14969 Results for: "Sodium+1-hexadecanesulphonate"

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Sprouty-4 (also known as SPRY4) is an inhibitor of the insulin receptor and EGFR-transduced mitogen-activated protein kinase (MAPK) signaling pathway downstream of FGF and EGF receptor tyrosine kinase activation. It is positioned upstream of RAS activation and impairs the formation of active GTP-RAS. SPRY4 is widely expressed, with different isoforms. The protein consists of 322 amino acids, with a cysteine-rich region, Src homology 3 binding regions, proline-rich regions, and a PEST sequence. It is expressed predominantly in the cytoplasm. Northern results show bands across most tissues, with strongest expression in heart, brain, placenta, lung, and intestine.

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Pierce™ Fab preparation kits use immobilised papain protease to digest human or mouse IgG antibodies to make separate Fab and Fc fragments and subsequently to purify the Fab using Protein A agarose.

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TLX3 Antibody: The Hox proteins play a role in patterns of embryonic development and cellular differentiation by regulating downstream target genes. TLX3, also known as homeobox11-like1 (HOX11L2), is a DNA-binding nuclear transcription factor that is expressed in a subset of the primary sensory nervous system. TLX3, along with the related TLX1, is a selector transcription factor that promotes an excitatory glutamatergic neuronal phenotype over an inhibitory GABAergic phenotype opposing LBX1 signals during dorsal spinal cord development. Chromosomal translocations of the TLX3 gene have been shown to result in some forms of T-cell acute lymphoblastic leukemia (T-ALL).

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NF-κ-B is a pleiotropic transcription factor which is present in almost all cell types and is involved in many biological processed such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-κ-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively.

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NF-κ-B is a pleiotropic transcription factor which is present in almost all cell types and is involved in many biological processed such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-κ-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively.

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TRIM33 Antibody: TRIM24 (TIF1alpha), TRIM28 (TIF1beta), and TRIM33 (TIF1gamma) are three related cofactors belonging to the tripartite motif superfamily that interact with distinct transcription factors. The structure of TRIM33 is similar to TRIM24 and TRIM28, exhibiting multiple domains (RING finger, coiled coil, B boxes, PHD/TTC, and bromodomain). TRIM33 functions in cell differentiation and development, playing a role in differentiation of hematopoietic cells. It interacts with the Smad2/3 transcription factor in hematopoietic, mesenchymal, and epithelial cell types to mediate different transcriptional effects in response to TGF-beta. It acts as an E3 ubiquitin-protein ligase and promotes SMAD4 ubiquitination.

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NCBP1 Antibody: NCBP1, also known as CBP80, is a component of the nuclear cap-binding protein complex (CBC), which binds to the monomethylated 5' cap of nascent pre-mRNA in the nucleoplasm. NCBP1 promotes high-affinity mRNA-cap binding and associates with the CTD of RNA polymerase II. The CBC promotes pre-mRNA splicing, 3'-end processing, RNA nuclear export, and nonsense-mediated mRNA decay (1,2). Recent evidence has shown that cellular-cap-binding proteins such as NCBP1 associate with influenza virus mRNAs, suggesting that these viral mRNAs may follow the normal cellular pathways for splicing, nuclear export, and translation.

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Rift Valley Fever Virus Polymerase Antibody: Rift Valley Fever (RFV) virus is an arthropod-borne virus endemic to Africa that infects humans and animals that is transmitted predominantly by mosquitoes. During human infections, symptoms can range from benign fever to severe encephalitis and fatal hepatitis with hemorrhagic fever. The Bunyaviridae family of viruses to which the RVF virus belongs are spherical enveloped viruses with a tripartite RNA genome of negative or ambisense polarity. The three segments are referred to as the L, M, and S segments. The L and M segments are negative polarity and code fore the L-dependent RNA polymerase and glycoprotein precursor respectively. The S segment is of ambisense polarity and encodes the nucleoprotein and non-structural proteins.

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AKT1S1 Antibody: The Akt signaling pathway contributes to the regulation of apoptosis after a variety of cell death signals. AKT1S1, also known as PRAS40, is a proline-rich substrate of the kinase AKT1 and is thought to play a role in neuroprotection mediated by nerve growth factor (NGF) after transient focal cerebral ischemia. AKT1S1 is also a substrate and potential regulator of mammalian target of rapamycin (mTOR), a serine/threonine kinase that regulates cell growth and cell cycle, and a negative regulator of autophagy. Treatment with the insulin-like growth factor-1 (IGF1) can indusce the phosphorylation of AKT1S1 via the PI3K/AKT signaling pathway in PC12 cells.

