Recombinant Human PILR-beta His-tag Protein, CF

2 μg/lane of Recombinant Human PILR-beta His-tag Protein (Catalog # 10319-PR) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing a band at 30-40 kDa under reducing and non-reducing conditions.

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

Recombinant Human PILR-beta His-tag Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Human CL-P1/COLEC12 (Catalog # 2690-CL) is immobilized at 2 μg/mL (100 μL/well), it binds Recombinant Human PILR‑ beta (Catalog # 10319-PR) with an ED₅₀ of 1-10 μg/mL
• Source: Human embryonic kidney cell, HEK293-derived human PILR-beta protein
  Gln20-Ala189, with a C-terminal 6-His tag
• Accession #: Q9UKJ0.1
• N-terminal Sequence: Gln20, as confirmed by mass spectrometry
• 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: 20 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: 30-40 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, -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after opening.
  • 3 months, -20 to -70 °C under sterile conditions after opening.
• Buffer: Supplied as a 0.2 μm filtered solution in PBS.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human PILR-beta His-tag Protein, CF

• activating receptor PILRbeta
• Activating receptor PILR-beta
• Cell surface receptor FDFACT
• cell surface receptor FDFACT1
• cell surface receptor FDFACT2
• FDFACT
• FDFACT1
• FDFACT2
• paired immunoglobin-like receptor beta
• paired immunoglobin-like type 2 receptor beta
• paired immunoglobulin-like receptor beta
• paired immunoglobulin-like type 2 receptor beta
• PILRB
• PILRbeta
• PILR-beta

Background

Paired immunoglobulin-like type 2 receptor beta (PILR-beta ) is a type I transmembrane (TM) glycoprotein that belongs to the Ig superfamily (1). PILR-beta is the activating counterpart to the inhibitory receptor immunoreceptor PILR-alpha which contains a tyrosine-based inhibitory motif (ITIM) (1). Mature human PILR-beta contains a V‑type Ig‑like extracellular domain (ECD) with a siglec-like fold, a single TM domain, and a truncated cytoplasmic tail (2, 3). The TM domain of PILR-beta contains a positively‑charged residue which interacts with immunoreceptor tyrosine-based activation (ITAM)-bearing adaptor molecules (2). The ECD of mature human PILR-beta shares 40% amino acid sequence identity with its mouse counterpart. PILR-beta is expressed on myeloid cells, such as natural killer, macrophage, and dendritic cells, as well as resident cells of the central nervous system, including microglial cells (2, 4). It is a binding partner for DAP12 and CD99 and has been shown to play an important role in innate immunity and inflammation (4-6). The PILR-alpha / beta pair have also been shown to regulate cell signaling via association with SHP-1 (7). Experiments studying the effects of S. aureus and T. gondii infections in mice have shown that up-regulation of PILR-beta led to significantly lower survival rates while knock-down of PILR-beta or activation of PILR-alpha resulted in significantly less inflammation and increased pathogen clearance (4, 5).

1. Wilson, M.D. et al. (2006) Physiol. Genomics 27:201.
2. Shiratori, I. et al. (2004) J. Exp. Med. 199:525.
3. Lu, Q. et al. (2014) PNAS 111:8221.
4. Tato, C.M. et al. (2012) PLoS One 7:e31690.
5. Banerjee, A. et al. (2010) Infect. Immun. 78:1353.
6. Tabata, S. et al. (2008) J. Biol. Chem. 283:8893.
7. Mousseau, D.D. et al. (2000) J. Biol. Chem. 275:4467.

Bioinformatics

• Uniprot:
  • Q9UKJ0.1()