Recombinant Human SIRP alpha/CD172a Fc Biotin Protein, CF

2 μg/lane of Biotinylated Recombinant Human SIRP alpha /CD172a Fc Chimera (Catalog # BT4546B) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 70-105 kDa and 140-210 kDa, respectively.

When Recombinant Human CD47 Fc Chimera (Catalog # 4670-CD) is coated at 0.1 μg/mL, Biotinylated Recombinant Human SIRP alpha/CD172a Fc Chimera (Catalog # BT4546B) binds with an ED50 of 6-48 ng/mL.

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

Recombinant Human SIRP alpha/CD172a Fc Biotin Protein, CF Summary

• Additional Information: Biotinylated via amines
• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Human CD47 Fc Chimera (Catalog # 4670-CD) is immobilized at 0.1 µg/mL (100 µL/well), Biotinylated Recombinant SIRP alpha /CD172a Fc Chimera (Catalog # BT4546B) binds with an ED₅₀ of 6-48 ng/mL.
• Source: Chinese Hamster Ovary cell line, CHO-derived human SIRP alpha/CD172a protein
  

  Human SIRP alpha /CD172a (Gly27-Arg370) & (Glu31-Arg370) Accession # NP_542970	IEGRMD	Human IgG1 (Pro100-Lys330)
  N-terminus		C-terminus

• Accession #: NP_542970
• N-terminal Sequence: Gly27 & Glu31
• Structure / Form: Disulfide-linked homodimer. Biotinylated via amines.
• Protein/Peptide Type: Recombinant Proteins
• Purity: >90%, 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 (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: 70-105 kDa, under reducting 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, -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
• Purity: >90%, 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 Human SIRP alpha/CD172a Fc Biotin 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 monomeric ~90 kDa type I transmembrane glycoprotein that belongs to the SIRP/SHPS (CD172) family of the immunoglobulin superfamily (1 - 4). SIRPs are paired receptors, with similar extracellular domains but differing C-termini and functions (1, 2). The 503 amino acid (aa) human SIRP alpha contains a 342 aa extracellular domain (ECD), with one V-type, and two C1 type Ig domains, and three potential N glycosylation sites. It has a 110 aa cytoplasmic sequence with ITIM motifs that recruit tyrosine phosphatases SHP-1 and SHP-2 when phosphorylated (4). Human SIRP alpha has more than 40 described polymorphisms, including the prominent BIT (Brain Ig like molecule with Tyrosine-based activation motifs, also called SIRP alpha ₂ or PTPNS) (5). One reported isoform lacks aa 1 - 101, which eliminates most of the V type Ig domain. Human SIRP alpha ECD shares 61%, 60%, 71%, 72% and 73% aa identity with mouse, rat, porcine, bovine and equine SIRP alpha , respectively; it shares 84% and 76% aa identity with human SIRP beta 1 and SIRP gamma , respectively (2). SIRP alpha is expressed mainly on myeloid cells, including macrophages, neutrophils, dendritic and Langerhans cells (3 - 6). It is also found on neurons, smooth muscle and endothelial cells (7 - 9). SIRP alpha shows adhesion to the ubiquitous CD47/IAP (integrin associated protein), while SIRP gamma binds more weakly and SIRP alpha 1 does not bind at all (1, 2). Mouse and human SIRP alpha -CD47 binding only cross-reacts for specific polymorphisms and influences engraftment of xenotransplanted stem cells (6, 10). 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 CD47^low cells from circulation (11, 13). SIRP alpha recognition of surfactants SP-A and SP-D in the lung can inhibit alveolar macrophage cytokine production (14). The CD47 integrin-SIRP alpha interaction is reported to promote macrophage fusion during osteoclastogenesis (15).

1. Barclay, A.N. & M.H. Brown (2006) Nat. Rev. Immunol. 6:457.
2. vanBeek, E.M. et al. (2005) J. Immunol. 175:7781.
3. Liu, Y. et al. (2005) J. Biol. Chem. 280:36132.
4. Kharitonenkov, A. et al. (1997) Nature 386:181.
5. Swissprot Accession # P78324.
6. Miyashita, M. et al. (2004) Mol. Biol. Cell 15:3950.
7. Wang, X.X. & K.H. Pfenninger (2005) J. Cell Sci. 119:172.
8. Maile, L.A. et al. (2003) Mol. Biol. Cell 14:3519.
9. Johansen, M.L. & E.J. Brown (2007) J. Biol. Chem. 282:24219.
10. Takenaka, K. et al. (2007) Nat. Immunol. 8:1313.
11. Ishikawa-Sekigami, T. et al. (2006) Biochem. Biophys. Res. Commun. 343:1197.
12. Olsson, M. et al. (2005) Blood 105:3577.
13. Ide, K. et al. (2007) Proc. Natl. Acad. Sci. USA 104:5062.
14. Gardai, S.J. et al. (2003) Cell 115:13.
15. Lundberg, P. et al. (2007) Biochem. Biophys. Res. Commun. 352:444.

Bioinformatics

• Uniprot:
  • NP_542970()