RYBP Protein (His tag)
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- Antigène Voir toutes RYBP Protéines
- RYBP (RING1 and YY1 Binding Protein (RYBP))
- Type de proteíne
- Recombinant
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Origine
- Humain
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Source
- Escherichia coli (E. coli)
- Purification/Conjugué
- Cette RYBP protéine est marqué à la His tag.
- Application
- SDS-PAGE (SDS)
- Purification
- purified by chromatography
- Pureté
- > 85 % by SDS - PAGE
- Top Product
- Discover our top product RYBP Protéine
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- Commentaires
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Synonyms: RING1 and YY1 binding protein, AAP1, DEDAF, YEAF1
- Restrictions
- For Research Use only
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- Format
- Liquid
- Concentration
- 0.5 mg/ml (determined by Bradford assay)
- Buffer
- 20 mM Tris-HCl buffer, pH 8.0, 20% glycerol, 1 MM DTT, 100 mM NaCl
- Stock
- 4 °C
- Stockage commentaire
- Avoid repeated freezing and thawing cycles.
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- Antigène
- RYBP (RING1 and YY1 Binding Protein (RYBP))
- Autre désignation
- RYBP (RYBP Produits)
- Synonymes
- AAP1 Protein, DEDAF Protein, YEAF1 Protein, 2410018J24Rik Protein, rybp Protein, aap1 Protein, dedaf Protein, yeaf1 Protein, cb337 Protein, wu:fi34f03 Protein, Dedaf Protein, zgc:153842 Protein, RING1 and YY1 binding protein Protein, RING1 and YY1 binding protein L homeolog Protein, RING1 and YY1 binding protein a Protein, RING1 and YY1 binding protein b Protein, RYBP Protein, Rybp Protein, rybp Protein, rybp.L Protein, rybpa Protein, rybpb Protein
- Sujet
- RYBP (RING1- and YY1-binding protein) is a member of the polycomb group (PcG). This protein interacts with MDM2 and decreases MDM2-mediated p53 ubiquitination, leading to stabilization of p53 and an increase in p53 activity. RYBP induces cell-cycle arrest and is involved in the p53 response to DNA damage. RYBP has been shown to interact with RING1, YY1, Caspase 10, E2F3, E2F2, Mdm2, Abl gene and CBX2. Recombinant human RYBP protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.
- Poids moléculaire
- 27.4kDa (252aa) confirmed by MALDI-TOF (Molecular size on SDS-PAGE will appear higher)
- NCBI Accession
- NP_036366
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