- Tel: 858.663.9055
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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
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The Zebrafish Psmc2 antibody targets Psmc2, also known as 26S proteasome regulatory subunit 7, a AAA+ ATPase of the 19S regulatory particle essential for ATP-dependent protein unfolding, substrate translocation, and ubiquitin-mediated proteolysis in Danio rerio. Zebrafish, also known as Danio rerio, express psmc2 strongly throughout early embryogenesis, with high enrichment in proliferative and metabolically active tissues such as the developing brain, somites, notochord, heart, and endodermal organs. Psmc2 localizes to the cytoplasm and nucleus as part of the hexameric ATPase ring of the 19S base, where it provides mechanical force for substrate processing prior to entry into the 20S catalytic chamber.
Psmc2 belongs to the AAA-ATPase family and corresponds to the Rpt1 subunit in yeast nomenclature. It contains conserved Walker A and Walker B motifs that mediate ATP binding and hydrolysis, enabling the conformational changes required for unfolding and translocating ubiquitinated substrates. In zebrafish embryos, psmc2 expression correlates with stages of rapid tissue remodeling and protein turnover. A Zebrafish Psmc2 antibody is suitable for detecting cytoplasmic and nuclear localization consistent with regions of high proteasomal activity where cellular differentiation, metabolic shifts, and signaling turnover are tightly regulated.
Functionally, Psmc2 is required for assembly and performance of the 26S proteasome. Through ATP-driven remodeling, Psmc2 cooperates with other AAA-ATPases to remove ubiquitin chains, unfold regulatory proteins, and feed substrates into the proteolytic core. In zebrafish, Psmc2-dependent degradation influences major developmental pathways including Wnt, Notch, Hedgehog, Fgf, and NF-kB signaling. These pathways govern germ layer patterning, neural differentiation, muscle formation, cardiac development, and metabolic homeostasis. Loss or disruption of psmc2 impairs proteasome assembly, causes accumulation of ubiquitinated proteins, induces proteotoxic stress, and results in widespread developmental abnormalities due to failed turnover of key regulatory factors.
Structurally, zebrafish Psmc2 forms part of the six-member AAA-ATPase ring that caps the 20S proteasome and creates a gated channel for substrate translocation. Its ATP-dependent mechanical activity coordinates with ubiquitin receptors, deubiquitinating enzymes, and the alpha-ring of the 20S core. The zebrafish psmc2 gene maps to chromosome 9 and is regulated by proliferative cues, metabolic signaling, and proteostasis-related transcription factors. Co-localization studies detect Psmc2 in perinuclear proteasome-rich clusters and within nuclei of transcriptionally active cells, often overlapping with ubiquitin accumulation zones, other Rpt ATPases, and catalytic beta-subunit markers.
A Zebrafish Psmc2 antibody is suitable for detecting Psmc2 in studies focused on ubiquitin-mediated protein degradation, proteasome assembly, ATP-driven substrate processing, developmental proteostasis, and signaling pathway regulation in Danio rerio. Its distribution across nuclear and cytoplasmic compartments provides a detailed readout of tissues undergoing high proteolytic demand, enabling researchers to assess proteasome dysfunction, analyze proteotoxic stress responses, and explore how controlled degradation of transcription factors and signaling intermediates shapes embryonic patterning and organ formation. This antibody is supplied for research use by NSJ Bioreagents.
Optimal dilution of the Zebrafish Psmc2 antibody should be determined by the researcher.
E. coli-derived zebrafish Psmc2 recombinant protein (amino acids K34-N433) was used as the immunogen for the Zebrafish Psmc2 antibody.
After reconstitution, the Zebrafish Psmc2 antibody can be stored for up to one month at 4oC. For long-term, aliquot and store at -20oC. Avoid repeated freezing and thawing.
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