Recombinant Cynomolgus Monkey SIRP alpha/CD172a Protein, CF Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinant Cynomolgus Monkey SIRP alpha /CD172a
is coated at 2 μg/mL, 100 μL/well,
Recombinant Human CD47 Fc Chimera (Catalog # 4670-CD)
binds with an ED 50 of 10-60 ng/mL. |
Source |
Mouse myeloma cell line, NS0-derived cynomolgus monkey SIRP alpha/CD172a protein Gly27 & Glu31-Arg369, with a C-terminal 6-His tag |
Accession # |
|
N-terminal Sequence |
Gly27, Glu31 |
Protein/Peptide Type |
Recombinant Proteins |
Purity |
>95%, 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 |
|
Theoretical MW |
38 kDa. 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 |
52-67 kDa, reducing conditions |
Packaging, Storage & Formulations
Storage |
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 1 mg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Cynomolgus Monkey SIRP alpha/CD172a Protein, CF
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. Cynomolgous
SIRP alpha ECD shares 88%, 61%, and 61% aa identity with human, mouse, and rat,
SIRP alpha, respectively. 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 CD47low 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).
-
Barclay, A.N. & M.H. Brown (2006) Nat. Rev. Immunol. 6:457.
- vanBeek, E.M. et al. (2005) J. Immunol. 175:7781.
- Liu, Y. et al. (2005) J. Biol. Chem. 280:36132.
- Kharitonenkov, A. et al. (1997) Nature 386:181.
- Swissprot Accession # P7832.
- Miyashita, M. et al. (2004) Mol. Biol. Cell 15:3950.
- Wang, X.X. & K.H. Pfenninger (2005) J. Cell Sci. 119:172.
- Maile, L.A. et al. (2003) Mol. Biol. Cell 14:3519.
- Johansen, M.L. & E.J. Brown (2007) J. Biol. Chem. 282:24219.
- Takenaka, K. et al. (2007) Nat. Immunol. 8:1313.
- Ishikawa-Sekigami, T. et al. (2006) Biochem. Biophys. Res. Commun. 343:1197.
- Olsson, M. et al. (2005) Blood 105:3577.
- Ide, K. et al. (2007) Proc. Natl. Acad. Sci. USA 104:5062.
- Gardai, S.J. et al. (2003) Cell 115:13.
- Lundberg, P. et al. (2007) Biochem. Biophys. Res. Commun. 352:444.
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