Primary Antibodies

<p>Glycogen Synthase Kinase 3 beta (GSK3β) is a multifunctional serine/threonine kinase widely expressed in most mammalian cells. GSK3β is highly active under basal conditions and acts downstream of phosphoinositide 3-kinase (PI3K) signalling. PI3K activation results in Akt phosphorylation and the subsequent phosphorylation of GSK3β at serine-9 and its inactivation. GSK3β in turn activates the production of pro-inflammatory cytokines including IL-1β, IL-6, IL-12, IL-17, TNFα and IFNγ, and supresses the production of IL-10, IL-1Ra, and IFNβ by immune cells.</p>

<p>JAK3</p>

<p>Ligand binding to type I receptors with a common subunit gamma result in local cytoplasmic Jak3 being recruited to the cytoplasmic tails of the receptor. The tail becomes phosphorylated creating STAT protein binding sites. The STAT complex then also becomes phosphorylated to form a homo/heterodimer and translocate to the nucleus to bind to DNA to activate transcription. For example, interleukin IL2 binds type I receptor ILR2 resulting in Jak1 with Jak3 recruitment to the cytoplasmic gamma subunit. This interaction leads to tyrosine phosphorylation of the receptor for Stat5A with Stat5B docking. These STATs are then phosphorylated and activated by Jak1 and Jak3 leading to their dimerization and translocation for activation of specific gene transcription.Jak3 also has vital roles in immune cell signalling pathways; IL2 binds IL2R on T cells and natural killer cells. It has been found that in these immune cells Jak3 is critical to facilitate tyrosine phosphorylation of the cytoplasmic IL2R subunit. Throughout T cell differentiation Jak3 is required for IL7 induced activation of IL7R to activate PI3k and STATs. Ablation of Jak3 completely halted T cell proliferation.  JAK3-deficient models have phenotypes like human severe combined immunodeficiency (SCID), due to the lack of developed lymphocytes. This was linked to the interaction found between Jak3 and the T cell protein tyrosine phosphatases (TCPTP) key to cytokine signalling in haematopoietic cells.</p>

<p>GPRC5B</p>

<p>Anti-Per3 antibody</p>

<p>Anti-Mgll antibody</p>

<p>Ligand binding to type I receptors with a common subunit gamma result in local cytoplasmic Jak3 being recruited to the cytoplasmic tails of the receptor. The tail becomes phosphorylated creating STAT protein binding sites. The STAT complex then also becomes phosphorylated to form a homo/heterodimer and translocate to the nucleus to bind to DNA to activate transcription. For example, interleukin IL2 binds type I receptor ILR2 resulting in Jak1 with Jak3 recruitment to the cytoplasmic gamma subunit. This interaction leads to tyrosine phosphorylation of the receptor for Stat5A with Stat5B docking. These STATs are then phosphorylated and activated by Jak1 and Jak3 leading to their dimerization and translocation for activation of specific gene transcription.Jak3 also has vital roles in immune cell signalling pathways; IL2 binds IL2R on T cells and natural killer cells. It has been found that in these immune cells Jak3 is critical to facilitate tyrosine phosphorylation of the cytoplasmic IL2R subunit. Throughout T cell differentiation Jak3 is required for IL7 induced activation of IL7R to activate PI3k and STATs. Ablation of Jak3 completely halted T cell proliferation.  JAK3-deficient models have phenotypes like human severe combined immunodeficiency (SCID), due to the lack of developed lymphocytes. This was linked to the interaction found between Jak3 and the T cell protein tyrosine phosphatases (TCPTP) key to cytokine signalling in haematopoietic cells.</p>

<p>Together with IL12B, IL23A forms part of the heterodimeric cytokine IL-23 which functions in innate and adaptive immunity. IL-23 is a member of the IL-12 family of cytokines that includes IL-12, IL-35, IL-27, and IL-39. IL-23 binds to a heterodimeric receptor complex composed of IL12RB1 and IL23R and activates the Jak-Stat signaling cascade. IL-23 is a key driver of Th17-mediated immune response during infection and inflammation and its over production is involved in several cancers.</p>

