Recombinant Cynomolgus SIRP beta 1/CD172b His Protein, CF Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. When
Recombinant Cynomolgus Monkey SIRP beta 1/CD172b is immobilized
at 1 μg/mL, 100 μL/well, the concentration of
Recombinant
Human SP-D (Catalog # 1920-SP)
that produces 50% of the optimal binding response is 0.15-0.9 μg/mL. |
Source |
Chinese Hamster Ovary cell line, CHO-derived cynomolgus monkey SIRP beta 1/CD172b protein Glu30-Pro369, with a C-terminal 6-His tag |
Accession # |
|
N-terminal Sequence |
Glu30 |
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 |
53-68 kDa, under reducing 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, -20 to -70 °C under sterile conditions after reconstitution.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
Purity |
>95%, 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 Cynomolgus SIRP beta 1/CD172b His Protein, CF
Background
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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