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The antibody against MED1 was raised in rabbit using the Synthesized peptide derived from Human TRAP220 around the non-phosphorylation site of T1457. as the immunogen. This antibody exists as a non-conjugated isotype IgG. The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen. This antibody has been validated on WB, IF, ELISA.
The antibody against MED1 was raised in rabbit using the Synthesized peptide derived from Human TRAP220 around the non-phosphorylation site of T1457. as the immunogen. This antibody exists as a non-conjugated isotype IgG. The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen. This antibody has been validated on WB, IF, ELISA.
$167.00
| Cat.No | ADC-37431A | Clonality | Polyclonal |
|---|---|---|---|
| Host Species | Rabbit | Target Name | MED1 |
| Form | Liquid | Species Reactivity | Human, Mouse |
| Isotype | IgG | Storage Buffer | 0.5% BSA and 0.02% sodium azide., Liquid in PBS containing 50% glycerol |
| Purification Method | The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen. | Conjugate | Non-conjugated |
| Application | ELISA, IF, WB | Storage | Upon receipt |
| Immunogen Description | Synthesized peptide derived from Human TRAP220 around the non-phosphorylation site of T1457. | Target Species | Human |
|---|---|---|---|
| Immunogen Sequence | Complete sequences for the immunogen, target protein, and peptides are available upon request. | Uniprot ID | Q15648 |
Uniprot Id
Q15648
Target Species
Human
Target Name
MED1
Target Full Name
Mediator of RNA polymerase II transcription subunit 1
Target Function
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. Acts as a coactivator for GATA1-mediated transcriptional activation during erythroid differentiation of K562 erythroleukemia cells.
Target Subcellular Location
Nucleus. Note=A subset of the protein may enter the nucleolus subsequent to phosphorylation by MAPK1 or MAPK3.
Target Protein Families
Mediator complex subunit 1 family
Target Tissue Specificity
Ubiquitously expressed.
Target Research Area
Epigenetics and Nuclear Signaling
Target Synonyms
Activator-recruited cofactor 205 kDa component; ARC205; CRSP1; CRSP200; DRIP205; DRIP230; MED1; MED1_HUMAN; Mediator complex subunit 1; Mediator of RNA polymerase II transcription subunit 1; p53 regulatory protein RB18A; PBP; Peroxisome proliferator-activated receptor-binding protein; PPAR binding protein ; PPAR-binding protein; PPARBP ; PPARGBP; RB18A; Thyroid hormone receptor-associated protein complex 220 kDa component; Thyroid receptor-interacting protein 2; TR-interacting protein 2; Trap220; TRIP-2; TRIP2; Vitamin D receptor-interacting protein complex component DRIP205
Target Background
The activation of gene transcription is a multistep process that is triggered by factors that recognize transcriptional enhancer sites in DNA. These factors work with co-activators to direct transcriptional initiation by the RNA polymerase II apparatus. The protein encoded by this gene is a subunit of the CRSP (cofactor required for SP1 activation) complex, which, along with TFIID, is required for efficient activation by SP1. This protein is also a component of other multisubunit complexes e.g. thyroid hormone receptor-(TR-) associated proteins which interact with TR and facilitate TR function on DNA templates in conjunction with initiation factors and cofactors. It also regulates p53-dependent apoptosis and it is essential for adipogenesis. This protein is known to have the ability to self-oligomerize.
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