ELISA/assay

Fish Androgen Receptor ELISA Kit

MBS043521

96 Strip Wells

600 USD

ELISA Kit

Fish Androgen Receptor ELISA Kit

Androgen Receptor

androgen receptor; Androgen receptor; androgen receptor; dihydrotestosterone receptor; androgen nuclear receptor variant 2; nuclear receptor subfamily 3 group C member 4; androgen receptor; Dihydrotestosterone receptor; Nuclear receptor subfamily 3 group C member 4

AR

AR; AR; KD; AIS; TFM; DHTR; SBMA; HYSP1; NR3C4; SMAX1; HUMARA; DHTR; NR3C4

ANDR_HUMAN

Fish

Store all reagents at 2-8 degree C

ELISA Type: Sandwich

178882

AAA51772.1

P10275

98,989 Da

Alpha6-Beta4 Integrin Signaling Pathway 198807!!Androgen Receptor Signaling Pathway 198806!!Coregulation Of Androgen Receptor Activity Pathway 138085!!FOXA1 Transcription Factor Network Pathway 137979!!Gene Expression Pathway 105937!!Generic Transcription Pathway 105938!!IL-6 Signaling Pathway 198864!!Integrated Breast Cancer Pathway 219801!!Integrated Pancreatic Cancer Pathway 711360!!Nongenotropic Androgen Signaling Pathway 138048

The androgen receptor gene is more than 90 kb long and codes for a protein that has 3 major functional domains: the N-terminal domain, DNA-binding domain, and 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. This gene contains 2 polymorphic trinucleotide repeat segments that encode polyglutamine and polyglycine tracts in the N-terminal transactivation domain of its protein. Expansion of the polyglutamine tract causes spinal bulbar muscular atrophy (Kennedy disease). Mutations in this gene are also associated with complete androgen insensitivity (CAIS). Two alternatively spliced variants encoding distinct isoforms have been described. [provided by RefSeq, Jul 2008]

