The antibody detects endogenous level of Androgen Receptor only when phosphorylated at serine 213.
Purification
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography usingepitope-specific phosphopeptide. The antibody against non-phosphopeptide was removedby chromatography using non-phosphopeptide corresponding to the phosphorylation site.
Immunogen
Peptide sequence around phosphorylation site of pSer213 (E-A-S (p) -G-A) derived from Human Androgen Receptor. Antibodies were produced by immunizing rabbits with synthetic phosphopeptide and KLH conjugates.
Western blotting: 1:500-1:1000 Immunofluorescence: 1:100-1:200
Restrictions
For Research Use only
Format
Liquid
Concentration
1 mg/mL
Buffer
Phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150 mM NaCl, 0.02 % sodium azide and 50 % glycerol.
Preservative
Sodium azide
Precaution of Use
This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage
4 °C/-20 °C
Storage Comment
Store at -20 °C for long term preservation (recommended). Store at 4 °C for short term use.
Target
Androgen Receptor (AR)
Alternative Name
Androgen Receptor
Background
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.