Steroid/thyroid hormone mechanism

Product Name: AHR antibody [RPT1]
Applications: ELISA, ICC/IF, IHC, IHC-F, IHC-P, IP, WB, ChIP assay
Predicted Target Size:
Positive Controls:
Form Supplied: Liquid
Concentration:
Purification:
Full Name: aryl hydrocarbon receptor
Background: The aryl hydrocarbon receptor (AhR), also known as the dioxin receptor, is a ligand-activated helix/loop/helix transcription factor found in a variety of vertebrate species. The known ligands for AhR are foreign planar aromatic compounds, such as polycyclic aromatic compounds and halogenated aromatic compounds such as 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD). Unlike the steroid/thyroid hormone receptors, there is no known physiological ligand for the Ah Receptor. ? Studies indicate that in non-ligand activated cells, AhR is found complexed with HSP90 predominantly in the cytoplasm. Upon binding to an agonist, the ligand-activated AhR is believed to transform to a nuclear, DNA binding form. This transformation process appears to involve dissociation of HSP90 from AhR followed by formation of a heterodimer with AhR nuclear translocator protein (Arnt). The AhR-ligand complex appears to initiate gene transcription of cytochrome P450 1A1.
Synonyms: Ahre, 11622, Ah, Ahr, Aryl hydrocarbon receptor, Ahh, In
Cellular Localization:
CAS NO: 53868-26-1
Product: NSC305787 (hydrochloride)
Host: Mouse
Clonality: Monoclonal
Isotype: IgG1
Immunogen: Synthetic peptide corresponding to residues R(12) K R R K P(17) V(22) K P I P A E G I K(31) of human AhR.
Antigen Species: Human
Species Reactivity: Human, Mouse, Pig, Rat, Primate
Conjugation: Unconjugated
Storage Buffer: Ascites containing % sodium azide.
Storage Instruction: Keep as concentrated solution. Aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.
Notes: For In vitro laboratory use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
Specificity:

To date relatively little information has been available on the structure of the N-terminal regions of the NHRs. Even though the full-length structure of the peroxisome proliferator-activated receptor- γ (PPAR- γ ) has been solved it failed to show any signature of structure formation in its very short NTD [ 26 ]. We and others have shown that the glucocorticoid receptor’s N-terminal transactivation AF1 region and a shorter core fragment of AF1, the AF1 core, are unstructured in aqueous solution [ 62 – 66 ]. In other words, the NTD amino acid sequences possess an intrinsically disordered (ID) conformation, a feature of activation domains of many transcription factors [ 27 , 62 , 65 , 67 , 68 ]. Similar results have been reported for the ER α and ER β , androgen-, and progesterone receptor [ 69 – 71 ]. Thus, activation domains of many signaling proteins including the ER’s NTD/AF1 are known to exist in an ID state. One of the reasons for their existence as an ID region seems to be to help them in promoting molecular recognition by providing surfaces capable of binding specific target molecules [ 72 – 75 ].

Because steroids are lipophilic, they diffuse easily through the cell membranes, and therefore have a very large distribution volume. In their target tissues, steroids are concentrated by an uptake mechanism which relies on their binding to intracellular proteins (or " receptors ", see below). High concentration of steroids are also found in adipose tissue, although this is not a target for hormone action. In the human male, adipose tissue contains aromatase activity, and seems to be the main source of androgen-derived estrogens found in the circulation. But most of the peripheral metabolism occurs in the liver and to some extent in the kidneys, which are the major sites of hormone inactivation and elimination, or catabolism (see below).

Steroid/thyroid hormone mechanism

steroid/thyroid hormone mechanism

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