SHP/NR0B2/Nuclear Receptor SHP Antibody Summary
| Immunogen |
Synthetic 16 amino acid peptide from ligand-binding domain of human NR0B2.
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| Specificity |
Human NR0B2. BLAST analysis of the peptide immunogen showed no homology with other human proteins.
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| Predicted Species |
Rat (94%), Bat (94%), Bovine (94%). Backed by our 100% Guarantee.
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| Clonality |
Polyclonal
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| Host |
Rabbit
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| Gene |
NR0B2
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| Purity |
Immunogen affinity purified
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| Innovators Reward |
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Applications/Dilutions
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| Positive Control |
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| Publications |
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Reactivity Notes
Gorilla, Gibbon, Marmoset. Predicted cross-reactivity based on sequence identity: Elephant (88%), Panda (88%), Equine (88%), Porcine (88%), Opossum (88%), Canine (81%).
Packaging, Storage & Formulations
| Storage |
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.
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| Buffer |
PBS
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| Preservative |
0.1% Sodium Azide
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| Concentration |
1.0 mg/ml
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| Purity |
Immunogen affinity purified
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Alternate Names for SHP/NR0B2/Nuclear Receptor SHP Antibody
- FLJ17090
- NR0B2
- nuclear receptor subfamily 0 group B member 2
- nuclear receptor subfamily 0, group B, member 2
- Orphan nuclear receptor SHP
- SHP
- SHPSHP1
- Small heterodimer partner
Background
SHP (short heterodimer partner) is a bile acid-dependent orphan NR0 Knirps-Like receptor with dimerization and ligand-binding domains but not the conventional DNA-binding domain. SHP has been shown to inhibit the transcriptional activity of other nuclear receptors, including thyroid hormone receptor, constitutive androstane receptor, and retinoic acid receptors. SHP affects hepatic cholesterol catabolism based on a two-step mechanism dependent on both coactivator competition and direct transcriptional repression by mediating the repression of CYP7A1, the rate-limiting enzyme for bile acid synthesis. Mutations in the SHP gene contribute to increased body weight, indicating a possible role of SHP in the development of early-onset diabetes (maturity-onset diabetes of the young, MODY). Loss of SHP in mice caused abnormal accumulation and increased synthesis of bile acids due to derepression of rate-limiting CYP7A1 and CYP8B1 hydroxylase enzymes in the biosynthetic pathway. SHP expression has been documented in human liver, adrenal, spleen, and pancreas. ESTs have been isolated from cancerous human kidney, lung, and stomach, as well as normal human heart, kidney, liver, and liver/spleen. Caution: The nuclear receptor SHP should not be confused with the tyrosine phosphatases SHP-1 and SHP-2.