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Mucin 1 (MUC1) is membrane-bound protein member of the mucin family. Mucins are O-glycosylated proteins that play an essential role in forming protective mucous barriers on epithelial surfaces and also play a role in intracellular signaling. MUC1 is expressed on the apical surface of epithelial cells that line the mucosal surfaces of many different tissues including lung, breast stomach and pancreas. MUC1 is proteolytically cleaved into alpha and beta subunits that form a heterodimeric complex. The N-terminal alpha subunit functions in cell-adhesion and the C-terminal beta subunit is involved in cell signaling. Overexpression, aberrant intracellular localization, and changes in glycosylation of this protein have been associated with carcinomas.

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ESR1 Antibody: Estrogen receptors (ER) are members of the steroid/thyroid hormone receptor superfamily of ligand-activated transcription factors. Estrogen receptors, including ESR1, also known as ER-alpha and ESR2 (ER-beta), contain DNA binding and ligand binding domains and are critically involved in regulating the normal function of reproductive tissues. ESR1 is a widely expressed nuclear protein and serves as a strong activator of estrogen responsive genes (1,2). Phosphorylation of serines 104 and 106, located in the N-terminal transcription activation function-1 domain (AF-1), plays a large role in regulating ER alpha activity.

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B2M Antibody: Beta2-microglobulin (B2M) is a principal component of the Major Histocompatibility Complex (MHC) class I molecule, a ternary membrane protein complex that displays fragments derived from proteolyzed cytosolic proteins on the surface of cells for recognition by the surveillance immune system (1,2). B2M is involved in the presentation of peptide antigens to the immune system and plays a critically important role in immune system function. It is expressed on nearly all nucleated cells and contains one Ig-like C1-type (immunoglobulin-like) domain. Mutations in the Beta 2-microglobulin gene can enhance the progression of malignant melanoma and osteoarthropathy (4,5).

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SPP1 Antibody: The secreted protein 1 (SPP1), also known as osteopontin, is a major noncollagenous protein of bone, but is also found in the extracellular matrix of other mineralized tissues and in bodily fluids. In bone, SPP1 is produced by osteoblasts, osteocytes, macrophages, and osteoclasts (1,2). SPP1 binds to cells through integrin and non-integrin receptors, as well as the adhesion receptor CD44 in an RGD-independent manner, enabling SPP1 to induce a number of functional effects including macrophage chemotaxis, cytoprotection, and regulation of T helper type 1 cells. SPP1 can regulate biomineralization by inhibiting the formation of hydroxyapatite (3) and the growth of calcium oxalate crystals.

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CRB2 Antibody: CRB2 (Crumbs homolog 2), like its homologs CRB1 and CRB3, is similar to the Drosophila crumbs protein and is expressed in retina, brain and kidney. Along with other proteins, the Crumbs proteins form a complex that help set up cell polarity in developing neuroepithelial cells. At the onset of neural specification, embryonic stem cells (ESCs) upregulate CRB2, which then localizes apically in neural rosettes. Gain- and loss-of-function studies of CRB2 have shown that CRB2 is essential for the stabilization of other polarity proteins. Unlike CRB1, mutations in CRB2 do not appear to play a role in retinitis pigmentosa or in Leber congenital amaurosis.

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N-RAS Antibody: Activating mutations and overexpression of classical Ras subfamily members (N-RAS, H-RAS, and K-RAS) have been widely investigated as key events in the development of human cancers. The N-RAS protein shuttles between the Golgi apparatus and the plasma membrane. This shuttling is regulated through palmitoylation and depalmitoylation by the ZDHHC9-GOLGA7 complex. N-RAS, which has intrinsic GTPase activity, is activated by a guanine nucleotide-exchange factor and inactivated by a GTPase activating protein. Mutations in this gene have been associated with somatic rectal cancer, follicular thyroid cancer, autoimmune lymphoproliferative syndrome, Noonan syndrome, and juvenile myelomonocytic leukemia.

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The protein encoded by BAD gene is a member of the BCL-2 family. BCL-2 family members are known to be regulators of programmed cell death. This protein positively regulates cell apoptosis by forming heterodimers with BCL-xL and BCL-2, and reversing their death repressor activity. Proapoptotic activity of this protein is regulated through its phosphorylation. Protein kinases AKT and MAP kinase, as well as protein phosphatase calcineurin were found to be involved in the regulation of this protein. Alternative splicing of this gene results in two transcript variants which encode the same isoform.

