Recombinant Mouse Complement Factor D Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 9207-SE

R&D Systems, part of Bio-Techne
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9207-SE-050
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Key Product Details

Source

NS0

Accession #

P03953

Conjugate

Unconjugated

Applications

Enzyme Activity

View all Complement Factor D/Adipsin Proteins and Enzymes »

Product Specifications

Source

Mouse myeloma cell line, NS0-derived mouse Complement Factor D/Adipsin protein
Ile26-Ser259, with a C-terminal 10-His tag

Purity

>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Endotoxin Level

<1.0 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Ile26 and His35

Predicted Molecular Mass

27 kDa

SDS-PAGE

40-49 kDa, reducing conditions

Activity

Measured by its ability to cleave a colorimetric peptide substrate, N-carbobenzyloxy-Lys-ThioBenzyl ester (Z-Lys-SBzl), in the presence of 5,5’Dithio-bis (2-nitrobenzoic acid) (DTNB). Edwards, K.M. et al. (1999) J. Biol. Chem. 274:30468.
The specific activity is >18 pmol/min/μg, as measured under the described conditions.

Formulation, Preparation and Storage

9207-SE
Formulation Supplied as a 0.2 μm filtered solution in Tris and NaCl.
Shipping The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after opening.

Background: Complement Factor D/Adipsin

Complement Factor D, also known as Adipsin, is a serine protease that catalyzes the initial proteolytic step in the alternative pathway of complement. It cleaves the C3b-bound Factor B, resulting in the formation of a C3bBcomplex, which functions as the alternative pathway C3 convertase (1-3). Factor D is primarily expressed in adipose tissue and is released into the circulation as a zymogen with a 5 amino acid (aa) N-terminal activation peptide (4-6). It is activated by MASP-1 mediated proteolytic removal of the activation peptide (6). Factor D triggered complement activation is important for the clearance of cell debris and control of inflammation following tissue damage (7). The C3 convertase generates C3a which binds to C3a R on pancreatic beta cells to induce insulin production and regulate glucose homeostasis (5). Mature mouse Complement Factor D shares 65% and 83% amino acid sequence identity with human and rat Complement Factor D, respectively. Its protease activity is regulated by reversible conformational changes, which is distinct from most serine proteases whose regulation involves either activation by zymogen processing or inactivation by binding to inhibitors. Compared to its cleavage of C3b-bound Factor B, Factor D has much lower activity toward synthetic peptide substrates. However, thioester substrates have been routinely used for assessing Factor D activity (8).

References

  1. Kijlstra, A. and T.T. Berendschot (2015) Ophthalmic Res. 54:64.
  2. Taylor, F.R. et al. (1999) Biochemistry 38:2849.
  3. Ricklin, D. et al. (2010) Nat. Immunol. 11:785.
  4. White, R.T. et al. (1992) J. Biol. Chem. 267:9210.
  5. Lo, J.C. et al. (2014) Cell 158:41.
  6. Takahashi, M. et al. (2010) J. Exp. Med. 207:29.
  7. Cresci, G.A. et al. (2015) Mol. Immunol. 64:9.
  8. Kim, S. et al. (1995) J. Biol. Chem. 270:24399.

Alternate Names

Adipsin, ADN, AMBP-1, CFD, PFD

Entrez Gene IDs

1675 (Human); 11537 (Mouse); 54249 (Rat)

Gene Symbol

CFD

UniProt

P03953

Additional Complement Factor D/Adipsin Products

Product Documents for Recombinant Mouse Complement Factor D Protein, CF

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Product Specific Notices for Recombinant Mouse Complement Factor D Protein, CF

For research use only

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