRCA1 complex and SUMO-targeted ubiquitin ligases, integrating ubiquitin and SUMO pathways that regulate chromatin and transcriptional processes. As part of the ubiquitin-proteasome system, UBE2W contributes to proteostasis and stress-induced adaptation in both nuclear and cytoplasmic compartments.

Immunohistochemical staining using UBE2W antibody shows both cytoplasmic and nuclear localization, reflecting its dual roles in protein degradation and DNA repair. The UBE2W antibody from