Recombinant Human PILR-beta Fc Chimera Avi-tag Protein, CF Summary
Additional Information |
Biotinylated |
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 μg/mL, Biotinylated Recombinant Human PILR‑ beta Fc Chimera Avi-tag binds with an ED 50 of 0.600-6.00 μg/mL. |
Source |
Chinese Hamster Ovary cell line, CHO-derived human PILR-beta protein Human PILR- beta (Gln20-Ala189) Accession # Q9UKJ0.1 | IEGRMD | Human IgG1 (Pro100-Lys330) | Avi-tag | N-terminus | | | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
Gln20, as confirmed by mass spectrometry. |
Structure / Form |
Biotinylated via Avi-tag. |
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 |
48 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 |
55-68 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 Human PILR-beta Fc Chimera Avi-tag Protein, CF
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 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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