Mouse PIR-B Antibody

Catalog # Availability Size / Price Qty
AF2754
AF2754-SP
Product Details
Citations (5)
FAQs
Supplemental Products
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Mouse PIR-B Antibody Summary

Species Reactivity
Mouse
Specificity
Detects mouse PIR-B in direct ELISAs and Western blots. In direct ELISAs, less than 40% cross-reactivity with recombinant mouse PIR-A is observed.
Source
Polyclonal Goat IgG
Purification
Antigen Affinity-purified
Immunogen
Mouse myeloma cell line NS0-derived recombinant mouse PIR-B
Gly24-Gly635
Accession # AAH26937
Formulation
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.
Label
Unconjugated

Applications

Recommended Concentration
Sample
Western Blot
0.1 µg/mL
Recombinant Mouse PIR-B

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

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Preparation and Storage

Reconstitution
Reconstitute at 0.2 mg/mL in sterile PBS.
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Shipping
Lyophilized product is shipped at ambient temperature. Liquid small pack size (-SP) is shipped with polar packs. Upon receipt, store immediately at the temperature recommended below.
Stability & 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.
  • 6 months, -20 to -70 °C under sterile conditions after reconstitution.

Background: PIR-B

Mouse PIR-B is a 125 kDa type I transmembrane glycoprotein with six Ig-like domains in its extracellular domain (ECD) and four ITIM-like sequences in its cytoplasmic domain. The ECD of PIR-B is highly homologous to the ECDs of multiple mouse PIR-A receptors (92‑99% amino acid sequence homology), which have short cytoplasmic tails lacking ITIM motifs. PIR-A receptors have a charged residue in their transmembrane domain that facilitates interaction with ITAM-containing adaptor molecules. Whereas PIR-A receptors deliver activation signals, PIR-B can inhibit receptor-mediated activation signaling. PIR-A and PIR-B have been shown to bind various mouse MHC class I molecules. They have been proposed to be orthologs of human leukocyte immunoglobulin-like receptors.

Long Name
Paired-Ig-like Receptor B
Entrez Gene IDs
18733 (Mouse); 65146 (Rat)
Alternate Names
CD85a; HL9; ILT5; ILT-5; leukocyte immunoglobulin like receptor B3; LILRA6; LILRB3; LIR3; LIR-3; PIRB; PIR-B

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Citations for Mouse PIR-B Antibody

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

5 Citations: Showing 1 - 5
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  1. The p75 receptor mediates axon growth inhibition through an association with PIR-B
    Authors: Y Fujita, R Takashima, S Endo, T Takai, T Yamashita
    Cell Death & Disease
  2. Involvement of Paired Immunoglobulin-Like Receptor B in Cognitive Dysfunction Through Hippocampal-Dependent Synaptic Plasticity Impairments in Mice Subjected to Chronic Sleep Restriction
    Authors: Xuying Li, Qian Zhai, Xingchun Gou, Minxue Quan, Yansong Li, Xiaohua Zhang et al.
    Molecular Neurobiology
  3. Endoplasmic Protein Nogo-B (RTN4-B) Interacts with GRAMD4 and Regulates TLR9-Mediated Innate Immune Responses.
    Authors: Kimura T, Endo S, Inui M, Saitoh S, Miyake K, Takai T
    J Immunol, 2015-04-27;194(11):5426-36.
    Species: Mouse
    Sample Types: Cell Lysates
    Applications: Western Blot
  4. Oligodendrocyte-myelin glycoprotein and Nogo negatively regulate activity-dependent synaptic plasticity.
    Authors: Raiker SJ, Lee H, Baldwin KT
    J. Neurosci., 2010-09-15;30(37):12432-45.
    Species: Mouse
    Sample Types: Cell Lysates
    Applications: Western Blot
  5. LOTUS suppresses amyloid beta -induced dendritic spine elimination through the blockade of amyloid beta binding to PirB
    Authors: Yuki Kawaguchi, Junpei Matsubayashi, Yutaka Kawakami, Ryohei Nishida, Yuji Kurihara, Kohtaro Takei
    Molecular Medicine

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