Recombinant Mouse Podoplanin Fc Chimera Protein, CF

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Product Details

Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Mouse Podoplanin Fc Chimera Protein, CF Summary

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.
Source
Mouse myeloma cell line, NS0-derived mouse Podoplanin protein
Mouse Podoplanin
(Gln21-Lys133)
Accession # Q62011
IEGRMDP Mouse IgG2A
(Glu98-Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
Results not obtained: Gln21 predicted
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
Pdpn
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
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.
SDS-PAGE
45-70 kDa, reducing conditions
Publications
Read Publications using
3244-PL in the following applications:

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
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.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse Podoplanin Fc Chimera Protein, CF

  • 36-KD
  • Aggrus
  • Gp36
  • Gp38
  • GP40
  • HT1A-1
  • hT1alpha-1
  • hT1alpha-2
  • lung type I cell membrane associated glycoprotein
  • lung type-I cell membrane-associated glycoprotein (T1A-2)
  • OTS 8
  • OTS8
  • PA2.26 antigen
  • PDPN
  • Podoplanin
  • RANDAM-2
  • T1A
  • T1A-2
  • T1-alpha

Background

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).

  1. Zimmer, G. et al. (1999) Biochem. J. 341:277.
  2. Katsue-Inoue, K. et al. (2007) J. Biol. Chem. 282:25993.
  3. Kato, Y. et al. (2003) J. Biol. Chem. 278:51599.
  4. Schacht, V. et al. (2005) Am. J. Pathol. 166:913.
  5. Breiteneder-Geleff, S. et al. (1997) Am. J. Pathol. 151:1141.
  6. Kato, Y. et al. (2005) Tumour Biol. 26:195.
  7. Kato, Y. et al. (2004) Oncogene 23:8552.
  8. Mishima, K. et al. (2006) Acta Neuropathol. 111:563.
  9. Mishima, K. et al. (2006) Acta Neuropathol. 111:483.
  10. Kato, Y. et al. (2006) Biochem. Biophys. Res. Commun. 349:1301.

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Publications for Podoplanin (3244-PL)(3)

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Bioinformatics

Gene Symbol Pdpn
Uniprot