Background:

E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates E3 ubiquitin ligase activity either through direct binding to substrates or by functioning as the essential RING domain subunit of larger E3 complexes. Triggers the ubiquitin-mediated degradation of many substrates, including proteins involved in transcription regulation(POU2AF1, PML, NCOR1), a cell surface receptor(DCC), an antiapoptotic protein(BAG1), and a protein involved in synaptic vesicle function in neurons(SYP). Mediates ubiquitination and proteasomal degradation of DYRK2 in response to hypoxia. It is thereby involved in apoptosis, tumor suppression, cell cycle, transcription and signaling processes. Has some overlapping function with SIAH1. Triggers the ubiquitin-mediated degradation of TRAF2, whereas SIAH1 does not. Promotes monoubiquitination of SNCA.

Clonality:

polyclonal

Classification:

Primary antibody

Alternative names:

N/A

Specificity:

Human, Mouse, Rat

Host:

Rabbit

Isotype:

IgG

Immunogen:

seven in absentia homolog 2(Drosophila)

Purification:

Immunogen affinity purified

Purity:

≥95% as determined by SDS-PAGE

Calculated molecular weight:

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Form:

liquid

Applications:

ELISA, WB

Recommended dilution:

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Storage:

PBS with 0.02% sodium azide and 50% glycerol pH 7.3,-20℃ for 12 months(Avoid repeated freeze / thaw cycles.)

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