Reactivity | HuSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Details of Functionality | Measured by its binding ability in a functional ELISA. Recombinant Human CL-P1/COLEC12 (Catalog # 2690-CL) immobilized at 2 μg/mL, 100 μg/mL, can bind to Recombinant Human PILR‑ beta Fc Chimera with an ED50 of 0.12-0.72 μg/mL. |
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Source | Human embryonic kidney cell, HEK293-derived human PILR-beta protein
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Accession # | |||||||
N-terminal Sequence | No results obtained. Gln20 predicted. |
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Structure / Form | Disulfide-linked homodimer |
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Protein/Peptide Type | Recombinant Proteins |
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Purity | >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
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Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 45.7 kDa (monomer). 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 | 57-66 kDa, reducing conditions |
Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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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. |
Paired immunoglobulin-like type 2 receptor beta (PILR-beta ) is a type I transmembrane (TM) glycoprotein belonging to the Ig superfamily. PILR-beta is the activating counterpart to the immunoreceptor tyrosine-based inhibitory motif (ITIM) containing PILR-alpha inhibitory receptor (1). Mature human PILR-beta is a 208 amino acid (aa) protein containing a 172 aa V-type Ig-like extracellular domain (ECD) with a siglec-like fold, a single TM, and a truncated cytoplasmic tail (2, 3). The TM 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 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, 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).
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Uniprot |
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