Recombinant Human SIRP beta 2 Fc Chimera Protein, CF Summary
|Human SIRP beta 2|
Accession # Q5JXA9
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.|
|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.
When Recombinant Human SIRP beta 2 Fc Chimera (Catalog #9998-SB) is immobilized at 1 µg/mL, Biotinylated Recombinant CD300B/LMIR-5 Fc Chimera binds with an ED50 of 2‑10 μg/mL.
2 μg/lane of Recombinant Human SIRP beta 2 Fc Chimera was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 77-85 kDa and 150-170 kDa, respectively.
Background: SIRP beta 2
Signal-regulatory protein beta-2(SIRP-beta-2), is a ~37 kDa monomeric single pass type I membrane glycoprotein. It belongs to the SIRP/SHPS (CD172) family of the immunoglobulin (Ig) superfamily (1). The SIRP family are paired receptors that have similar extracellular domains but differing C-terminal domains and functions (1). SIRP-beta-2 contains an N-terminal signal peptide (aa1-32), two extracellular Ig-like domains: a V-type 1 (aa 33-143) and a V-type 2 (aa 157-258) containing three potential N-linked glycosylation sites, a helical transmembrane domain (aa 288-308), and a cytoplasmic domain (aa 309-342) (1). A positively charged residue within the transmembrane domain, in analogy to SIRP-beta-1, is implicated to mediate interaction with the adaptor DAP12 protein, which contains immunoreceptor tyrosine-based activation motifs (ITAMs) (2). Proteins in the SIRP family are typically expressed in immune cells, especially in the myeloid lineages (3). Based on expression patterns, SIRPs are thought to have roles in immune regulation (4). SIRP family members role in innate immunity and host defense has potential significance as a therapeutic target in cancer and inflammation (5, 6). There are currently no known mouse or rat homologs for this protein.
- van Beek, E.M. et al. (2005) J. Immunol. 175:7781.
- Liu, Y. et al. (2005) Journal of Biological Chemistry. 280:36132.
- Matozaki, T. et al. (2009) Trends in Cell Biology. 19:72.
- Barclay A.N. et al. (2006) Nat Rev Immunol. 6:457.
- Barclay A.N. et al. (2014) Annu Rev Immunol. 32:25.
- Veillette A. (2018) Trends Immunol. 39:173.
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