Rabbit anti-Human SHP/NR0B2 Polyclonal Antibody

Uniprot Id

Q15466

Target Species

Human

Target Name

NR0B2

Target Full Name

Nuclear receptor subfamily 0 group B member 2

Target Function

Transcriptional regulator that acts as a negative regulator of receptor-dependent signaling pathways. Specifically inhibits transactivation of the nuclear receptor with which it interacts. Inhibits transcriptional activity of NEUROD1 on E-box-containing promoter by interfering with the coactivation function of the p300/CBP-mediated transcription complex for NEUROD1. Essential component of the liver circadian clock which via its interaction with NR1D1 and RORG regulates NPAS2-mediated hepatic lipid metabolism. Regulates the circadian expression of cytochrome P450 (CYP) enzymes. Represses: NR5A2 and HNF4A to down-regulate CYP2C38, NFLI3 to up-regulate CYP2A5, BHLHE41/HNF1A axis to up-regulate CYP1A2, CYP2E1 and CYP3A11, and NR1D1 to up-regulate CYP2B10, CYP4A10 and CYP4A14.

Target Involvement

Obesity (OBESITY)

Target Subcellular Location

Nucleus. Cytoplasm. Note=Colocalizes with NEUROD1 in the nucleus.

Target Protein Families

Nuclear hormone receptor family, NR0 subfamily

Target Tissue Specificity

Liver. Low levels of expression were detected in heart and pancreas.

Target Synonyms

NR0B2; NR0B2_HUMAN; Nr0b2a; Nuclear receptor subfamily 0 group B member 2; Nuclear receptor subfamily 0; group B; member 2a; Orphan nuclear receptor SHP; SHP; SHP-1; Shp1; Small heterodimer partner

Target Background

The protein encoded by this gene is an unusual orphan receptor that contains a putative ligand-binding domain but lacks a conventional DNA-binding domain. The gene product is a member of the nuclear hormone receptor family, a group of transcription factors regulated by small hydrophobic hormones, a subset of which do not have known ligands and are referred to as orphan nuclear receptors. The protein has been shown to interact with retinoid and thyroid hormone receptors, inhibiting their ligand-dependent transcriptional activation. In addition, interaction with estrogen receptors has been demonstrated, leading to inhibition of function. Studies suggest that the protein represses nuclear hormone receptor-mediated transactivation via two separate steps: competition with coactivators and the direct effects of its transcriptional repressor function.