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Rabbit anti-Human MED1 Polyclonal Antibody

The antibody against MED1 was raised in rabbit using the Synthesized peptide derived from the Internal region of Human TRAP220. 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, IHC, ELISA.

ADC-37432A

The antibody against MED1 was raised in rabbit using the Synthesized peptide derived from the Internal region of Human TRAP220. 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, IHC, ELISA.

$167.00

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Specifications


Cat.No ADC-37432A ClonalityPolyclonal
Host SpeciesRabbitTarget NameMED1
FormLiquidSpecies ReactivityHuman, Mouse
IsotypeIgGStorage Buffer0.5% BSA and 0.02% sodium azide., Liquid in PBS containing 50% glycerol
Purification MethodThe antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.ConjugateNon-conjugated
ApplicationELISA, IHC, WBStorageUpon receipt

Immunogen Information


Immunogen DescriptionSynthesized peptide derived from the Internal region of Human TRAP220.Target SpeciesHuman
Immunogen SequenceComplete sequences for the immunogen, target protein, and peptides are available upon request.Uniprot IDQ15648
Background Information
  • 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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