Recombinant Mouse SIRP beta 1B Fc Chimera Protein, CF

When Recombinant Mouse SIRP beta 1B Fc Chimera (Catalog # 10335-SB) is immobilized at 1 μg/mL (100 μL/well), Recombinant Human SP-D (Catalog # 1920-SP) binds with an ED50 of 40‑320 ng/mL.

• Reactivity: Mu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Mouse SIRP beta 1B Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Mouse SIRP beta 1B Fc Chimera (Catalog # 10335-SB) is immobilized at 1 µg/mL (100 µL/well), Recombinant Human SP‑D (Catalog # 1920-SP) binds with an ED₅₀ of 40-320 ng/mL.
• Source: Mouse myeloma cell line, NS0-derived mouse SIRP beta 1B protein
  

  Mouse SIRP beta 1B (Met28-Gly360) Accession # NP_001166931.1	IEGRMDP	Mouse IgG2a (Glu98-Lys330)
  N-terminus		C-terminus

• Accession #: NP_001166931.1
• N-terminal Sequence:

  Met28 and Arg29

• 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: 64 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: 70-95 kDa and 175-200 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.
• 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 Mouse SIRP beta 1B Fc Chimera Protein, CF

• SIRP beta 1B

Background

Signal-regulatory protein beta 1b (SIRP beta 1b), or CD172b, is a disulfide-linked type I membrane glycoprotein belonging to the SIRP/SHPS/CD172 family of the immunoglobulin (Ig) superfamily. The three SIRP family members are paired receptors that have a conserved extracellular domain (ECD) but differing C-terminal domains and functions (1). The ECD of SIRP beta 1b contains one V-set Ig and two C1-set Ig domains. The mature ECD of mouse SIRP beta 1b shares 57% amino acid sequence identity with human SIRP beta 1. Proteins in the SIRP family are typically expressed in cells of monocyte, macrophage or dendritic lineages and positively charged residues within the transmembrane domain mediate interactions with DAP12 proteins which contain immunoreceptor tyrosine-based activation motifs (ITAMs) (3, 4). SIRP beta 1 has a relatively short cytoplasmic region and lacks the signaling motifs for association with phosphatases. However, formation of the SIRP beta 1/DAP12 complex in myeloid cells induces tyrosine phosphorylation, mitogen-activated protein kinase activation, and cellular activation (5, 6). Engagement of SIRP beta 1 by specific monoclonal antibodies promoted Fc gamma receptor-dependent or - independent phagocytosis in mouse peritoneal macrophages (7). Surfactant protein D (Sp-D) has been shown to bind SIRP alpha and SIRP beta 1 in a calcium-dependent and sugar-specific manner on a distinct binding site from CD47 (8). Although the SIRP beta 1 extracellular regions share a high degree of homology with the SIRP alpha, SIRP beta 1 has been shown not to bind CD47 (9).

1. vanBeek, E.M. et al. (2005) J. Immunol. 175:7781.
2. van den Berg, T. et al. (2008) Trends in Immunology 29:203.
3. Liu, Y. et al. (2005) Journal of Biological Chemistry 280:36132.
4. Matozaki, T. et al. (2009) Trends in Cell Biology 19:72.
5. Dietrich, J. et al. (2000) J. Immunol. 164:9.
6. Brook, G. et al. (2004) J. Immunol. 173:2562.
7. Hayashi, A. et al. (2004) J. Biol. Chem. 279:29450.
8. Fournier B. et al. (2012) J. Biol. Chem. 287:19386.
9. Seiffert M. et al. (2001) Blood 97:2741.

Bioinformatics

• Uniprot:
  • NP_001166931.1()