Skip to main content

MED13 Recombinant Protein Antigen

Novus Biologicals, part of Bio-Techne | Catalog # NBP2-57545PEP

Novus Biologicals, part of Bio-Techne
Catalog #
Availability
Size / Price
Qty
Loading...
NBP2-57545PEP

Key Product Details

Source

E. coli

Tag

N-terminal His6ABP (ABP = Albumin Binding Protein derived from Streptococcal Protein G)

Conjugate

Unconjugated

Applications

Antibody Competition

Product Specifications

Description

A recombinant protein antigen with a N-terminal His6-ABP tag corresponding to human MED13.

Source: E. coli

Amino Acid Sequence: SASVQVASATYTTENLDLAFNPNNDGADGMGIFDLLDTGDDLDPDIINILPASPTGSPVHSPGSHYPHGGDAGKGQSTDRLLSTEPH

Fusion Tag: N-terminal His6ABP (ABP = Albumin Binding Protein derived from Streptococcal Protein G)

This product is intended to be used as a blocking antigen for antibody competition assays. Any other use of this antigen is done at the risk of the user. The use of this product for commercial production is strictly prohibited. Please contact technical support if you have any questions.

Purity

>80% by SDS-PAGE and Coomassie blue staining

Predicted Molecular Mass

27 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.

Applications

Antibody Competition (10 - 100 molar excess)

Application Notes

This recombinant antigen is only intended to be used as a blocking agent to confirm antibody specificity with the corresponding antibody, catalog number NBP2-57545.

It is purified by IMAC chromatography, and the expected concentration is greater than 0.5 mg/ml.

For current lot information, including availability, please contact our technical support team click nb-technical@bio-techne.com

For further blocking tide related information and a protocol, click here.

Protein / Peptide Type

Recombinant Protein Antigen

Formulation, Preparation and Storage

NBP2-57545PEP
Formulation PBS and 1M Urea, pH 7.4.
Preservative No Preservative
Concentration Please see the vial label for concentration. If unlisted please contact technical services.
Shipping The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Store at -20C. Avoid freeze-thaw cycles.

Background: MED13

MED13 encodes a component of the mediator complex (also known as TRAP, SMCC, DRIP, or ARC), a transcriptional coactivator complex thought to be required for the expression of almost all genes. The mediator complex is recruited by transcriptional activators or nuclear receptors to induce gene expression, possibly by interacting with RNA polymerase II and promoting the formation of a transcriptional pre-initiation complex. The product of this gene is proposed to form a sub-complex with MED12, cyclin C, and CDK8 that can negatively regulate transactivation by mediator.

Alternate Names

Activator-recruited cofactor 250 kDa component, KIAA0593HSPC221, mediator complex subunit 13ARC250, mediator of RNA polymerase II transcription, subunit 13 homolog, THRAP1mediator of RNA polymerase II transcription subunit 13, thyroid hormone receptor associated protein 1, Thyroid hormone receptor-associated protein 1, Thyroid hormone receptor-associated protein complex 240 kDa component, thyroid hormone receptor-associated protein complex component TRAP240, thyroid hormone receptor-associated protein, 240 kDa subunit, Trap240, TRAP240DRIP250, Vitamin D3 receptor-interacting protein complex component DRIP250

Gene Symbol

MED13

Additional MED13 Products

Product Documents for MED13 Recombinant Protein Antigen

Certificate of Analysis

To download a Certificate of Analysis, please enter a lot number in the search box below.

Product Specific Notices for MED13 Recombinant Protein Antigen

This product is for research use only and is not approved for use in humans or in clinical diagnosis. This product is guaranteed for 1 year from date of receipt.

Loading...
Loading...
Loading...