MED20 Human
Description
MED20 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 235 amino acids (1-212 a.a.) and having a molecular mass of 25.6kDa.
MED20 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
The Mediator complex is a large, multi-protein assembly that plays a crucial role in the regulation of gene transcription in eukaryotic cells. It serves as a bridge connecting transcription factors bound to DNA and RNA polymerase II, facilitating the transcription of genetic information from DNA to mRNA. The Mediator complex is composed of multiple subunits, each contributing to its overall function and structural integrity. One such subunit is Mediator Complex Subunit 20 (MED20).
The Mediator complex in humans is approximately 1.4 MDa in size and includes 26 subunits . These subunits are organized into three main modules: the Head, Middle, and Tail, along with a separable four-subunit kinase module . MED20 is one of the essential components of this complex, contributing to its structural and functional dynamics.
MED20, like other subunits of the Mediator complex, plays a pivotal role in the regulation of transcription by RNA polymerase II. The Mediator complex is involved in various stages of transcription, including the initiation, elongation, and termination phases . It interacts with transcription factors and other regulatory proteins to modulate the transcriptional activity of RNA polymerase II, ensuring precise and efficient gene expression.
Recombinant MED20 refers to the MED20 protein that has been produced through recombinant DNA technology. This involves cloning the MED20 gene into an expression vector, introducing the vector into a host cell (such as bacteria or yeast), and then inducing the host cell to produce the MED20 protein. Recombinant MED20 is used in various research applications to study its structure, function, and interactions within the Mediator complex.
The study of recombinant MED20 has provided valuable insights into the structural organization and functional mechanisms of the Mediator complex. Advances in cryo-electron microscopy (cryo-EM) have allowed researchers to visualize the Mediator complex at high resolution, revealing intricate details of subunit interactions and conformational changes . These studies have enhanced our understanding of how MED20 and other subunits contribute to the regulation of gene transcription.
