Recombinant Mouse SIRP beta 1B Fc Chimera Protein, CF Summary
Product Specifications
Mouse SIRP beta 1B (Met28-Gly360) Accession # NP_001166931.1 | IEGRMDP | Mouse IgG2a (Glu98-Lys330) |
N-terminus | C-terminus | |
Analysis
Met28 and Arg29
Product Datasheets
Carrier Free
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.
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.
10335-SB
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
Reconstitution | Reconstitute at 500 μg/mL in PBS. |
Shipping | The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Scientific Data

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