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. Ref.34 Ref.48 Ref.50 Ref.51 Ref.60 Ref.65 Ref.67. Enzyme regulation: AIM-100 (4-amino-5,6-biaryl-furo[2,3-d]pyrimidine) suppresses TNK2-mediated phosphorylation at Tyr-267. Inhibits the binding of the Tyr-267 phosphorylated form to androgen-responsive enhancers (AREs) and its transcriptional activity. Ref.53. Subunit structure: Binds DNA as a homodimer. Part of a ternary complex containing AR, EFCAB6/DJBP and PARK7. Interacts with HIPK3 and NR0B2 in the presence of androgen. The ligand binding domain interacts with KAT7/HBO1 in the presence of dihydrotestosterone. Interacts with EFCAB6/DJBP, PELP1, PQBP1, RANBP9, RBAK, SPDEF, SRA1, TGFB1I1, ZNF318 and RREB1. Interacts with ZMIZ1/ZIMP10 and ZMIZ2/ZMIP7 which both enhance its transactivation activity. Interacts with SLC30A9 and RAD54L2/ARIP4 . By similarity. Interacts via the ligand-binding domain with LXXLL and FXXLF motifs from NCOA1, NCOA2, NCOA3, NCOA4 and MAGEA11. The AR N-terminal poly-Gln region binds Ran resulting in enhancement of AR-mediated transactivation. Ran-binding decreases as the poly-Gln length increases. Interacts with HIP1 (via coiled coil domain). Interacts (via ligand-binding domain) with TRIM68. Interacts with TNK2. Interacts with USP26. Interacts with RNF6. Interacts (regulated by RNF6 probably through polyubiquitination) with RNF14; regulates AR transcriptional activity. Interacts with PRMT2 and TRIM24. Interacts with GNB2L1/RACK1. Interacts with RANBP10; this interaction enhances dihydrotestosterone-induced AR transcriptional activity. Interacts with PRPF6 in a hormone-independent way; this interaction enhances dihydrotestosterone-induced AR transcriptional activity. Interacts with STK4/MST1. Interacts with ZIPK/DAPK3. Interacts with LPXN. Interacts with MAK. Part of a complex containing AR, MAK and NCOA3. Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.37 Ref.38 Ref.41 Ref.42 Ref.43 Ref.44 Ref.45 Ref.46 Ref.47 Ref.48 Ref.49 Ref.50 Ref.51 Ref.52 Ref.54 Ref.59 Ref.60 Ref.65 Ref.67. Subcellular 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. Ref.7 Ref.33 Ref.42 Ref.50. Tissue specificity: Isoform 2 is mainly expressed in heart and skeletal muscle. Ref.7. Domain: Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain. In the presence of bound steroid the ligand-binding domain interacts with the N-terminal modulating domain, and thereby activates AR transcription factor activity. Agonist binding is required for dimerization and binding to target DNA. The transcription factor activity of the complex formed by ligand-activated AR and DNA is modulated by interactions with coactivator and corepressor proteins. Interaction with RANBP9 is mediated by both the N-terminal domain and the DNA-binding domain. Interaction with EFCAB6/DJBP is mediated by the DNA-binding domain. Ref.59 Ref.65. Post-translational modification: Sumoylated on Lys-386 (major) and Lys-520. Ubiquitinated. Deubiquitinated by USP26. 'Lys-6' and 'Lys-27'-linked polyubiquitination by RNF6 modulates AR transcriptional activity and specificity. Ref.50 Ref.52Phosphorylated in prostate cancer cells in response to several growth factors including EGF. Phosphorylation is induced by c-Src kinase (CSK). Tyr-534 is one of the major phosphorylation sites and an increase in phosphorylation and Src kinase activity is associated with prostate cancer progression. Phosphorylation by TNK2 enhances the DNA-binding and transcriptional activity and may be responsible for androgen-independent progression of prostate cancer. Phosphorylation at Ser-81 by CDK9 regulates AR promoter selectivity and cell growth. Phosphorylation by PAK6 leads to AR-mediated transcription inhibition. Ref.36 Ref.39 Ref.45 Ref.51 Ref.53 Ref.54Palmitoylated by ZDHHC7 and ZDHHC21. Palmitoylation is required for plasma membrane targeting and for rapid intracellular signaling via ERK and AKT kinases and cAMP generation. Ref.56. Polymorphism: The poly-Gln region of AR is highly polymorphic and the number of Gln varies in the population (from 17 to 26). A smaller size of the poly-Gln region may be associated with the development of prostate cancer.The poly-Gly region of AR is polymorphic and ranges from 24 to 31 Gly. A poly-Gly region shorter or equal to 23 may be associated with the development of androgenetic alopecia. Involvement in disease: Androgen insensitivity syndrome (AIS) [MIM:300068]: An X-linked recessive form of pseudohermaphroditism due end-organ resistance to androgen. Affected males have female external genitalia, female breast development, blind vagina, absent uterus and female adnexa, and abdominal or inguinal testes, despite a normal 46,XY karyotype.Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.4 Ref.16 Ref.18 Ref.61 Ref.76 Ref.78 Ref.81 Ref.83 Ref.84 Ref.85 Ref.86 Ref.87 Ref.88 Ref.90 Ref.91 Ref.95 Ref.96 Ref.98 Ref.100 Ref.102 Ref.104 Ref.106 Ref.115 Ref.116 Ref.117 Ref.119 Ref.120 Ref.121 Ref.122 Ref.123 Ref.124 Ref.126 Ref.127 Ref.129 Ref.130 Ref.131 Ref.137 Ref.139 Ref.140 Ref.143 Ref.144 Ref.146 Ref.147 Ref.148 Ref.149 Ref.152 Ref.155 Ref.156 Ref.157 Ref.160 Ref.162 Ref.163 Ref.164 Ref.165 Ref.166 Ref.167 Ref.168 Ref.169 Ref.170 Ref.172 Ref.175 Ref.176 Ref.181 Ref.182 Ref.183 Ref.184 Ref.188 Ref.191 Ref.192 Ref.195 Ref.196 Ref.198 Ref.201Spinal and bulbar muscular atrophy X-linked 1 (SMAX1) [MIM:313200]: An X-linked recessive form of spinal muscular atrophy. Spinal muscular atrophy refers to a group of neuromuscular disorders characterized by degeneration of the anterior horn cells of the spinal cord, leading to symmetrical muscle weakness and atrophy. SMAX1 occurs only in men. Age at onset is usually in the third to fifth decade of life, but earlier involvement has been reported. It is characterized by slowly progressive limb and bulbar muscle weakness with fasciculations, muscle atrophy, and gynecomastia. The disorder is clinically similar to classic forms of autosomal spinal muscular atrophy.Note: The disease is caused by mutations affecting the gene represented in this entry. Caused by trinucleotide CAG repeat expansion. In SMAX1 patients the number of Gln ranges from 38 to 62. Longer expansions result in earlier onset and more severe clinical manifestations of the disease. Ref.200Defects in AR may play a role in metastatic prostate cancer. The mutated receptor stimulates prostate growth and metastases development despite of androgen ablation. This treatment can reduce primary and metastatic lesions probably by inducing apoptosis of tumor cells when they express the wild-type receptor.Androgen insensitivity, partial (PAIS) [MIM:312300]: A disorder that is characterized by hypospadias, hypogonadism, gynecomastia, genital ambiguity, normal XY karyotype, and a pedigree pattern consistent with X-linked recessive inheritance. Some patients present azoospermia or severe oligospermia without other clinical manifestations.Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.79 Ref.82 Ref.85 Ref.88 Ref.90 Ref.92 Ref.97 Ref.99 Ref.100 Ref.101 Ref.104 Ref.110 Ref.111 Ref.112 Ref.113 Ref.114 Ref.116 Ref.118 Ref.121 Ref.123 Ref.127 Ref.131 Ref.135 Ref.137 Ref.139 Ref.141 Ref.142 Ref.145 Ref.149 Ref.154 Ref.161 Ref.164 Ref.169 Ref.173 Ref.174 Ref.177 Ref.178 Ref.180 Ref.182 Ref.184 Ref.187 Ref.195 Ref.196. Miscellaneous: In the absence of ligand, steroid hormone receptors are thought to be weakly associated with nuclear components; hormone binding greatly increases receptor affinity. The hormone-receptor complex appears to recognize discrete DNA sequences upstream of transcriptional start sites.Transcriptional activity is enhanced by binding to RANBP9.The level of tyrosine phosphorylation may serve as a diagnostic tool to predict patient outcome in response to hormone-ablation therapy. Inhibition of tyrosine phosphorylation may be an effective intervention target for hormone-refractory prostate cancer. Sequence similarities: Belongs to the nuclear hormone receptor family. NR3 subfamily.Contains 1 nuclear receptor DNA-binding domain.

96 Strip Wells

600 USD