Recombinant Mouse SIRP alpha/CD172a Fc Chimera Protein, CF

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Recombinant Mouse SIRP alpha /CD172a Fc Chimera (Catalog # 7154-SA) supportsthe adhesion of mouse red blood cells. The ED50 for this effect is 0.4‑1.6 µg/mL.

Product Details

Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Mouse SIRP alpha/CD172a Fc Chimera Protein, CF Summary

Details of Functionality
Measured by the ability of the immobilized protein to support the adhesion of mouse red blood cells.

The ED50 for this effect is 0.4-1.6 μg/mL.

Optimal dilutions should be determined by each laboratory for each application.

Source
Mouse myeloma cell line, NS0-derived mouse SIRP alpha/CD172a protein
Mouse SIRP alpha /CD172a
(Met1-Asn373) (Gly365Asp)
Accession # P97797
IEGRMDP Mouse IgG2A
(Glu98-Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
Lys32
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
Sirpa
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
65.1 kDa (monomer).
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
115-125 kDa, reducing conditions
Publications
Read Publication using
7154-SA in the following applications:

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 under reducing conditions and visualized by silver stain.
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 alpha/CD172a Fc Chimera Protein, CF

  • BIT
  • BITbrain-immunoglobulin-like molecule with tyrosine-based activation motifs
  • Brain Ig-like molecule with tyrosine-based activation motifs
  • CD172 antigen-like family member A
  • CD172a antigen
  • CD172a
  • Inhibitory receptor SHPS-1
  • Macrophage fusion receptor
  • MFR
  • MFRtyrosine phosphatase SHP substrate 1
  • MyD-1 antigen
  • MYD1
  • MYD-1
  • P84
  • protein tyrosine phosphatase, non-receptor type substrate 1
  • PTPNS1
  • SHP substrate 1
  • SHPS1
  • SHPS-1
  • SHPS1CD172A
  • signal-regulatory protein alpha
  • Signal-regulatory protein alpha-1
  • Signal-regulatory protein alpha-2
  • Signal-regulatory protein alpha-3
  • SIRP alpha
  • SIRPA
  • SIRPalpha
  • Sirp-alpha-1
  • SIRPalpha2
  • Sirp-alpha-2
  • Sirp-alpha-3
  • SIRPtyrosine-protein phosphatase non-receptor type substrate 1

Background

Signal regulatory protein alpha (SIRP alpha , designated CD172a), also called SHPS-1 (SHP substrate 1) and previously, MyD-1 (Myeloid/Dendritic-1), is a homodimeric, 100-105 kDa type I transmembrane glycoprotein that belongs to the SIRP/SHPS (CD172) family of the immunoglobulin superfamily (1-5). SIRPs are paired receptors, with similar extracellular domains but differing C-termini and functions (1, 2). The 513 amino acid (aa) mouse SIRP alpha contains a 342 aa extracellular domain (ECD) with one V‑type and two C1 type Ig domains and many potential N‑glycosylation sites. It has a 117 aa cytoplasmic sequence with ITIM motifs that recruit tyrosine phosphatases SHP-1 and SHP-2 when phosphorylated (4). Mouse and human SIRP alpha have at least 30 described polymorphisms, including the human SIRP alpha prominent variant BIT (Brain Ig like molecule with Tyrosine-based activation motifs, also called SIRP alpha 2 or PTPNS) (2). In mouse, one splice variant lacks aa 147-364, which eliminates the C type Ig domains, while another lacks only aa 425-428 (6). Mouse SIRP alpha ECD shares 61%, 75%, 62%, 61%, and 59% aa sequence identity with human, rat, equine, bovine, and porcine SIRP alpha , respectively, and shares 62% aa identity with mouse SIRP beta 1 (2). SIRP alpha is expressed mainly on myeloid cells, including macrophages, neutrophils, dendritic and Langerhans cells (3 ‑ 7). It is also found on neurons, smooth muscle and endothelial cells (8-10). SIRP alpha shows adhesion to the ubiquitous CD47/IAP (integrin associated protein), while SIRP gamma binds more weakly and SIRP beta 1 does not bind at all (1, 2). Mouse and human SIRP alpha are allelic in nature, and variation(s) in the V-type Ig-like domain likely impacts its binding to CD47 (11). SIRP alpha engagement generally produces a negative regulatory signal (4). Low SIRP alpha recognition of CD47, which occurs on aged erythrocytes or platelets or xenogenic cells, promotes clearance of CD47low cells from circulation (12 ‑ 14). SIRP alpha recognition of surfactants SP‑A and SP‑D in the lung can inhibit alveolar macrophage cytokine production (15). The CD47 integrin-SIRP alpha interaction is reported to promote macrophage fusion during osteoclastogenesis (16).

  1. Barclay, A.N. (2009) Curr. Opin. Immunol. 21:47.
  2. van Beek, E.M. et al. (2005) J. Immunol. 175:7781.
  3. Liu, Y. et al. (2005) J. Biol. Chem. 280:36132.
  4. Sano, S-I. et al. (1999) Biochem. J. 344:667.
  5. Lee, W.Y. et al. (2010) J. Biol. Chem. 285:37953.
  6. Swissprot Accession # P97797.
  7. Miyashita, M. et al. (2004) Mol. Biol. Cell 15:3950.
  8. Wang, X.X. & K.H. Pfenninger (2005) J. Cell Sci. 119:172.
  9. Maile, L.A. et al. (2003) Mol. Biol. Cell 14:3519.
  10. Johansen, M.L. & E.J. Brown (2007) J. Biol. Chem. 282:24219.
  11. Takenaka, K. et al. (2007) Nat. Immunol. 8:1313.
  12. Ishikawa-Sekigami, T. et al. (2006) Biochem. Biophys. Res. Commun. 343:1197.
  13. Olsson, M. et al. (2005) Blood 105:3577.
  14. Ide, K. et al. (2007) Proc. Natl. Acad. Sci. USA 104:5062.
  15. Gardai, S.J. et al. (2003) Cell 115:13.
  16. Lundberg, P. et al. (2007) Biochem. Biophys. Res. Commun. 352:444.

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Publications for SIRP alpha/CD172a (7154-SA)(1)

We have publications tested in 1 confirmed species: Mouse.

We have publications tested in 1 application: Cell Culture.


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Bioinformatics

Gene Symbol Sirpa
Uniprot