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This gene, ZNF683, which is located on chromosome 1, is predicted to encode a zinc finger protein, currently with unknown fucntion.

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ZFP42 is a transcription factors and a specific marker of undifferentiated embryonic stem (ES) cells.

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EBI3 Antibody: EBI3 is a subunit in two distinct heterodimeric cytokines: interleukin-27 (IL-27) and IL-35. Like interleukin-23 (IL-23), IL-27 is a recently discovered member of the IL-6/IL-12 family of proinflammatory and immunoregulatory cytokines. It exists as a heterodimer composed of the p40-related protein EBI3 and an IL-12 p35-related protein termed p28. IL-27 is produced after activation by antigen-presenting cells and induces proliferation of naïve but not memory CD4+ T-cells. It acts by binding to its receptor WSX-1 (also known as TCCR) and gp130 which results in the activation of a Jak/STAT signaling cascade, suggesting the IL-27 is involved in the regulation of immune processes. It has been suggested that IL-27 can also be used as a therapeutic agent against cancer as it can also induce tumor-specific anti-tumor activity mediated through CD8+ T-cells, IFN-gamma, and T-bet. IL-35 is composed of EBI3 and the p35 subunit of IL-12 and has been reported to have therapeutic effects against collagen-induced arthritis by expanding the population of regulatory T cells and suppressing Th17 cells. At least two isoform of EBI3 are known to exist.

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IL-16 Antibody: IL-16 was initially identified as a chemotactic cytokine, but is now known to possess a wide range of activities. Later studies have more fully characterized IL-16 as an immunomodulatory cytokine that contributes to the regulatory process of CD4+ T cell recruitment and activation at sites of inflammation in association with asthma and several autoimmune diseases. The precursor of IL-16 (pro-IL-16) is thought to be cleaved towards the C-terminal region by Caspase-3, releasing a 20 kDa active form that binds to and signals through CD4. Besides acting as a chemotactic cytokine, IL-16 is thought to also be involved in the regulation of T cell proliferation and multiple infectious, immune-mediated, and autoimmune inflammatory disorders including irritable bowel syndrome, systemic lupus erythematosus, and neurodegenerative disorders. At least two isoforms of IL-16 are known to exist; the longer isoform (also known as NIL-16) is detected only in neurons of the cerebellum and hippocampus.

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EBI3 Antibody: EBI3 is a subunit in two distinct heterodimeric cytokines: interleukin-27 (IL-27) and IL-35. Like interleukin-23 (IL-23), IL-27 is a recently discovered member of the IL-6/IL-12 family of proinflammatory and immunoregulatory cytokines. It exists as a heterodimer composed of the p40-related protein EBI3 and an IL-12 p35-related protein termed p28. IL-27 is produced after activation by antigen-presenting cells and induces proliferation of naïve but not memory CD4+ T-cells. It acts by binding to its receptor WSX-1 (also known as TCCR) and gp130 which results in the activation of a Jak/STAT signaling cascade, suggesting the IL-27 is involved in the regulation of immune processes. It has been suggested that IL-27 can also be used as a therapeutic agent against cancer as it can also induce tumor-specific anti-tumor activity mediated through CD8+ T-cells, IFN-gamma, and T-bet. IL-35 is composed of EBI3 and the p35 subunit of IL-12 and has been reported to have therapeutic effects against collagen-induced arthritis by expanding the population of regulatory T cells and suppressing Th17 cells. At least two isoform of EBI3 are known to exist.

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PRICKLE2 Antibody: PRICKLE2, also known as Pk2 or EPM5, is a member of a highly conserved protein family that function in the noncanonical WNT signaling pathway which regulates intracellular calcium release and planar cell polarity. Both PRICKLE2 and the related protein PRICKLE1 are expressed in postmitotic neurons and promote neurite outgrowth, and both proteins promote neurite outgrowth via the Dishevelled dependent pathway in C1300 cells. PRICKLE2 localizes to the postsynaptic density and interacts with PSD-95 and NMDA receptors. Defects in the gene encoding PRICKLE2 are associated with autosomal recessive progressive myoclonic epilepsy.

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SDF2 is believed to be a secretory protein. It has regions of similarity to hydrophilic segments of yeast mannosyltransferases. Its expression is ubiquitous and the gene appears to be relatively conserved among mammals. The protein encoded by this gene is believed to be a secretory protein. It has regions of similarity to hydrophilic segments of yeast mannosyltransferases. Its expression is ubiquitous and the gene appears to be relatively conserved among mammals.

