SIAH1 is an E3 ligase that regulates protein ubiquitination and proteasome-mediated degradation. Studies have reported that the N-terminal RING domain regulates proteolysis, whereas the C-terminal sequences modulate target protein binding activities. It has also been implicated in p53 response-mediated degradation of β-catenin. Rabbit Anti-SIAH1 (AB1) antibody recognizes bovine, human, mouse, rat, canine, and zebrafish SIAH1.
Immunogen
Synthetic peptide directed towards the N terminal region of human SIAH1
Application
Rabbit Anti-SIAH1 (AB1) antibody can be used for western blot applications at 1.25 μg/ml.
Biochem/physiol Actions
SIAH1 is a protein that is a member of the seven in absentia homolog (SIAH) family. The protein is an E3 ligase and is involved in ubiquitination and proteasome-mediated degradation of specific proteins. The activity of this ubiquitin ligase has been implicated in the development of certain forms of Parkinson′s disease, the regulation of the cellular response to hypoxia and induction of apoptosis. Alternative splicing results in several additional transcript variants, some encoding different isoforms and others that have not been fully characterized.
Sequence
Synthetic peptide located within the following region: FTCLPAARTRKRKEMSRQTATALPTGTSKCPPSQRVPALTGTTASNNDLA
Physical form
Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Molecular and cellular biology, 19(1), 724-732 (1998-12-22)
The Drosophila seven in absentia (sina) gene was initially discovered because its inactivation leads to R7 photoreceptor defects. Recent data indicate that Sina binds to the Sevenless pathway protein Phyllopod, and together they mediate degradation of Tramtrack, a transcriptional repressor
Destruction of beta-catenin is regulated through phosphorylation-dependent interactions with the F box protein beta-TrCP. A novel pathway for beta-catenin degradation was discovered involving mammalian homologs of Drosophila Sina (Siah), which bind ubiquitin-conjugating enzymes, and Ebi, an F box protein that
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