Recombinant Human SP-D Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 1920-SP

R&D Systems, part of Bio-Techne
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1920-SP-050
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Key Product Details

Source

NS0

Accession #

P35247

Structure / Form

Oligomer

Conjugate

Unconjugated

Applications

Binding Activity

View all SP-D Proteins and Enzymes »

Product Specifications

Source

Mouse myeloma cell line, NS0-derived human SP-D protein
Ala21-Phe375 (Glu22Gly)

Purity

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

Endotoxin Level

<0.10 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Ala21

Predicted Molecular Mass

35.4 kDa (monomer)

SDS-PAGE

40-48 kDa, reducing conditions

Activity

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 0.5-3 µg/mL.

Reviewed Applications

Read 1 review rated 5 using 1920-SP in the following applications:

Formulation, Preparation and Storage

1920-SP
Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution
Reconstitute at 100 μg/mL in sterile PBS.

Reconstitution Buffer Available:
Size / Price
Qty
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.

Background: SP-D

SP-D (surfactant protein-D; also PSP-D) is a 43 kDa member of the collectin family of innate immune modulators. It is constitutively secreted by alveolar lining cells and epithelium associated with tubular structures. Its principal components consist of a collagen-like region and a C-terminal carbohydrate recognition domain (CRD), a structure that further places it in a subset of an expanded group of proteins termed defense collagens (1-4). Human SP-D is synthesized as a 375 amino acid (aa) precursor. It contains a 20 aa signal sequence and a 355 aa mature region. The mature molecule is characterized by the presence of 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, 6). Two additional, potential isoforms exist. One shows a 13 aa N-terminal extension, while the other combines the N-terminal extension with a deletion of aa’s # 206-375. Mature human SP-D shares 75% and 78% aa identity with mouse and pig SP-D, respectively. Monomeric SP-D is unusual (3). The basic form of SP-D is that of a glycosylated, disulfide-linked 150 kDa trimer that generates an alpha-helical coiled-coil structure linked to a “head” of three symmetrical CRDs (4, 7). Each CRD recognizes the hydroxides of one monosaccharide (4). Trimerization allows for the discrimination of monosaccharide patterns specific to microbial pathogens (7). Typically, SP-D forms a higher-order 620 kDa, X-shaped dodecamer through disulfide bonds associated with the N-terminus (8). This allows for even finer discrimination of self vs. nonself carbohydrate patterns, and facilitates binding to complex antigens (8, 9). One polymorphism, a Met11-Thr11 transition in human, apparently precludes the formation of oligomers, potentially affecting the ability of affected individuals to interact with microorganisms (9, 10). Finally, SP-D is known to bind both SIRP alpha and the calreticulin/CD91 complex on macrophages. 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. When virtually all CRDs are occupied by ligand, however, free CRDs are not available for SIRP alpha binding. Instead, the dodecamer is depicted to undergo a structural rearrangement, exposing the N-termini of all four linked trimers. This exposed terminus is known to bind to the calreticulin/CD91 complex, an event that initiates inflammation. Thus, it would appear that SP-D allows for a graded response to environmental challenge. SP-D provides a mechanism for the clearance of small antigenic insults without the need for a damaging inflammatory response (3).

References

  1. Holmskov, U. et al. (2003) Annu. Rev. Immunol. 21:547.
  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. Rust, K. et al. (1991) Arch. Biochem. Biophys. 290:116.
  6. Lu, J. et al. (1992) Biochem. J. 284:795.
  7. Hakansson, K. et al. (1999) Structure 7:225.
  8. Ohya, M. et al. (2006) Biochemistry 45:8657.
  9. Crouch, E.C. et al. (2006) Am. J. Respir. Cell Mol. Biol. 35:84.
  10. Leth-Larsen, R. et al. (2005) J. Immunol. 174:1532.

Long Name

Surfactant Pulmonary Associated Protein D

Alternate Names

Collectin 7, PSP-D, SFTP4, SFTPD, SPD

Entrez Gene IDs

6441 (Human); 20390 (Mouse)

Gene Symbol

SFTPD

UniProt

P35247

Additional SP-D Products

Product Documents for Recombinant Human SP-D Protein, CF

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Product Specific Notices for Recombinant Human SP-D Protein, CF

For research use only

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