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Caspase-12 Antibody: (Large)Three distinct signaling pathways lead to programmed cell death (apoptosis). The death receptor and mitochondrion pathways are the main, in which the key apoptotic proteases capase-8 and caspase-9, respectively, are involved. The endoplasmic reticulum (ER) stress is the third apoptotic pathway and caspase-12 is involved. Caspase-12 is localized to the ER but not to cytoplasm or mitochondrion. Caspase-12 is activated by ER stress, including disruption of ER calcium homeostasis, and mediates ER stress-induced apoptosis. Caspase-12 is co-localized to the ER with several proteins that are involved in Alzheimer's disease including gamma-secretase presenilin and beta-amyloid precursor protein (APP). Caspase-12 mediates cytotoxicity induced by amyloid-beta. Caspase-12 is ubiquitously expressed in mouse tissues.

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SARS Spike Antibody: A novel coronavirus has recently been identified as the causative agent of SARS (Severe Acute Respiratory Syndrome). Coronaviruses are a major cause of upper respiratory diseases in humans. The genomes of these viruses are positive-stranded RNA approximately 27-31kb in length. SARS infection can be mediated by the binding of the viral spike protein, a glycosylated 139 kDa protein and the major surface antigen of the virus, to the angiotensin-converting enzyme 2 (ACE2) on target cells. This binding can be blocked by a soluble form of ACE2.

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APP is a cell surface receptor and transmembrane precursor protein that is cleaved by secretases to form a number of peptides. Some of these peptides are secreted and can bind to the acetyltransferase complex APBB1/TIP60 to promote transcriptional activation, while others form the protein basis of the amyloid plaques found in the brains of patients with Alzheimer disease. Mutations in this gene have been implicated in autosomal dominant Alzheimer disease and cerebroarterial amyloidosis (cerebral amyloid angiopathy). Multiple transcript variants encoding several different isoforms have been found for this gene.This gene encodes a cell surface receptor and transmembrane precursor protein that is cleaved by secretases to form a number of peptides. Some of these peptides are secreted and can bind to the acetyltransferase complex APBB1/TIP60 to promote transcriptional activation, while others form the protein basis of the amyloid plaques found in the brains of patients with Alzheimer disease. Mutations in this gene have been implicated in autosomal dominant Alzheimer disease and cerebroarterial amyloidosis (cerebral amyloid angiopathy). Multiple transcript variants encoding several different isoforms have been found for this gene.

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SCO2 peptide is used for blocking the activity of SCO2 antibody.

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Interleukin 6 (IL-6) is a pleiotropic alpha-helical cytokine that plays important roles in acute phase reactions, inflammation, hematopoiesis, bone metabolism and cancer progression. IL-6 activity is essential for the transition from acute inflammation to either acquired immunity or chronic inflammatory disease. It is secreted by multiple cell types as a 22kDa-28kDa phosphorylated and variably glycosylated molecule. IL-6 induces signallling through a cell surface heterodimeric receptor complex composed of a ligand binding subunit (IL-6R) and a signal transducing subunit (gp130). IL-6 is a key factor for the growth of plasma cells.

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Anti-EPB41L5 Goat Polyclonal Antibody

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IL-6 is reported to be produced by fibroblasts, activated T cells, activated monocytes or macrophages and endothelial cells. It acts upon a variety of cells including fibroblasts, myeloid progenitor cells, T cells, B cells and hepatocytes. In addition, IL-6 appears to interact with IL2 in the proliferation of T lymphocytes. IL-6 potentiates the proliferative effect of IL-3 on multipotential hematopoietic progenitors. IL-6 is a multifunctional 24 kDa protein originally discovered in the medium of RNA stimulated fibroblastoid cells. It is upregulated by IL1, TNF, PDGF, IFN beta, TNF alpha, NGF, IL17 and downregulated by glucocorticoids IL4, TGF beta. IL-6 appears to be directly involved in the responses that occur after infection and cellular injury, and it may prove to be as important as IL1 and TNF alpha in regulating the acute phase response. IL6 has also been implicated in regulating adipose mass.

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Interleukin 5 (IL-5) is a cytokine produced primarily by activated T lymphocytes. It exists as an antiparallel disulfide linked homodimeric glycoprotein with 115 amino acid residues in each chain. Known also as EDF (eosinophil differentiating factor), functions predominantly as an eosinophilopoietic factor. Analysis of its crystal structure reveals a novel two domain structure, with each domain showing significant homology to the cytokine fold in GMCSF, MCSF, IL-2, IL-4 and growth hormone. Human and mouse IL-5 have 70% amino acid sequence homology.

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GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the gaba/benzodiazepine receptor and opening an integral chloride channel.

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GLI1 is a protein which is a member of the Kruppel family of zinc finger proteins. The function of this gene has not been determined; however, it may play a role in normal development gene transcription. Mouse mutation studies indicate possible involvement in human foregut malformation.

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The function remains unknown.

