|Calculated MW||110 KDa|
|Other Names||Androgen receptor, Dihydrotestosterone receptor, Nuclear receptor subfamily 3 group C member 4, AR, DHTR, NR3C4|
|Target/Specificity||Synthetic phospho-peptide corresponding to amino acid residues surrounding Ser94 conjugated to KLH.|
|Format||Prepared from rabbit serum by affinity purification via sequential chromatography on phospho- and dephosphopeptide affinity columns.|
|Antibody Specificity||Specific for the ~110k AR protein phosphorylated at Ser94. Immunolabeling is blocked by preadsorption of antibody with the phospho-peptide that was used to generate the antibody but not by the corresponding dephospho-peptide.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Phospho Ser94 Androgen Receptor (AR) Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
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Provided below are standard protocols that you may find useful for product applications.
The androgen receptor (AR) is a DNA-binding transcription factor that regulates genes critical for the development and maintenance of the male sexual phenotype. Defects in androgen receptor have been shown to play a role in prostate cancer, and inhibition of AR activity through modulation of signal transduction pathways may delay prostate cancer progression (Heinlein and Chang 2004). Multiple phosphorylation sites have been identified on the androgen receptor that affect cross-talk between growth factor signaling and androgen in prostate development and cancer (Gioeli et al., 2002). One of these sites, at Ser94, appears constitutively phosphorylated and exhibits no response to treatments with stimulating hormone (Gioeli et al., 2002). The site at Ser94 is unique among the AR phosphorylation sites in that it does not achieve a maximal level of phosphorylation between translation and the initial round of nuclear import, having a strong bias for androgen-independent phosphorylation in the cytoplasm (Kesler et al., 2007).
Heinlein C, Chang C. (2004) Androgen Receptor in Prostate Cancer. Endocrine Reviews. 25(2):276-308
Gioeli D, Ficarro S, Kwiek J, Aaronson D, Hancock M, Catling A, White F, Christian R, Settlage R, Shabanowitz J, Hunt D, Weber M. (2002) Androgen Receptor Phosphorylation, Regulation and Indentification of the Phosphorylation Sites. J Biol Chem. 277(32):29304-29314
Kesler C, Gioeli D, Conaway M, Weber M, Paschal B. (2007) Subcellular Localization Modulates Activation Function 1 Domain Phosphorylation in the Androgen Receptor. Molecular Endocrinology. 21(9):2071-2084
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