Recombinant Mouse SIRP beta 1a His-tag Protein, CF

When Recombinant Mouse SIRP beta 1a His-tag (Catalog # 10289-SB) is immobilized at 1 μg/mL (100 μL/well), Recombinant Human SP‑D (Catalog # 1920-SP) binds with an ED50 of 30-180 ng/mL.

2 μg/lane of Recombinant Mouse SIRP beta 1a His-tag was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 48-62 kDa.

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

Recombinant Mouse SIRP beta 1a His-tag Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Mouse SIRP beta 1a His-tag (Catalog # 10289-SB) is immobilized at 1 µg/mL (100 µL/well), Recombinant Human SP‑D (Catalog # 1920-SP) binds with an ED₅₀ of 30-180 ng/mL.
• Source: Mouse myeloma cell line, NS0-derived mouse SIRP beta 1a protein
  Val28-Gly360, with a C-teminal 6-His tag
• Accession #: NP001002898
• N-terminal Sequence: Val28
• 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: 48-62 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.
• 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 Mouse SIRP beta 1a His-tag Protein, CF

• SIRP beta 1a
• SIRPB1A

Background

Signal-regulatory protein beta 1a (SIRP beta 1a) 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. 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). Mouse SIRP beta 1a shares 57% and 59% amino acid sequence identity with human SIRP beta 1 and rat SIRP alpha, respectively. 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).

1. vanBeek, E.M. et al. (2005) J. Immunol. 175:7781.
2. van den Berg, T. et al. (2008) Trends in Immunology 29:203.
3. Liu, Y. et al. (2005) Journal of Biological Chemistry 280:36132.
4. Matozaki, T. et al. (2009) Trends in Cell Biology 19:72.
5. Dietrich, J. et al. (2000) J Immunol. 164:9.
6. Brook, G. et al. (2004) J. Immunol. 173:2562.
7. Hayashi, A. et al. (2004) J Biol Chem. 279:29450.
8. Fournier, B. et al. (2012) J. Biol. Chem. 287:19386.
9. Seiffert, M. et al. (2001) Blood 97:2741.

Bioinformatics

• Uniprot:
  • NP001002898()