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Recombinant Cynomolgus Monkey CD43 Fc Chimera Protein, CF

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2 μg/lane of Recombinant Cynomolgus Monkey CD43 Fc Chimera Protein (Catalog # 11205-CD) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, ...read more

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Summary
Reactivity Pm-CmSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Cynomolgus Monkey CD43 Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Cynomolgus Monkey CD-43 Fc Chimera (Catalog # 11205-CD) is immobilized at 1.00 μg/mL (100 μL/well), Recombinant Human Siglec-1 Protein (Catalog # 5197-SL) binds with an ED50 of 1.50-7.50 μg/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived cynomolgus monkey CD43 protein
Cynomolgus Monkey CD43
(Asp20-Thr258)
Accession # EHH60309.1
IEGRMD Human IgG1
(Pro100-Lys330)
N-terminusC-terminus
Accession #
N-terminal Sequence
Asp20
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
50 kDa.
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
106-118 kDa, under reducing conditions.

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 with Trehalose.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 500 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 Cynomolgus Monkey CD43 Fc Chimera Protein, CF

  • CD43 antigen
  • CD43
  • CD43)
  • Galactoglycoprotein
  • GALGP
  • GPL115
  • Leukocyte sialoglycoprotein
  • Leukosialin
  • LSN
  • Ly-48
  • sialophorin (gpL115, leukosialin, CD43)
  • Sialophorin
  • SPN

Background

CD43, also known as Leukosialin and Sialophorin and Ly-48, is a type I transmembrane sialylated mucin that is expressed on most leukocytes and some tumor cells (1). Notably, the membrane expression of CD43 seems to be a characteristic of leukocytes, while cytoplasmic expression without membrane insertion occurs in endothelium and select epithelia. While CD43 restricts leukocyte adhesion and modulates T cell activation, these activities are context specific (2). CD43 can both induce and protect against apoptosis and can either promote or block cell adhesion (3). CD43 with altered glycosylations are expressed in cancers (4). The extracellular portion of cynomolgus monkey CD43 has a 78.2%, and 93.0% identity to human and rhesus monkeys, respectively.. CD43 induced cellular adhesion through the binding to molecules such as E-selectin (5, 6), galectin-1 and galectin-3 (7), siglec-1 (8), M-ficolin (9), integrins (10), cell surface nucleolin (11), and ICAM-1 (intercellular adhesion molecule type 1) (12). During cancer development, CD43 signalling induces the activation of 𝛽-catenin, NF-𝜅B (13, 14), NFAT, and AP-1, which are prosurvival transcription factors that can promote tumorigenesis when deregulated (15, 16).
  1. Santamaría, M. et al. (1996) Cancer Res. 56:3526.
  2. Manjunath, N. et al. (1995) Nature 377:535.
  3. Brown, T.J. et al. (1996) J. Biol. Chem. 271:27686.
  4. Tuccillo, F.M. et al. (2014) BioMed Res International. https://doi.org/10.1155/2014/742831.
  5. Fuhlbrigge, R.C. et al. (2006) Blood 107:1421.
  6. Matsumoto, M. et al. (2005) J. Immuno. 175:8042.
  7. Yang, R.Y. et al. (2008) Expert Rev. Mol. Med. 10:e17.
  8. van den Berg, T.K. et al. (2001) J. Immuno. 166:3637.
  9. Moreno-Amaral, A.N. et al. (2012) J. Leukoc. Bio. 91:469.
  10. Sanchez-Mateos, P. et al. (1995) Blood, 86:2228.
  11. Hirano, K. et al. (2005) J. Biol. Chem. 280:39284.
  12. Rosenstein, Y. et al. (1991) Nature 354:233.
  13. Fiume, G. et al. (2013) PLoS ONE 8:e66087.
  14. Fiume, G. et al. (2012) Nucleic Acids Res. 40:3548.
  15. Andersson, C.C. et al. (2005) Biochem. J. 387:377.
  16. Santana, M.A. et al. (2000) J Biol. Chem. 275:31460.

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