Recombinant Mouse SP-D Protein, CF

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Recombinant Mouse SP-D Protein, CF Summary

Product Specifications

>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Measured by its ability to bind fluorescein-conjugated E. coli Bioparticles. Kuan, S.F. et al. (1992) J. Clin. Invest. 90:97. The ED50 for this effect is 0.3‑1.5 µg/mL.
Chinese Hamster Ovary cell line, CHO-derived mouse SP-D protein
Accession #
N-terminal Sequence
Structure / Form
Predicted Molecular Mass
35.7 kDa (monomer)
40-50 kDa, reducing conditions

Product Datasheets

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Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.


Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 200 μg/mL in PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.
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Background: SP-D

SP‑D (surfactant protein‑D; also PSP‑D) is a 43 kDa member of the collectin family of innate immune modulators (1 ‑ 5). It is constitutively secreted by alveolar lining cells and epithelium associated with tubular structures. SP‑D is found in serum, plasma, broncho‑alveolar lavage (BAL) fluid, and amniotic fluid (1, 2, 6). Lung injuries often increase release of SP‑D to the circulation (3, 6). Mouse SP‑D is synthesized as a 374 amino acid (aa) precursor. Mouse SP‑D cDNA encodes a 19 aa signal sequence and a 355 aa mature region with a 25 aa N‑terminal linking‑region, a 177 aa hydroxyproline and hydroxylysine collagen‑like domain, a 46 aa coiled‑coil segment, and a 106 aa, C‑terminal collectin‑like C‑type lectin domain (CRD) (5). Mature mouse SP‑D shares 72 ‑ 76% aa sequence identity with human, porcine, equine, canine and bovine SP‑D, and 92% with rat SP‑D. SP‑D is usually found as a glycosylated, disulfide‑linked 150 kDa alpha ‑helical coiled‑coil trimer with a “head” of three symmetrical CRDs (2 ‑ 4, 7). Each CRD recognizes the hydroxides of one monosaccharide, and trimerization allows for the discrimination of monosaccharide patterns specific to microbial pathogens (4, 7, 8). Typically, SP‑D forms a higher‑order 620 kDa, X‑shaped dodecamer through N‑terminal disulfide bonds, allowing for even finer discrimination of self vs. nonself carbohydrate patterns and facilitating binding to complex antigens (1). SP‑D also binds SIRP alpha and the calreticulin/CD91 complex on macrophages (9, 10). When the ratio of antigen/pathogen to available CRDs is low, antigen can be bound without occupying all available CRDs. The free CRDs will bind to SIRP alpha, generating a signal that downmodulates the inflammatory response. During high CRD ligand binding (low SIRP alpha binding), the dodecamer rearranges to expose N‑termini that bind the calreticulin/CD91 complex, an event that initiates inflammation (1). Also, direct and indirect binding of neutrophil defensins and macrophage CD14 and TLRs to SP‑D can modulate response to viruses and bacterial lipopolysaccharides (1 ‑ 3, 11 ‑ 15). Thus, SP‑D allows for a graded response to environmental challenge and clearance of small antigenic insults without the need for a damaging inflammatory response (1 ‑ 3).

  1. Forbes, L.R. and A. Haczku (2010) Clin. Exp. Allergy 40:547.
  2. Kishore, U. et. al. (2006) Mol. Immunol. 43:1293.
  3. Hartl, D. and M. Griese (2006) Eur. J. Clin. Invest. 36:423.
  4. Sim, R.B. et. al. (2006) Novartis Found Symp. 279:170.
  5. Motwani, M. et al. (1995) J. Immunol. 155:5671.
  6. Honda, Y. et al. (1995) Am. J. Respir. Crit. Care Med. 152:1860.
  7. Hakansson, K. et. al. (1999) Structure 7:225.
  8. Crouch, E.C. et. al. (2006) Am. J. Respir. Cell Mol. Biol. 35:84.
  9. Janssen, W.J. et al. (2008) Am. J. Respir. Crit. Care Med. 178:158.
  10. Gardai, S.J. et al. (2003) Cell 115:13.Ohya, M. et. al. (2006) Biochemistry 45:8657.
  11. Ohya, M. et. al. (2006) Biochemistry 45:8657.
  12. Pastva, A.M. et al. (2007) Proc. Am. Thorac. Soc. 4:252.
  13. Sano, H. and Y. Kuroki (2005) Mol. Immunol. 42:279.
  14. Hartshorn, K.L. et al. (2006) J. Immunol. 176:6962.
  15. Yamazoe, M. et al. (2008) J. Biol. Chem. 283:35878.
Long Name
Surfactant Pulmonary Associated Protein D
Entrez Gene IDs
6441 (Human); 20390 (Mouse)
Alternate Names
COLEC7collectin-7; Collectin 7; Collectin-7; Lung surfactant protein D; PSPD; PSP-D; SFTP4; SFTP4pulmonary surfactant-associated protein D; SFTPD; SPD; SP-D; SP-Dpulmonary surfactant apoprotein; surfactant protein D; surfactant, pulmonary-associated protein D; surfactant-associated protein, pulmonary 4

Citation for Recombinant Mouse SP-D Protein, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

1 Citation: Showing 1 - 1

  1. Association of surfactant protein D with pulmonary metastases from colon cancer
    Authors: Y Tajima, M Tsuruta, H Hasegawa, K Okabayashi, T Ishida, M Yahagi, A Makino, K Koishikawa, S Akimoto, DD Sin, Y Kitagawa
    Oncol Lett, 2020;20(6):322.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay


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