NOTCH2 Protein, Human (Biotinylated, HEK293, His-Avi)

NOTCH2 protein is a receptor for ligands such as JAG1, JAG2 and DLL1 and is critical for cell fate determination. Ligand activation promotes cleavage and releases NICD, which forms a transcription activator complex with RBPJ/RBPSUH, affecting cell differentiation, proliferation and apoptosis. NOTCH2 Protein, Human (Biotinylated, HEK293, His-Avi) is the recombinant human-derived NOTCH2 protein, expressed by HEK293 , with C-Avi, C-His labeled tag. The total length of NOTCH2 Protein, Human (Biotinylated, HEK293, His-Avi) is 505 a.a., with molecular weight of 70-80 kDa.

NOTCH2 protein functions as a receptor for membrane-bound ligands, including Jagged-1 (JAG1), Jagged-2 (JAG2), and Delta-1 (DLL1), playing a pivotal role in regulating cell-fate determination. Upon ligand activation, NOTCH2 undergoes cleavage, releasing the Notch intracellular domain (NICD), which forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes within the enhancer of split locus. This activation influences cellular differentiation, proliferation, and apoptotic programs. NOTCH2 is implicated in bone remodeling and homeostasis, collaborating with RELA/p65 to enhance NFATc1 promoter activity and positively regulate RANKL-induced osteoclast differentiation. Additionally, it positively regulates self-renewal in liver cancer cells. NOTCH2 exists as a heterodimer composed of a C-terminal fragment (N(TM)) and an N-terminal fragment (N(EC)), likely linked by disulfide bonds. It interacts with various proteins, including transcriptional coactivators MAML1, MAML2, and MAML3, as well as factors such as HIF1AN, TCIM, and FBXW7, implicating its involvement in diverse cellular processes and regulatory pathways. Interactions with MINAR1, NOTCH2NL, MDK, and MINAR2 further contribute to the intricate network of NOTCH2 signaling.

Human

HEK293

C-Avi;C-His

Q04721 (L26-Q530)

4853  [NCBI]

70-80 kDa

Greater than 95% as determined by Tris-Bis PAGE.

<1 EU/μg, determined by LAL method.