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FUT6 is a Golgi stack membrane protein that is involved in the creation of sialyl-Lewis X, an E-selectin ligand. Mutations in this gene are a cause of fucosyltransferase-6 deficiency. The protein encoded by this gene is a Golgi stack membrane protein that is involved in the creation of sialyl-Lewis X, an E-selectin ligand. Mutations in this gene are a cause of fucosyltransferase-6 deficiency. Two transcript variants encoding the same protein have been found for this gene.

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ACRP30 was identified as a novel adipocyte-specific synthesized and secreted protein with structural resemblance to complement factor C1q. Like adipsin, ACRP30 secretion is induced ~10-fold during adipocyte differentiation. Plasma levels are reduced in obese humans, and low levels are associated with insulin-resistance. Treatment of db/db mice with TZD increased ACRP30 levels.

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Acyl-Protein Thioesterase 2 is a cytoplasmic protein that belongs to the AB Hydrolase 2 family. LYPLA2 is a lysophospholipase and hydrolyses fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS. LYPLA2 has hydrolase activity that converts Palmitoyl-protein to palmitate and protein. LYPLA2 regulates the multifunctional lysophospholipids by acting on biological membranes. LYPLA2 participates in Glycerophospholipid metabolism pathway, fatty acid metabolic process and lipid metabolic process.

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Valosin-Containing Protein (VCP) is a nuclear protein that belongs to the AAA ATPase family. VCP is a putative ATP-binding protein involved in vesicle transport and fusion, 26S proteasome function, and assembly of peroxisomes. It is necessary for the fragmentation of Golgi stacks during mitosis and their reassembly after mitosis. VCP has been implicated in a number of cellular events that are regulated during mitosis, including homotypic membrane fusion, spindle pole body function, and ubiquitin-dependent protein degradation. VCP participates in the formation of the transitional endoplasmic reticulum (tER) and regulates E3 ubiquitin-protein ligase activity of RNF19A.

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IRF2 encodes interferon regulatory factor 2, a member of the interferon regulatory transcription factor (IRF) family. IRF2 competitively inhibits the IRF1-mediated transcriptional activation of interferons alpha and beta, and presumably other genes that employ IRF1 for transcription activation. However, IRF2 also functions as a transcriptional activator of histone H4.

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DEK was first identified in a fusion with the CAN nucleoporin protein in a specific subtype of acute myelogenous leukemia. DEK has also been shown to be an autoantigen in patients with pauciarticular onset juvenile rheumatoid arthritis. Further, the last 65 amino acids of DEK can partially reverse the mutation-prone phenotype of cells from patients with ataxia-telangiectasia

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Anti-PKP2 Goat Polyclonal Antibody

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Anti-LAMA5 Goat Polyclonal Antibody

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Anti-PRDM14 Goat Polyclonal Antibody

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ETS1 Protein (ETS1) is a nuclear protein that belongs to the ETS family. Members of this family recognize the core consensus DNA sequence GGAA/T in target genes. Proteins function either as transcriptional activators or repressors of numerous genes. They are involved in stem cell development, cell senescence and death, and tumorigenesis. ETS1 is a transcription factor, containing one ETS DNA-binding domain and one PNT (pointed) domain. it has been shown to interact with TTRAP, UBE2I and Death Associated Protein 6.

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Interleukin-35 is a newest and potent suppressive cytokine of the IL-12 family. Unlike other members of the IL-12 family which are produced mainly by antigen-presenting cells (APCs), IL-35 has been identified as a potentially immunosuppressive cytokine primarily produced by regulatory T (Treg) cells, and to a lesser extent by activated dendritic cells and macrophages. IL-35 is composed of the IL-12 p35 subunit and the IL-27 Epstein–Barr virus-induced protein 3 (EBI3) subunit. IL-35 plays an important role in many disease models and has been recently shown to have additional functions aside from inhibition of proliferation, including inducing its own expression in non-Treg cells.

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CD274, also known as B7-H1 or programmed death ligand 1 (PD-L1), is a 40 kD type I transmembrane protein and a member of the B7 family within the immunoglobulin receptor superfamily. Programmed death-1 ligand-1 (PD-L1, CD274, B7-H1) has been identified as the ligand for the immunoinhibitory receptor programmed death-1(PD1/PDCD1) and has been demonstrated to play a role in the regulation of immune responses and peripheral tolerance. By binding to PD1 on activated T-cells and B-cells, PD-L1 may inhibit ongoing T-cell responses by inducing apoptosis and arresting cell-cycle progression. Accordingly, it leads to growth of immunogenic tumour growth by increasing apoptosis of antigen specific T cells and may contribute to immune evasion by cancers. PD-L1 thus is regarded as promising therapeutic target for human autoimmune disease and malignant cancers.