MED4 Protein (AA 1-270) (His tag)
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- Antigène Voir toutes MED4 Protéines
- MED4 (Mediator Complex Subunit 4 (MED4))
- Type de proteíne
- Recombinant
- Attributs du protein
- AA 1-270
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Origine
- Humain
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Source
- Escherichia coli (E. coli)
- Purification/Conjugué
- Cette MED4 protéine est marqué à la His tag.
- Application
- SDS-PAGE (SDS)
- Attributs du produit
- MED4, 1-270aa, uman, His tag, E.coli
- Pureté
- > 80 % by SDS - PAGE
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- Restrictions
- For Research Use only
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- Format
- Liquid
- Concentration
- 0.5 mg/ml (determined by Bradford assay)
- Buffer
- Liquid. 20mM Tris-HCl buffer (pH8.0) containing 20% glycerol, 1mM DTT, 100mM NaCl
- Stock
- 4 °C
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- Antigène
- MED4 (Mediator Complex Subunit 4 (MED4))
- Autre désignation
- MED4 (MED4 Produits)
- Synonymes
- zgc:110646 Protein, ARC36 Protein, DRIP36 Protein, HSPC126 Protein, TRAP36 Protein, VDRIP Protein, Vdrip Protein, 2410046H15Rik Protein, Vdirp Protein, mediator complex subunit 4 Protein, mediator complex subunit 4 S homeolog Protein, med4 Protein, med4.S Protein, MED4 Protein, Med4 Protein
- Sujet
- Mediator complex subunit 4(MED4) is also known as mediator of RNA polymerase II transcription subunit 4 or vitamin D3 receptor-interacting protein complex 36 kDa component (DRIP36). This protein is a component of the vitamin D receptor-interacting protein (DRIP) complex which functions as a nuclear receptor coactivator. The DRIP complex is capable of activating nuclear receptors in a ligand-dependent manner. Recombinant human MED4, fused to His-tag at C-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. Synonyms: ARC36, DRIP36, VDRIP, Mediator complex subunit 4 Activator-recruited cofactor 36 kDa component, HSPC126, Mediator of RNA polymerase II transcription subunit 4, TRAP/SMCC/PC2 subunit p36 subunit, Vitamin D3 receptor-interacting protein complex 36 kDa component. NCBI no.: AAH05189
- Poids moléculaire
- 30.7kDa (278aa), confirmed by MALDI-TOF
- Pathways
- Intracellular Steroid Hormone Receptor Signaling Pathway, Nuclear Hormone Receptor Binding, Regulation of Lipid Metabolism by PPARalpha
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