PDGFRB Antibodies

Structure of PDGFRB

The protein encoded by the PDGFRB gene is a transmembrane tyrosine kinase receptor with a molecular weight of approximately 123 kDa. This value is highly conserved among different species because its protein structure and function are of vital importance.

This protein is composed of 1106 amino acids, and its primary structure folds to form characteristic extracellular ligand-binding domains (five immunoglobulin-like domains), transmembrane regions, and intracellular tyrosine kinase domains. In its three-dimensional structure, the kinase domain presents a self-inhibitory conformation in the non-activated state, and specific amino acids in the near-membrane region (such as human Asn666) are crucial for maintaining this conformation. Ligand binding triggers receptor dimerization, leading to auto-phosphorylation of tyrosine residues (such as Tyr857 and Tyr1021), thereby opening the kinase active center and recruiting downstream signaling molecules to drive cellular responses.

Fig. 1 Structures of WT PDGFRB and NRIP1::PDGFRB predicted with AlphaFold2.¹

Key structural properties of PDGFRB:

• Extracellular immunoglobulin-like domains
• Proximal membrane autoinhibitory domain
• Split tyrosine kinase domain

Functions of PDGFRB

The receptor protein encoded by the PDGFRB gene plays a core role in cell signal transduction, with its main function being to regulate cell proliferation, survival and migration. However, it has also been found to be involved in a variety of physiological and pathological processes, including angiogenesis, tissue repair and tumorigenesis.

Like most single-pass transmembrane receptors, the activation of PDGFRB strictly depends on ligand-induced dimerization, and its signal transduction is typically spatiotemporal specific. Its function-acquired mutations can disrupt this regulation, leading to the continuous activation of receptors, and are key drivers of various myeloproliferative neoplasms and stromal tumors.

Applications of PDGFRB and PDGFRB Antibody in Literature

• Hao, Li, et al. "Somatic PDGFRB activating variants promote smooth muscle cell phenotype modulation in intracranial fusiform aneurysm." Journal of Biomedical Science 31.1 (2024): 51. https://doi.org/10.1186/s12929-024-01040-7 

Research reveals that somatic mutations in PDGFRB activate the JAK-STAT pathway, leading to inflammatory phenotypic transformation in vascular smooth muscle cells and thereby driving the formation of fusiform aneurysms. Experiments have confirmed that the JAK inhibitor ruxolitinib can reverse this process, providing a new direction for treatment.

• Mathorne, Stine Westergaard, et al. "A novel PDGFRB sequence variant in a family with a mild form of primary familial brain calcification: a case report and a review of the literature." BMC neurology 19.1 (2019): 60. https://doi.org/10.1186/s12883-019-1292-8

A novel PDGFRB mutation (p.Gly612Arg) associated with cerebral calcification has been identified through research. This mutation is located in the tyrosine kinase domain. The symptoms and calcification degree of patients are usually mild. CT scans can detect asymptomatic mutation carriers.

• Li, Zhaoming, et al. "Recurrent PDGFRB mutations in unicentric Castleman disease." Leukemia 33.4 (2019): 1035-1038. https://doi.org/10.1038/s41375-018-0323-6

Whole exome sequencing studies have found that 17% of patients with single-center Castleman disease (UCD) have the PDGFRB p.asen666SER mutation. This mutation has the highest incidence in UCD among related cancers and is disease-specific, providing new clues for its pathogenesis.

• Sadras, Teresa, et al. "Unusual PDGFRB fusion reveals novel mechanism of kinase activation in Ph-like B-ALL." Leukemia 37.4 (2023): 905-909. https://doi.org/10.1038/s41375-023-01843-x 

The study found that a novel CD74::PDGFRB fusion variant was discovered in children with Ph-like B-ALL. Although this variation does not form chimeric proteins, it can activate PDGFRB tyrosine kinases, drive leukemia occurrence, and provide a basis for targeted therapy.

• Nédélec, Audrey, et al. "Penttinen syndrome‐associated PDGFRB Val665Ala variant causes aberrant constitutive STAT1 signaling." Journal of cellular and molecular medicine 26.14 (2022): 3902-3912. https://doi.org/10.1111/jcmm.17427

Research has found that the PDGFRB p.Val665Ala mutation that causes Penttinen progeria continuously activates STAT1, triggering a unique interferon-like response that is not inhibited by ruxolitinib. This characteristic differs from other carcinogenic mutations and may explain its unique symptoms.

Creative Biolabs: PDGFRB Antibodies for Research

Creative Biolabs specializes in the production of high-quality PDGFRB antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom PDGFRB Antibody Development: Tailor-made solutions to meet specific research requirements.
• Bulk Production: Large-scale antibody manufacturing for industry partners.
• Technical Support: Expert consultation for protocol optimization and troubleshooting.
• Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.

For more details on our PDGFRB antibodies, custom preparations, or technical support, contact us at email.