When Recombinant Human SIRP beta 1/CD172b (Catalog # 9978-SB) isimmobilized at 1 µg/mL, Recombinant Human SP‑D (Catalog # 1920-SP) binds with anED50 of 0.1-0.8 μg/mL.
2 μg/lane of Recombinant Human SIRP beta 1/CD172b (Catalog #9978-SB) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR)conditions and visualized by Coomassie® Blue staining, showing bands at 45-61 ...read more
Recombinant Human SIRP beta 1/CD172b Protein, CF Summary
Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human SIRP beta 1/CD172b (Catalog # 9978-SB) is immobilized at 1 µg/mL (100
µL/well),
Recombinant
Human SP‑D (Catalog # 1920-SP)
binds with an ED50 of 0.1-0.8 μg/mL
Source
Human embryonic kidney cell, HEK293-derived human SIRP beta 1/CD172b protein
Human SIRP beta 1/CD172b (Glu30-Ala369) Accession # O00241
HH
Hemagglutinin Tag (YPYDVPDYA)
N-terminus
C-terminus
N-terminal Sequence
Glu30
Structure / Form
Dimer, non covalent
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
Bioactivity
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
45-61 kDa, under reducing conditions
Publications
Read Publication using 9978-SB in the following applications:
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 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 beta 1/CD172b Protein, CF
CD172 antigen-like family member B
CD172b antigen
CD172b
DKFZp686A05192
FLJ26614
signal-regulatory protein beta 1
signal-regulatory protein beta-1
SIRP beta 1
SIRPB1
SIRP-beta-1 isoform 3
SIRP-BETA-1
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. 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. The extracellular domain contains 3 intramolecular disulfide
bonds and one interchain disulfide at Cys320. 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). Human SIRP beta 1 shares a 57% sequence identity with
mouse and rat SIRP beta 1. 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.
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