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Recombinant Human Properdin Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human Properdin Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. Recombinant Human Properdin binds to Zymosan with a ED50 of ≤1.25 µg/mL.
Source
Human embryonic kidney cell, HEK293-derived human Properdin protein
Asp28-Leu469, with a C-terminal 10-His tag
Accession #
N-terminal Sequence
Asp28
Protein/Peptide Type
Recombinant Proteins
Gene
CFP
Purity
>95%, by SDS-PAGE with silver 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
57-63 kDa, reducing conditions

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after opening.
  • 3 months, -20 to -70 °C under sterile conditions after opening.
Buffer
Supplied as a 0.2 μm filtered solution in Sodium Citrate and NaCl.
Purity
>95%, by SDS-PAGE with silver staining.

Notes

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

Alternate Names for Recombinant Human Properdin Protein, CF

  • BFD
  • CFP
  • Complement Factor P
  • complement factor properdin
  • PFC
  • PFCcomplement
  • PFD
  • Properdin

Background

Properdin, also known as Complement Factor P, is an approximately 53 kDa glycoprotein that positively regulates the complement alternative pathway (AP) (1, 2). It consists of seven thrombospondin repeat (TSR) domains, referred to as TSR0-TSR6 beginning at the N-terminus (3). Under physiological conditions, Properdin can form cyclic dimers, trimers, and tetramers through head-to-tail interactions of monomeric subunits (4-6). Non-physiological high molecular weight polymers of Properdin can also form during long term storage and freeze/thaw cycles (5, 7). Mature human Properdin shares 79% and 77% amino acid sequence identity with rat and mouse Properdin, respectively. Interestingly, human Properdin has been shown to restore LPS-dependent AP complement activity in Properdin-/- mouse serum (8). Properdin may also act as a pattern-recognition molecule, since it binds glycosaminoglycan (GAG) chains of proteoglycans on apoptotic T cells to promote complement activation and phagocytosis (9). Furthermore, Properdin has been shown to bind certain microbial targets and serve as a platform for C3bBbP assembly and function (10, 11). Underscoring its importance to immunity, Properdin deficiency is associated with significant risk of meningococcal disease in humans (12). It may also be involved in the development of abdominal aortic aneurysm, an inflammatory vascular disease (13).
  1. Pillemer, L. et al. (1954) Science 120:279.
  2. Kemper, C. et al. (2010) Annu. Rev. Immunol. 28:131.
  3. Alcorlo, M. et al. (2013) Proc. Natl. Acad. Sci. USA 110:13504.
  4. Smith, C.A. et al. (1984) J. Biol. Chem. 259:4582.
  5. Pangburn, M.K. (1989) J. Immunol. 142:202.
  6. Cortes, C. et al. (2013) Front. Immunol. 3:412.
  7. Farries, T.C. et al. (1987) Biochem. J. 243:507.
  8. Kimura, Y. et al. (2008) Blood 111:732.
  9. Kemper, C. et al. (2008) Proc. Natl. Acad. Sci. USA 105:9023.
  10. Hourcade, D.E. (2006) J. Biol. Chem. 281:2128.
  11. Spitzer, D. et al. (2007) J. Immunol. 179:2600.
  12. Linton, S.M. and B.P. Morgan (1999) Clin. Exp. Immunol. 118:189.
  13. Zhou, H.F. et al. (2012) Proc. Natl. Acad. Sci. USA 109:E415.

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Bioinformatics

Gene Symbol CFP
Uniprot