|Other Names||Androgen receptor, Dihydrotestosterone receptor, Nuclear receptor subfamily 3 group C member 4, AR, DHTR, NR3C4|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP2509a is HPHARIKLENPLD, containing a predicted sumoylation site from the central region of human ANDR. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Steroid hormone receptors are ligand-activated transcription factors that regulate eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Transcription factor activity is modulated by bound coactivator and corepressor proteins. Transcription activation is down-regulated by NR0B2. Activated, but not phosphorylated, by HIPK3 and ZIPK/DAPK3.|
|Cellular Location||Nucleus. Cytoplasm. Note=Predominantly cytoplasmic in unligated form but translocates to the nucleus upon ligand-binding. Can also translocate to the nucleus in unligated form in the presence of GNB2L1|
|Tissue Location||Isoform 2 is mainly expressed in heart and skeletal muscle.|
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Provided below are standard protocols that you may find useful for product applications.
Androgen receptor (ANDR) has 3 major functional domains: the N-terminal domain, DNA-binding domain, and an androgen-binding domain. The protein functions as a steroid-hormone activated transcription factor. Upon binding the hormone ligand, the receptor dissociates from accessory proteins, translocates into the nucleus, dimerizes, and then stimulates transcription of androgen responsive genes. The gene for this protein contains 2 polymorphic trinucleotide repeat segments that encode polyglutamine and polyglycine tracts in the N-terminal transactivation domain of the protein. Expansion of the polyglutamine tract causes spinal bulbar muscular atrophy (Kennedy disease). Mutations are also associated with complete androgen insensitivity (CAIS). PIAS1 and PIASxalpha function as SUMO-E3 ligases toward androgen receptor; sumoylation of ANDR represses androgen receptor dependent transcription.
Nishida, et al. J. Biol. Chem. 277 (44), 41311-41317 (2002)Sills, E.S., et al., Int. J. Mol. Med. 9(1):45-48 (2002).Chavez, B., et al., J. Hum. Genet. 46(10):560-565 (2001).Ahmed, S.F., et al., J. Clin. Endocrinol. Metab. 85(2):658-665 (2000).Marcelli, M., et al., Cancer Res. 60(4):944-949 (2000).
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