Thermo Fisher Scientific Human Progesterone Receptor, Ligand Binding Domain, GST Tag Recombinant Protein

Applications

Tested Dilution

Publications

Kinase Assay (KA)

Assay-dependent

-

Product Specifications

Species

Human

Expression System

Baculovirus

Amino acid sequence

675-933

Tag

GST-tag

Class

Recombinant

Type

Protein

Conjugate

Unconjugated Unconjugated Unconjugated

Form

Liquid

Concentration

See Label

Purification

purified

Storage buffer

proprietary buffer

Contains

no preservative

Storage conditions

-80° C, Avoid Freeze/Thaw Cycles

Shipping conditions

Dry ice

Product Specific Information

Progesterone receptor ligand binding domain (PR-LBD) is a 59.83 kDa recombinant human protein (amino acids 675-933) expressed as a glutathione-S-transferase (GST) fusion protein in baculovirus-infected insect cells. PR is expressed and purified in the absence of exogenous ligands, making it ideal for ligand binding and coregulator displacement studies.

PR-LBD human recombinant protein is:

• Flexible—use in your in-house assay or as part of our PolarScreen™ Competitor assays for a complete assay solution
• Ready to use—active and tagged (with GST)
• Convenient—available in bulk sizes

Contact us for bulk quantities or for assistance with other nuclear receptor assay needs, from assay development to library screening and beyond.

Used in:
PolarScreen™ Progesterone Receptor Competitor Assay, Red
PolarScreen™ Progesterone Receptor Competitor Assay, Green

Protein Form: Ligand Binding Domain, Recombinant

Target Information

The progesterone receptor (PR) is a member of the steroid family of nuclear receptors. The PR mediates the physiological effects of progesterone, which plays a central role in reproductive events associated with the establishment and maintenance of pregnancy. PR is found as a 94 kDa protein (Form A) or a 120 kDa protein (Form B) due to the use of alternative translation initiation sites. PR-B is the transcriptionally active form and is responsible for activating genes for the maintenance of the endometrium, maintenance of pregnancy, and inhibition of ovulation. PR-A is identical to PR-B except for a 165 amino acid deletion at the N-terminus. This deletion exposes a 140 amino acid inhibitory domain (ID) that acts as a repressor of steroid hormone transcriptional activity. In its inactive state, PgR forms a multiprotein complex which includes heat shock proteins and immunophins. Upon binding of progesterone hormone to its receptor, there is a conformational change that allows dimerization and binding of the receptor to progesterone response elements (PRE) sequences, resulting in activated transcription. A Null mutation in the PGR gene leads to pleiotrophic reproductive abnormalities.

For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.