Verified Applications: ELISA for PRLR-specific antibody binding assays.
Suggested Applications: ELISA for PRLR and prolactin (PRL) ligand protein binding assays. SPR & BLI for PRLR-specific antibody and PRL protein binding assays. Animal immunization, RUO.
Purity: Greater than 90% dimer form as determined by SDS-PAGE under non-reducing condition
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Mouse Prolactin receptor (PRLR) is a class 1 cytokine receptor glycoprotein that can homodimerize. The recombinant mouse PRLR protein dimer (CSP-25160-01) is a cis-homodimer (cis-dimer) and contains a PRLR extracellular domain (UniProt# Q08501, amino acids Gln20-Asp229) fused with a proprietary cis-dimer motif followed by a His tag at the C-terminus. This dimeric protein is expressed in HEK293T cells. The recombinant mouse PRLR protein dimer is bioactive and binds PRLR-specific antibodies. This mouse PRLR dimer can be used as an antigen for in vitro assays and antibody screening, and as an immunogen for immunization to generate antibodies targeting more conformational epitopes.
Protein Name: PRLR
UniProt #: AA: Q08501
Predicted Molecular Weight: 65 kDa
SDS PAGE Molecular Weight: The migration range of the dimer protein with glycosylation under non-reduced condition is between 120 and 190 kDa on SDS PAGE.
Protein Construct: Mouse PRLR protein dimer contains a PRLR extracellular domainfused with a proprietary cis-dimer motif followed by a His tag at the C-terminus.
Background
Prolactin receptor (PRLR), also known as PRL-R, is a class 1 cytokine receptor glycoprotein that binds prolactin (PRL). PRLR contains an extracellular domain with a cytokine homology module formed by two fibronectin type III domains, D1 and D2, followed by a transmembrane domain and cytoplasmic domain. PRLR is expressed on cells in mammary glands, pituitary gland, and other tissues. PRLR exists as a monomer and can form dimers. PRLR dimerization is a critical mechanism in PRL signaling, influencing numerous physiological and pathological processes. PRLR pathological dimerization, including constitutive or ligand-independent PRLR dimers sustain abnormal signaling, contributes to cancer, hyperprolactinemia, and immune dysfunction. Dysregulation of PRLR can promote tumor activity and positively regulate the proliferation of malignant cells in breast cancer. PRLR is an attractive therapeutic target for PRLR related diseases including breast cancer, hyperprolactinemia, and metabolic disorders. While structurally and functionally similar to human PRLR, mouse PRLR is a species-specific tool essential for preclinical studies, basic research, and translational research in cancer immunotherapy.
MW: Molecular Weight marker reduced condition
NR: PRLR dimer under non-reduced condition
Immobilized mouse PRLR protein dimer