PDPN Antibodies

Structure of PDPN

PDPN is a type I transmembrane glycoprotein with a molecular weight of approximately 36-40 kDa. There are variations in molecular weight among different species, mainly due to the degree of glycosylation and minor changes in the amino acid sequence.

The molecular weight of human PDPN is approximately 38 kDa and it is glycosylated; in mice, it is about 36 kDa, with slightly different glycosylation sites from those in humans; in rats, it is approximately 36-38 kDa, and the sequence is highly similar to that of humans; in dogs, it is about 37 kDa, with relatively conserved structure; in rabbits, it is about 38 kDa, and the antibody cross-reactivity is good.

The extracellular region of the PDPN protein is rich in serine and threonine residues, which is the main area for O-glycosylation. Its transmembrane region is highly conserved, while the intracellular region is relatively short but contains multiple phosphorylation sites, which can mediate intracellular signal transduction. The platelet receptor CLEC-2 recognizes the specific glycosylation epitopes of PDPN and activates downstream signaling pathways. This protein is stably expressed in lymphatic endothelial cells, but is abnormally highly expressed in some tumor cells, often indicating an increased risk of lymph node metastasis.

Fig. 1 Schematic representation of podoplanin (PDPN) structure and functions.¹

Key structural properties of PDPN:

• Type I transmembrane glycoprotein structure, with a longer extracellular region
• The O-glycosylation region rich in serine/threonine
• Across the membrane area highly conservative, intracellular shorter tail area
• Nearly with CLEC - 2 receptor recognition with platelet membrane end table

Functions of PDPN

The main function of PDPN is to participate in lymphangiogenesis and tumor metastasis, but it also plays a role in various physiological and pathological processes, including platelet aggregation, immune regulation and developmental signal transduction.

The binding of PDPN to its endogenous ligand CLEC-2 is highly specific. This axis is involved in the maturation of cerebral blood vessels and lymphatic vessel separation during embryonic development, and is largely silent in adulthood. However, it is reactivated in various malignant tumors.

Applications of PDPN and PDPN Antibody in Literature

1. Suzuki, Hiroyuki, Mika K. Kaneko, and Yukinari Kato. "Roles of podoplanin in malignant progression of tumor." Cells 11.3 (2022): 575. https://doi.org/10.3390/cells11030575

Studies have shown that PDPN is a glycoprotein that is overexpressed in various tumors, which can promote tumor malignancy progression and immune evasion, and participate in the remodeling of the tumor microenvironment. Targeted therapeutic strategies against PDPN have become a new research direction in cancer treatment.

2. Sikorska, Justyna, et al. "Podoplanin (PDPN) affects the invasiveness of thyroid carcinoma cells by inducing ezrin, radixin and moesin (E/R/M) phosphorylation in association with matrix metalloproteinases." BMC cancer 19.1 (2019): 85. https://doi.org/10.1186/s12885-018-5239-z

The research shows that in thyroid cancer BcPAP cells, inhibiting the expression of PDPN can reduce cell migration and invasion by regulating E/R/M proteins and MMPs, and its effect is related to the MAPK signaling pathway.

3. Feng, Chunyan, et al. "A novel PDPN antagonist peptide CY12-RP2 inhibits melanoma growth via Wnt/β-catenin and modulates the immune cells." Journal of Experimental & Clinical Cancer Research 43.1 (2024): 9. https://doi.org/10.1186/s13046-023-02910-y

Studies have shown that PDPN is overexpressed in melanoma. Its antagonist peptide CY12-RP2 can specifically bind to PDPN and effectively inhibit tumor growth and metastasis by suppressing the Wnt/β-catenin pathway and activating immune cells.

4. Wang, Xuya, et al. "PDPN contributes to constructing immunosuppressive microenvironment in IDH wildtype glioma." Cancer Gene Therapy 30.2 (2023): 345-357. https://doi.org/10.1038/s41417-022-00550-6

Studies have confirmed that PDPN is highly expressed in IDH wild-type gliomas and is an independent poor prognostic indicator. It promotes the M2 polarization of macrophages and the degranulation of neutrophils, thereby driving the formation of an immunosuppressive microenvironment.

5. Li, Ke, et al. "A circular RNA activated by TGFβ promotes tumor metastasis through enhancing IGF2BP3-mediated PDPN mRNA stability." Nature Communications 14.1 (2023): 6876. https://doi.org/10.1038/s41467-023-42571-1

The study found that TGFβ-induced circITGB6 stabilizes PDPN mRNA, enhancing the epithelial-mesenchymal transition and metastasis ability of colorectal cancer. Its high expression is associated with poor prognosis in patients. Targeting circITGB6 is expected to inhibit tumor metastasis.

Creative Biolabs: PDPN Antibodies for Research

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

• Custom PDPN 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 PDPN antibodies, custom preparations, or technical support, contact us at email.