Product Pathways - Neuroscience
Phospho-BMAL1 (Ser42) Antibody #13936
|13936S||100 µl ( 10 western blots )||￥3,900.00 现货查询||购买询价|
|13936||carrier free & custom formulation / quantity||email request|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IP=Immunoprecipitation,
Specificity / Sensitivity
Phospho-BMAL1 (Ser42) Antibody recognizes endogenous levels of BMAL1 protein only when phosphorylated at Ser42. The antibody recognizes additional proteins of approximately 40 kDa and 100 kDa in some cells.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser42 of mouse BMAL1 protein. Antibodies are purified by protein A and peptide affinity chromatography.
Western blot analysis of extracts from mouse brain and rat eye using Phospho-BMAL1 (Ser42) Antibody. The phospho-specificity of Phospho-BMAL1 (Ser42) Antibody was verified by peptide blocking using a phosphopeptide or non-phosphopeptide targeting residue Ser42.
Western blot analysis of extracts from mouse brain, untreated (-) or λ phosphatase-treated (+), using Phospho-BMAL1 (Ser42) Antibody (upper) and α-Actinin (D6F6) XP® Rabbit mAb #6487 (lower).
Western blot analysis of extracts from 293T cells, mock transfected (-) or transfected with a construct expressing DDK-tagged full length wild-type mouse BMAL1 protein (wt mBMAL1-DDK, +) or DDK-tagged full length mouse BMAL1 Ser42A site specific mutant (S42A mBMAL1-DDK; +), using Phospho-BMAL1 (Ser42) Antibody (upper) and DYKDDDDK Tag (9A3) Mouse mAb #8146 (lower). Wild-type and S42A site specific mutant BMAL1 constructs were kindly provided by Dr. Jonathan Lipton (Boston Children's Hospital).
Circadian rhythms govern many key physiological processes that fluctuate with a period of approximately 24 hours. These processes include the sleep-wake cycle, glucose, lipid and drug metabolism, heart rate, hormone secretion, renal blood flow, and body temperature, as well as basic cellular processes such as DNA repair and the timing of the cell division cycle (1,2). The mammalian circadian system consists of many individual tissue-specific clocks (peripheral clocks) that are controlled by a master circadian pacemaker residing in the suprachiasmatic nuclei (SCN) of the brain (1,2). The periodic circadian rhythm is prominently manifested by the light-dark cycle, which is sensed by the visual system and processed by the SCN. The SCN processes the light-dark information and synchronizes peripheral clocks through neural and humoral output signals (1,2).
The cellular circadian clockwork consists of interwoven positive and negative regulatory loops, or limbs (1,2). The positive limb includes the CLOCK and BMAL1 proteins, two basic helix-loop-helix-PAS containing transcription factors that bind E box enhancer elements and activate transcription of their target genes. CLOCK is a histone acetyltransferase (HAT) protein, which acetylates both histone H3 and H4 (3). BMAL1 binds to CLOCK and enhances its HAT activity (3). The CLOCK/BMAL1 dimer exhibits a periodic oscillation in both nuclear/cytoplasmic localization and protein levels, both of which are regulated by phosphorylation (4,5). CLOCK/BMAL1 target genes include the Cry and Per genes, whose proteins form the negative limb of the circadian clockwork system (1,2). CRY and PER proteins (CRY1, CRY2, PER1, PER2 and PER3) form oligomers that also periodically shuttle between the nucleus and cytoplasm. When in the nucleus, CRY/PER proteins inhibit CLOCK/BMAL1-mediated transcriptional activation, thus completing the circadian transcriptional loop (1,2). In tissues, roughly six to eight percent of all genes exhibit a circadian expression pattern (1,2). This 24-hour periodicity in gene expression results from coordination of the positive and negative regulatory limbs of the cellular clockwork system, and is fine-tuned by outside signals received from the SCN.
- Albrecht, U. and Eichele, G. (2003) Curr Opin Genet Dev 13, 271-7.
- Virshup, D.M. et al. (2007) Cold Spring Harb Symp Quant Biol 72, 413-20.
- Doi, M. et al. (2006) Cell 125, 497-508.
- Kondratov, R.V. et al. (2003) Genes Dev 17, 1921-32.
- Kwon, I. et al. (2006) Mol Cell Biol 26, 7318-30.
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