Reactivity | MuSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Details of Functionality | Measured by its binding ability in a functional ELISA. When 0.5 μg/mL of rmPodoplanin/Fc is immobilized onto a Goat Anti-Mouse IgG Fc chimera (R&D Systems, Catalog # G-202-C) coated plate, the concentration of rhCLEC-2 that produces 50% of the optimal binding response is found to be approximately 0.3-1.8 nM. |
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Source | Mouse myeloma cell line, NS0-derived mouse Podoplanin protein
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Accession # | |||||||
N-terminal Sequence | Results not obtained: Gln21 predicted |
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Structure / Form | Disulfide-linked homodimer |
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Protein/Peptide Type | Recombinant Proteins |
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Gene | Pdpn |
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Purity | >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
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Endotoxin Note | <0.01 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 19.0 kDa (monomer). 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. |
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SDS-PAGE | 45-70 kDa, reducing conditions |
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Publications |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in PBS |
Purity | >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions | Reconstitute at 100 μg/mL in PBS. |
Podoplanin, also known as glycoprotein 38 (gp38), PA2.26 antigen, T1-alpha (T1A), and aggrus, is a 38 kDa type I transmembrane sialoglycoprotein and member of the podoplanin family (1, 2). Podoplanin is synthesized as a 172 amino acid (aa) precursor with a 22 aa signal sequence, a 119 aa extracellular domain (ECD), a 21 aa transmembrane region, and a short, 10 aa cytoplasmic tail (SwissProt #: Q62011). The ECD contains abundant Ser/Thr residues as potential sites for O-glycosylation, and the cytoplasmic region contains putative sites for kinase C and cAMP phosphorylation (2, 3). Mouse Podoplanin shares 77% and 46% aa sequence identity with rat and human Podoplanin, respectively. Podoplanin is expressed on glomerular epithelial cells (podocytes), type I lung alveolar cells, lymphatic endothelial cells (4, 5), and on numerous tumors including colorectal tumors (3), squamous cell carcinomas (4, 6), testicular seminoma (7), and brain tumors (8-10). One study shows high expression of Podoplanin mRNA in placenta, lung, skeletal muscle, and heart, and weaker levels in brain, kidney, and liver (1). Podoplanin is the ligand for C-type lectin-like receptor 2 (CLEC-2) (2). Their association is dependent on sialic acid on O-glycans of Podoplanin (2). Through its association with CLEC-2, Podoplanin induces platelet aggregation and tumor metastasis (2). Podoplanin is also necessary for lymphatic vessel formation, normal lung cell proliferation and alveolus formation at birth (2).
Spheroids vs. Organoids: Which 3D Cell Culture Model is Best for You? By Jennifer Jones, M.S.Spheroids and organoids are two words that, like “butter” and “margarine”, are often referred to interchangeably but have distinct meanings. The progression and adopt... Read full blog post. |
Meningeal lymphatics: recent discovery defying the concept of central nervous system 'immune privilege' By Jennifer Sokolowski, MD, PhD. Identification and characterization of meningeal lymphaticsThe recent discovery of a lymphatic system in the meninges surrounding the brain and spinal cord has spurred a surge of int... Read full blog post. |
Podoplanin (OST8, Glycoprotein (Gp) 36 or 38, Lung Type I Cell Membrane Associated Glycoprotein) Podoplanin is a mucin-type 1 transmembrane glycoprotein found in a wide range of tissues. It appears to be differentially expressed in endothelial cells of lymphatic but not blood vessel origin. In normal skin and kidney, podoplanin co-localizes with ... Read full blog post. |
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