<p>Anti-PYY antibody</p>

<p>Anti-MINK1 antibody</p>

<p>N-methyl-D-aspartate receptors (NMDARs) are ligand-gated ionotropic glutamate receptors that mediate excitatory synaptic transmission and are important for many aspects of nervous system function including: synaptic plasticity; learning and memory; neuronal development and circuit formation. NMDARs have also been implicated in various neuronal disorders. NMDARs are heteromers consisting of an obligate NR1 and most commonly one or two kinds of NR2 subunits or occasionally NR3 subunits.NR2B is the predominant subunit found in the postnatal brain, however over time NRA2 levels increase and eventually outnumber NR2B subunits in a process known as the NR2B-NR2A developmental switch. The greater ratios of the NR2B subunit in post-natal brains leads to NMDA receptors which remain open longer compared to those with more NR2A subunits, and may be related to the greater memory abilities in the immediate postnatal period compared to late in life. The phosphorylation of NR2B is closely linked to its transport and the phosphorylation of NR2B at Ser1303 is an initial step of NMDA €induced excitotoxicity. NR2B is phosphorylated at Ser1303 by protein kinase C (PKC) and is dephosphorylated by protein phosphatase 1 (PP1). The involvement of NMDAR in the central nervous system (CNS) has become a focus area for neurodegenerative diseases such as Alzheimer's disease, epilepsy and ischemic neuronal cell death.</p>

<p>Anti-KCNK18/TRESK antibody</p>

<p>GPRC5B</p>

<p>Anti-SCN9A/Nav1.7 antibody</p>

Nuclear lamin proteins (lamin A, B and C) form a complex structural scaffold, called the nuclear lamina, which is associated with the inside of the nuclear envelope. Lamins bind to a huge number of nuclear protein complexes and are involved in several processes, including chromatin organisation, gene regulation, genome stability, nuclear and cytoskeletal organisation, mechanical stability, differentiation, and tissue-specific functions. Mutations in lamin proteins result in laminopathies such as muscular dystrophy and the accelerated aging condition, Hutchinson-Gilford progeria. This antibody recognises human lamin A and C in both Western blots and immunohistochemistry with a strong signal and low background noise, and has an AF488 dye conjugated to it. AF488 is a popular, bright green, PH-stable fluorescent dye.

<p>Timely chromosome segregation during mitosis and meiosis is orchestrated by separase activity cleaving the multi-subunit cohesin complex from the centromere. Sister chromosomes remain attached at the centromere till after meiosis I anaphase due to shugoshins protecting cohesin from separase activity. Recent work shows shugoshin's role is to interact with PP2A and maintaining cohesin in a dephosphorylated state thus protecting the centromeric RecB protein from separase activity.<br>In mammals, there are 2 known sugoshins paralogues, Sgo1 and Sgo2. Sgo1 appears to play the primary role in cohesin protection during mitosis when most cohesin complex dissociates from the chromosome arms. Whereas Sgo2 aids centromeric cohesion during meiosis. Reduced levels of Sgo1 have been associated with colorectal cancers due to the increased chromosomal instability leading to tumourigenesis. Defective Sgo1 has also been linked to aneuploidy. This KLH conjugated Sgo1 antibody is the ideal research tool to investigate the functions of shugoshins as there is still much to uncover.</p>

<p>The pluripotency-associated master transcriptional regulator SOX2 is essential during mammalian embryogenesis, embryonic stem cell maintenance and later in life, however SOX2 expression can also be highly detrimental. SOX2 has been shown to be expressed in at least 25 different cancers, consequently, too little or too much SOX2 can dramatically alter tumour growth. SOX2 is therefore tightly regulated at the transcriptional level, by microRNAs, long non-coding RNAs, and post-translational modifications.</p>

<p>ROBO2</p>

<p>Cystatin-C</p>

<p>Anti-VMP1 antibody</p>