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The transient receptor potential (TRP) protein family consists of a diverse group of cation channels functioning in a variety of homeostatic and regulatory pathways. Four subfamilies exist, based on channel domain homology: C type (canonical), V type (vanilloid receptor related), M type (melastatin related) and P type (PKD). TRPV4, belongs to the V type subfamily and plays a role in systemic osmoregulation. TRPV4 is a calcium channel multi-pass membrane protein activated by various stimuli, including thermal stress, fatty acid metabolites and hypotonicity. TRPV4 is highly expressed in lung and kidney and widely expressed in brain. It plays an important role in regulating neural excitability.

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PMSA (FOLH1) is a type II transmembrane glycoprotein belonging to the M28 peptidase family. Three functionally distinct proteins are encoded, including poly-gamma-glutamate carboxypeptidase in the intestine, N-acetylated alpha-linked acidic dipeptidase 1 in the brain, and prostate- specific membrane antigen in the prostate. A mutation in the intestinal form may be associated with impaired intestinal absorption of dietary folates, resulting in low blood folate levels and consequent hyperhomocysteinemia. The form expressed in the brain may be involved in a number of pathological conditions associated with glutamate excitotoxicity. The prostate form is up-regulated in cancerous cells and is used as an effective diagnostic and prognostic indicator of prostate cancer. This gene likely arose from a duplication event of a nearby chromosomal region.

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Acts as part of the IKK complex in the conventional pathway of NF-κ-B activation and phosphorylates inhibitors of NF-κ-B thus leading to the dissociation of the inhibitor/NF-κ-B complex and ultimately the degradation of the inhibitor. As part of the non-canonical pathway of NF-κ-B activation, the MAP3K14-activated CHUK/IKKA homodimer phosphorylates NFKB2/p100 associated with RelB, inducing its proteolytic processing to NFKB2/p52 and the formation of NF-κ-B RelB-p52 complexes. Also phosphorylates NCOA3. Phosphorylates 'Ser-10' of histone H3 at NF-κ-B-regulated promoters during inflammatory responses triggered by cytokines.

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KREMEN1 Antibody: Kremen (Kringle containing protein marking the eye and the nose) proteins are type I transmembrane proteins that contain extracellular kringle, WSC and CUB domains and an intracellular region without any conserved motifs. Kremens bind a subset of the secreted Dickkopf proteins (Dkk 1, 2, and 4) with high affinity to modulate the canonical Wnt signaling pathway that is transduced by the ternary receptor complex composed of Wnt, Frizzled, and the LDL receptor related protein 5/6 (LRP5/6) coreceptor. KREMEN1 is a receptor for the Dickkopf protein which blocks Wnt/beta catenin signaling. It is necessary to ensure normal spatial and temporal patterns of Wnt activity during developmental processes.

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PRRT2 Antibody: The proline-rich transmembrane protein 2 (PRRT2) contains a proline-rich domain in its N-terminal half and is predominantly expressed in brain and spinal cord in embryonic and postnatal stages. While little is known of the function of this protein, mutations in PRRT2 have been shown to be the causative gene of paroxysmal kinesigenic dyskinesia, which is characterized by recurrent, brief attacks of abnormal involuntary movements induced by sudden voluntary movements. Recent studies have shown that PRRT2 may also be involved in some forms of benign familial infantile epilepsy (BFIE), an autosomal dominant epilepsy syndrome.

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PTRF Antibody: The polymerase I and transcript release factor (PTRF) enables the dissociation of paused ternary polymerase I transcription complexes from the 3' end of pre-rRNA transcripts, regulating rRNA transcription by promoting the dissociation of transcription complexes and the re-initiation of polymerase I on nascent rRNA transcripts. PTRF also localizes to caveolae at the plasma membrane and is thought to play a critical role in the formation of caveolae and the stabilization of caveolins, translocating from caveolae to the cytoplasm after insulin stimulation. PTRF is also thought to modify lipid metabolism and insulin-regulated gene expression. Mutations in this gene result in a disorder characterized by generalized lipodystrophy and muscular dystrophy.

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SHISA4 Antibody: SHISA4 plays an essential role in the maturation of presomitic mesoderm cells by individual attenuation of both FGF and WNT signaling. The Shisa family of single-transmembrane proteins is characterized by an N-terminal cysteine-rich domain and a proline-rich C-terminal region. Its founding member, Xenopus Shisa, promotes head development by antagonizing Wnt and FGF signaling. Shisa physically interacted with immature forms of the Wnt receptor Frizzled and the FGF receptor within the ER and inhibited their posttranslational maturation and trafficking to the cell surface. Loss of Shisa function sensitized the neuroectoderm to Wnt signaling and suppressed head formation during gastrulation.

