Description: True Blue

Description: True Blue

Description: True Blue

Description: True Blue

Description: True Blue

Description: Members of the IRAK (IL-1R-associated kinase)/Pelle family play a major role in IL-1R/TLR mediated inflammatory responses and in innate immunity. IRAK and IRAK-2 regulate the activity of a signaling cascade that mediates the activation of NF-κB and MAP kinase. IRAK-4 interacts with and phosphorylates IRAK, while IRAK-M is thought to inhibit the recruitment and activation of IRAK-4 and IRAK. The importance of the IRAK family in inflammation and immunity is illustrated by the fact that animals lacking IRAK-4 are impaired in their responses to viral and bacterial challenges and are completely resistant to LPS challenge.;;For images please see PDF data sheet

Description: Antigen stimulation of immune cells triggers Ca++ entry through Ca++ release-activated Ca++ (CRAC) channels. The ORAI family is a recently identified set of proteins that are essential components of these CRAC channels. A missense mutation in the ORAI1 protein in humans is the cause of one form of hereditary severe combined immune deficiency (SCID) which results in ablated T-cell Ca++ entry. It has been suggested that ORAI1 functions as a highly selective Ca++ plasma membrane channel that is gated through interactions with the stromal interaction molecule 1 (STIM1), the store-activated endoplasmic reticulum Ca++ sensor. Like ORAI1, ORAI2 also functions as a highly selective Ca++ plasma membrane channel that is gated through interactions with STIM1, although at a lesser efficacy than ORAI1. Although ORAI3 can also function as Ca++ plasma membrane channel, ORAI3 channels failed to produce detectable Ca++ selective currents in cells co-transfected with ORAI3 and STIM1, indicating that ORAI3 channels undergo a lesser degree of depotentiation than ORAI1 or ORAI2. Na+ currents through ORAI1, 2 and 3 channels were equally inhibited by extracellular Ca++, indicating that each have similar affinities for Ca++ within the selectivity filter. STIM1, in its function as a Ca++ sensor and an activator of CRAC channels, migrates to the plasma membrane from endoplasmic reticulum-like sites which act as cellular Ca++ stores. A related molecule, STIM2, inhibits the STIM1-mediated store-operated Ca++ entry, and can form complexes with STIM1, suggesting these two proteins may play a coordinated role in controlling Ca++ entry. The ORAI antibodies are predicted to have no cross-reactivity to the other ORAI proteins. Similarly, the STIM antibodies will not cross-react with the other STIM protein.;;For images please see PDF data sheet

Description: Glutamate receptors are the predominant excitatory neurotransmitter receptors in the mammalian brain and are activated in a variety of normal neurophysiologic processes. Grik1, also known as glutamate receptor 5, belongs to the kainate family of glutamate receptors, which are composed of four subunits and function as ligand-activated ion channels. Grik1 is expressed in GABAergic interneurons of the hippocampus and are thought to participate in the formation of various subtypes of kainate receptors with Grik2 and Grik5/KA2. Stimulation of Grik1 leads to intracellular calcium release and activation of protein kinase C. Excessive activation has been associated with psychiatric, neurological and neurodegenerative diseases. Grik2, also known as glutamate receptor 6, may be associated with autosomal recessive mental retardation and possibly other neurological disorders such as schizophrenia. Numerous isoforms of Grik2 are known to exist and may be subject to RNA editing within the second transmembrane domain, which is thought to alter the properties of ion flow. Grik3, also known as glutamate receptor 7, has recently been shown to be an essential subunit of presynaptic kainate autoreceptors at hippocampal mossy fiber synapses as grik3-null mice show significantly reduced short- and long-term synaptic potentiation. Grik4 codes for the KA1 subunit of kainate-type ionotropic gluatamate receptors; mutations in this gene show significant association with both schizophrenia and bipolar disorder. Grik5, also known as kainate-preferring glutamate receptor subunit KA2, does not form homomeric channels, but instead forms heteromers with Grik2. In Grik2- but not Grik1-null mice, Grik5 surface expression is greatly reduced in neurons, indicating that Grik2/Grik5 heteromers are required for exit from the endoplasmic reticulum to the cell surface. ;;For images please see PDF data sheet

Description: Cell-mediated immune responses are initiated by T lymphocytes that are themselves stimulated by cognate peptides bound to MHC molecules on antigen-presenting cells (APC). T-cell activation is generally self-limited as activated T cells express receptors such as PD-1 (also known as PDCD-1) that mediate inhibitory signals from the APC. PD-1 can bind two different but related ligands, PD-L1 and PD-L2. PD-L1 is a B7-related protein that inhibits cell-mediated immune responses by reducing the secretion of IL-2 and IL-10 from memory T cells. This suggests that PD-L1 may be useful in reducing allogenic CD4+ memory T-cell responses to endothelial cells, thereby reducing the likelihood of host immune responses to allografts.

Description: The lymphocyte activation gene-3 (LAG3) is a member of the immunoglobulin superfamily and binds MHC class II with high affinity (1), negatively regulating T-cell function and homeostasis (2). It is expressed in B, T, and NK cells, monocytes, and dendritic cells (3), and acts to regulate T cell expansion (4). LAG3 is also an important immune checkpoint protein, with anti-LAG3 antibodies activating T effector cells and affecting regulatory T cell functions. Furthermore LAG3 appears to act in a synergistic fashion with PD-1/PD-L1, suggesting that a dual antibody approach may prove useful in cancer immunotherapy.

Description: Serum, Plasma, Culture Media

Description: Liquid Samples

Description: The 4x Detection Buffer is optimized for use with the PRMT5 Homogeneous Assay Kit (BPS Bioscience #52052).

Description: The members of the SAP90/PSD-95-associated protein (SAPAP) family (also known as the DLGAP family) specifically interact with PSD-95/SAP90, a membrane-associated guanylate kinase localized at postsynaptic density (PSD) in neuronal cells. The SAPAP proteins are thought to be adaptor proteins that also interact with different synaptic scaffolding proteins, cytoskeletal and signaling components, such as focal adhesion kinase (FAK) and proline-rich tyrosine kinase 2 (PYK2). SAPAP1, -2 and -4 mRNA are targeted to cell bodies, whereas SAPAP3 mRNA is detected mainly in cell bodies. SAPAP1 protein however, is targeted to the synapse and is not reliant on the synaptic localization of PSD-95 or the synaptic scaffolding molecule (S-SCAM). SAPAP3 protein is targeted to dendrites. Recent experiments have suggested that SAPAP3 may be involved in obsessive-compulsive disorder (OCD), as mice lacking SAPAP3 exhibited OCD-like symptoms which could be relieved by lentiviral-mediated selective expression of SAPAP3 in the striatum of SAPAP3-mutant mice. Multiple isoforms of the SAPAP proteins are known to exist.;;For images please see PDF data sheet