Recombinant Cynomolgus SIRP beta 1/CD172b His Protein, CF Summary
Glu30-Pro369, with a C-terminal 6-His tag
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.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.|
|Reconstitution||Reconstitute at 500 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.
When Recombinant Cynomolgus Monkey SIRP beta 1/CD172b (Catalog # 10192-SB) is immobilized at 1 μg/mL, 100 μL/well, Recombinant Human SP-D(Catalog # 1920-SP) binds with an ED50of 0.15-0.9 μg/mL.
2 μg/lane of Recombinant Cynomolgus Monkey SIRP beta 1/CD172b His-tag was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® blue staining, showing bands at 53-68 kDa.
Background: SIRP beta 1/CD172b
Signal-regulatory protein beta 1 (SIRP beta 1) is a disulfide-linked type I membrane glycoprotein that belongs to the SIRP/SHPS (CD172) family of the immunoglobulin (Ig) superfamily (1). Mature cynomolgus SIRP beta 1 consists of a 342 amino acid (aa) extracellular domain (ECD), a 26 aa transmembrane segment, and a short 4 aa cytoplasmic domain. Within the ECD, cynomolgus SIRP beta 1 shares 87% aa sequence identity with human SIRP beta 1. The SIRP family are paired receptors that have similar extracellular domains but differing C-terminal domains and functions (1). Members of this family are characterized by an extracellular region containing a V-set Ig domain containing a J-like sequence and two C1-set Ig domains (2). Positively charged residues within the transmembrane domain mediate interactions with DAP12 proteins which contain immunoreceptor tyrosine-based activation motifs (ITAMs) (3). Proteins in the SIRP family are typically expressed in cells of monocyte, macrophage or dendritic lineages (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 induce 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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