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The cytokine IL-1 is responsible for initiating a variety of activities through the activation of transcription factors, NF-kappa B and AP-1, thereby promoting host response to injury or infection. IL-1F10 (Interleukin-1 family member 10), also known as FIL1T, IL1HY2 or FKSG75, is highly expressed in the skin, spleen and proliferating B-cells of the tonsil. IL-1F10 binds soluble IL-1 receptor type 1, and is one of nine Interleukin 1 families clustered on chromosome 2, where it is thought to participate in the regulation of adapted and innate immune responses. IL-1F10 and IL-1RN polymorphisms may play an important role in the susceptibility to developing rheumatoid arthritis.

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Nhe-1 Antibody: The Na+/H+ antiporter (Nhe-1) is a ubiquitous membrane-bound enzyme involved in pH regulation of vertebrate cells and is specifically inhibited by the diuretic drug amiloride and activated by a variety of signals including growth factors, mitogens, neurotransmitters, and tumor promoters. Nhe-1 acts as an anchor for actin filaments to control the integrity of the cortical cytoskeleton. This occurs through a previously unrecognized structural link between Nhe-1 and the actin-binding proteins ezrin, radixin, and moesin, collectively referred to as ERM proteins. A structural role for Nhe-1 has been proposed in regulating the cortical cytoskeleton that is independent of its function as an ion exchanger. It is also thought that Nhe-1 play a role in hypertension. At least two isoforms of Nhe-1 are known to exist.

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CD10 is a 100 kDa glycoprotein, also designated Common Acute Lymphocytic Leukemia Antigen (CALLA). It is a cell surface enzyme with neutral metalloendopeptidase activity which inactivates a variety of biologically active peptides. CD10 is expressed on the cells of lymphoblastic, Burkitt’s, and follicular germinal center lymphomas, and on cells from patients with chronic myelocytic leukemia (CML). It is also expressed on the surface of normal early lymphoid progenitor cells, immature B cells within adult bone marrow and germinal center B cells within lymphoid tissue. CD10 is also present on breast myoepithelial cells, bile canaliculi, fibroblasts, with especially high expression on the brush border of kidney and gut epithelial cells.

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Dynamin-1 (Dyn1), with 864-amino acid protein (about 95 kDa), belongs to the dynamin family. Dynamin-1 (neuron-specific), dynamin-2 (ubiquitously expressed), and dynamin-3 (expressed only in the testis, brain, and lung), constitute the dynamin family. Members of the dynamin family are GPTase, microtubule-associated proteins which are involved in endocytosis, synaptic transmission and neurogenesis. Dynamin-1 is phosphorylated in nerve terminals exclusively in the cytosolic compartment and in vitro by protein kinase C. Dynamin-1 is a large GTPase enzyme required in membrane constriction and fission during multiple forms of endocytosis. Dynamin-1 is also a key molecule required for the recycling of synaptic vesicles in neurons, and it has been known that dynamin-1 gene expression is induced during neuronal differentiation.

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Biochemically, most members of the CK family fall into one of two classes, type I (acidic polypeptides) and type II (basic polypeptides). The type II cytokeratins consist of basic or neutral proteins which are arranged in pairs of heterotypic keratin chains coexpressed during differentiation of simple and stratified epithelial tissues. Cytokeratins comprise a diverse group of intermediate filament proteins (IFPs) that are expressed as pairs in both keratinized and non-keratinized epithelial tissue. Cytokeratins play a critical role in differentiation and tissue specialization and function to maintain the overall structural integrity of epithelial cells. Cytokeratins have been found to be useful markers of tissue differentiation which is directly applicable to the characterization of malignant tumors.

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ULK3 belongs to the Ser/Thr protein kinase superfamily and plays a role in the ATP-dependent phosphorylation of target proteins. Knockout of ULK genes results in a severe defect in the autophagy pathway. ULK3, like the other Unc-51-like kinases such as ULK1, ULK2 and ULK4, is highly conserved among eukaryotes. ULK3 has been shown to be a positive regulator of the Hedgehog signaling pathway by enhancing GLI1 and GLI2 transcriptional activity. Furthermore, ULK3 can also interact with SUFU, a protein required for the negative regulation of GLI proteins; this interaction blocks the autophosphorylation of ULK3 and blocks its ability to regulate the GLI proteins.

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NF-κ-B is a pleiotropic transcription factor which is present in almost all cell types and is involved in many biological processed such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-κ-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively.