protein

EBP1 Protein, Human (His)

HY-P75726

5 μg;10 μg;50 μg;100 μg

35;55;150;240 USD

EBP1 Protein, Human (His)

proteins

E. coli

5 μg;10 μg;50 μg;100 μg

35;55;150;240 USD

EBP1 protein participates in the signal transduction pathway regulated by ERBB3 and is related to growth regulation. As an androgen receptor (AR) corepressor, it is regulated by the ERBB3 ligand neregulin-1/heregulin (HRG). EBP1 Protein, Human (His) is the recombinant human-derived EBP1 protein, expressed by E. coli , with N-His labeled tag.

Human

The EBP1 protein is implicated in playing a role in an ERBB3-regulated signal transduction pathway and is associated with growth regulation. It acts as a corepressor of the androgen receptor (AR) and is modulated by the ERBB3 ligand neuregulin-1/heregulin (HRG). Furthermore, EBP1 inhibits transcription of some E2F1-regulated promoters, potentially by recruiting histone acetylase (HAT) activity. It exhibits RNA-binding capabilities and associates with various mature and precursor rRNAs, suggesting involvement in the regulation of intermediate and late steps of rRNA processing and ribosome assembly. Additionally, EBP1 mediates cap-independent translation of specific viral internal ribosomal entry sites (IRESs). Functionally, it plays a role in regulating cell proliferation, differentiation, and survival, with isoform-specific effects on apoptosis suppression (isoform 1) and cell differentiation promotion (isoform 2). The protein interacts with various partners, including the cytoplasmic domain of ERBB3, and exhibits dynamic associations with AR, NCL/nucleolin, HDAC2, RB1, AKT1, RNF20, HUWE1, and DNAJC21, highlighting its versatility in engaging with diverse cellular components and participating in intricate molecular processes.

Proliferation-associated protein 2G4; hG4-1; ErbB3-binding protein 1; PA2G4

Greater than 90% as determined by reducing SDS-PAGE

Lyophilized from a 0.2 μm filtered solution of 50 mM Tris-HCL, 300 mM NaCl, pH 8.0.

Room temperature in continental US; may vary elsewhere.