MED4 Human

Mediator Complex Subunit 4 Human Recombinant
Cat. No.
BT6023
Source
Escherichia Coli.
Synonyms
Mediator of RNA polymerase II transcription subunit 4, Mediator complex subunit 4, Vitamin D3 receptor-interacting protein complex 36 kDa component, Activator-recruited cofactor 36 kDa component, TRAP/SMCC/PC2 subunit p36 subunit, DRIP36, ARC36, MED4, VDRIP, TRAP36, HSPC126, FLJ10956, RP11-90M2.2.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 80.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

MED4 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 278 amino acids (1-270 a.a.) and having a molecular mass of 30.7kDa. MED4 is fused to 8 amino acids His Tag at C-terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
Mediator complex subunit 4 (MED4) is a crucial component of the Mediator complex, a coactivator that plays a vital role in regulating the transcription of almost all genes dependent on RNA polymerase II. As a part of the vitamin D receptor-interacting protein (DRIP) complex, MED4 contributes to its function as a nuclear receptor coactivator. The DRIP complex exhibits the ability to activate nuclear receptors in a ligand-dependent manner. MED4 acts as a critical link, transmitting information from gene-specific regulatory proteins to the basal RNA polymerase II transcription apparatus. It is recruited to promoters through direct interactions with regulatory proteins, serving as a scaffold for assembling a functional preinitiation complex comprising RNA polymerase II and general transcription factors.
Description
The MED4 protein, produced in E.Coli, is a single, non-glycosylated polypeptide chain consisting of 278 amino acids (with the sequence spanning from amino acid 1 to 270). It has a molecular weight of 30.7kDa. This MED4 protein is engineered with an 8 amino acid His Tag fused at its C-terminus to facilitate purification, which is achieved through proprietary chromatographic techniques.
Physical Appearance
Clear, colorless solution that has been sterilized by filtration.
Formulation
The MED4 protein solution is provided at a concentration of 0.5mg/ml and is formulated in a buffer consisting of 20mM Tris-HCl (pH 8.0), 20% glycerol, 1mM DTT, and 100mM NaCl.
Stability
For short-term storage (up to 2-4 weeks), the MED4 protein solution should be stored at 4°C. For extended storage, it is recommended to freeze the solution at -20°C. To further enhance stability during long-term storage, consider adding a carrier protein (such as HSA or BSA) to a final concentration of 0.1%. Repeated freezing and thawing of the protein solution should be avoided.
Purity
The purity of the MED4 protein is determined to be greater than 80.0% based on SDS-PAGE analysis.
Synonyms
Mediator of RNA polymerase II transcription subunit 4, Mediator complex subunit 4, Vitamin D3 receptor-interacting protein complex 36 kDa component, Activator-recruited cofactor 36 kDa component, TRAP/SMCC/PC2 subunit p36 subunit, DRIP36, ARC36, MED4, VDRIP, TRAP36, HSPC126, FLJ10956, RP11-90M2.2.
Source
Escherichia Coli.
Amino Acid Sequence

MAASSSGEKE KERLGGGLGV AGGNSTRERL LSALEDLEVL SRELIEMLAI SRNQKLLQAG EENQVLELLI HRDGEFQELM KLALNQGKIH HEMQVLEKEV EKRDGDIQQL QKQLKEAEQI LATAVYQAKE KLKSIEKARK GAISSEEIIK YAHRISASNA VCAPLTWVPG DPRRPYPTDL EMRSGLLGQM NNPSTNGVNG HLPGDALAAG RLPDVLAPQY PWQSNDMSMN MLPPNHSSDF LLEPPGHNKE DEDDVEIMST DSSSSSSESD LEHHHHHH.

Product Science Overview

Introduction

The Mediator complex is a large, multi-protein complex that is evolutionarily conserved across eukaryotes. It plays a crucial role in the regulation of transcription by RNA polymerase II. The complex is composed of multiple subunits, each contributing to its overall function. One of these subunits is Mediator Complex Subunit 4 (MED4), which is also known as Human Recombinant MED4 when produced through recombinant DNA technology.

Discovery and Structure

The Mediator complex was initially identified in yeast in the early 1990s by the Kornberg and Young laboratories . The complex was found to stimulate activator-dependent transcription in vitro and was tightly bound to RNA polymerase II. The Mediator complex in humans consists of approximately 30 subunits, which are organized into three main modules: Head, Middle, and Tail, along with a separable four-subunit kinase module .

Function of MED4

MED4 is a component of the Middle module of the Mediator complex. It plays a significant role in bridging the interactions between the other subunits and RNA polymerase II. MED4 is essential for the proper assembly and stability of the Mediator complex, thereby facilitating the transcriptional activation of various genes.

Recombinant Production

Human Recombinant MED4 is produced using recombinant DNA technology, which involves inserting the gene encoding MED4 into an expression vector. This vector is then introduced into a host cell, such as E. coli or yeast, where the protein is expressed and subsequently purified. The recombinant production of MED4 allows for the study of its structure and function in a controlled environment, providing valuable insights into its role within the Mediator complex.

Research and Applications

Research on MED4 and the Mediator complex has advanced significantly over the past two decades. Structural studies using techniques like cryo-electron microscopy (cryo-EM) have revealed detailed insights into the organization and interactions of Mediator subunits . These studies have highlighted the importance of MED4 in maintaining the integrity of the complex and its role in transcriptional regulation.

The recombinant production of MED4 has also facilitated various applications in biomedical research. For instance, it allows for the investigation of MED4’s role in disease mechanisms, the development of potential therapeutic targets, and the exploration of its interactions with other proteins and nucleic acids.

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