Recombinant Human PILR-beta Fc Chimera Avi-tag Protein, CF Summary
|Human PILR- beta |
Accession # Q9UKJ0.1
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CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.|
|Reconstitution||Reconstitute at 500 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
When Recombinant Human CL-P1/COLEC12 (2690-CL) is immobilized at 2 μg/mL, 100 μg/mL, Biotinylated Recombinant Human PILR‑ beta Fc Chimera Avi-tag (Catalog # AVI9828) binds with an ED50 of 0.600-6.00 μg/mL.
2 μg/lane of Recombinant Human PILR-beta Fc Chimera Avi-tag Protein (Catalog # AVI9828) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 55-68 kDa.
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 immunoreceptor PILR-alpha, forming a set of paired immune regulatory receptors responsible for regulating inflammatory responses (1). Mature human PILR-beta contains a V-type Ig-like extracellular domain (ECD) with a siglec-like fold, a single transmembrane domain, and a truncated cytoplasmic tail (2, 3). The transmembrane 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% aa sequence identity with the ECD of mouse PILR-beta. 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, such as 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). Our Avi-tag Biotinylated PILR-beta features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.
- Wilson, M.D. et al. (2006) Physiol. Genomics 27:201.
- Shiratori, I. et al. (2004) J. Exp. Med. 199:525.
- Lu, Q. et al. (2014) PNAS 111:8221.
- Tato, C.M. et al. (2012) PLoS One 7:e31690.
- Banerjee, A. et al. (2010) Infect. Immun. 78:1353.
- Tabata, S. et al. (2008) J. Biol. Chem. 283:8893.
- Mousseau, D.D. et al. (2000) J. Biol. Chem. 275:4467
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