37479 Results for: "Prosci"

Supplier: Prosci

Apolipoprotein B (Low density lipoprotein). Apolipoprotein B is a major protein constituent of chylomicrons, VLDL and LDL. It functions as a recognition signal for the cellular binding and internalization of LDL particles.

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Thrombomodulin (TM, CD141, THBD) is an endothelial cell expressed transmembrane glycoprotein that can form a complex with the coagulation factor, Thrombin. The Thrombomodulin/Thrombin complex converts protein C to its activated form, protein Ca, which in turn proteolytically cleaves and deactivates factor Va and factor VIIIa, two essential components of the coagulation mechanism. This inactivation reduces the generation of additional thrombin and thereby effectively prevents continued coagulation. Reduced levels of Thrombomodulin can correlate with the pathogenesis of certain cardiovascular diseases, such as atherosclerosis and thrombosis. However, the serum levels of the truncated circulating form of Thrombomodulin are typically elevated during inflammation and in the presence of various inflammatory related diseases. Recombinant soluble Thrombomodulin is a 491 amino acid glycoprotein containing the extracellular domain of Thrombomodulin.

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ABL2(ARG, Abelson-related gene) is a cytoplasmic tyrosine kinase which is closely related to but distinct from ABL1. The similarity of the proteins includes the tyrosine kinase domains and extends amino-terminal to include the SH2 and SH3 domains. ABL2 is expressed in both normal and tumor cells. The ABL2 gene product is expressed as two variants bearing different amino termini, both approximately 12-kb in length. c-Abl shows both cytoplasmic and nuclear localization，c-Abl is involved in two different chromosomal translocations present in human leukemias, which generate Bcr-Abl and TEL-Abl.

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TFCP2 binds a variety of cellular and viral promoters including fibrinogen, alpha-globin, SV40 and HIV-1 promoters. Activation of the alpha-globin promoter in erythroid cells is via synergistic interaction with UBP1. It also functions as part of the SSP (stage selector protein) complex. TFCP2 facilitates the interaction of the gamma-globin genes with enhancer elements contained in the locus control region in fetal erythroid cells. It interacts by binding to the stage selector element (SSE) in the proximal gamma-globin promoter.

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RET (ret proto-oncogene) is a member of the cadherin superfamily and a receptor tyrosine kinase, which are cell-surface molecules that transduce signals for cell growth and differentiation. It can undergo oncogenic activation in vivo and in vitro by cytogenetic rearrangement. Ligands that bind the Ret receptor include the glial cell line-derived neurotropic factor (GDNF) and its congeners neurturin, persephin and artemin. Alterations in the corresponding Ret gene are associated with diseases including papillary thyroid carcinoma, multiple endocrine neoplasia (type 2A and 2B), familial medullary thyroid carcinoma and a congenital developmental disorder known as Hirschsprung抯 disease. The Tyr905 residue located in the Ret kinase domain plays a crucial role in Ret catalytic and biological activity. Substitution of Phe for Tyr905 dramatically inhibits Ret autophosphorylation activity.

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SORL1 (sortilin-related receptor, L A repeats containing) also known as sorting protein-related receptor containing LDLR class A (SorLA), is a Type I membrane protein that may be involved in cell-cell interaction. SorLA, a single transmembrane receptor, binds LDL and transports it into cells by endocytosis. SorLA is synthesized as a proreceptor which is processed to the mature form by a furin-like propeptidase. It can also bind to RAP (receptor-associated protein). SorLA is a multifunctional endocytis receptor important in lipoprotein and protease uptake. The N-terminal propeptide, which is removed, can be cleaved by furin or homologous proteases. Endogenous SorLA binds the neuropeptide head activator (HA) and is important for HA signaling and function. The gene encoding for the protein maps to chromosome 8p23.1. SorLA is expressed mainly in brain (cerebral cortex, cerebellum and the occipital pole), but can also be found in liver, spinal cord, kidney, testis and pancreas.

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Alpha-synuclein (SNCA), with 140-amino acid protein (about 15 kDa), belongs to the synuclein family, which also includes beta- and gamma-synuclein. SNCA is a soluble protein, expressed principally in the brain but also expressed in low concentrations in all tissues examined (except liver). SNCA is implicated in the regulation of dopamine release and transport. The triplication of the SNCA can cause Parkinson disease (PD) and diffuse Lewy body disease within the same kindred. SNCA peptides are a major component of amyloid plaques in the brains of patients with Alzheimer's disease. Immunohistochemistry for SNCA has become the histological technique of choice for the diagnosis for Parkinson's disease, Dementia with Lewy bodies and Multiple System Atrophy.

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Steroid receptor RNA activator 1 (SRA), with 237-amino acid protein (about 27 kDa), belongs to the growing family of functional non-coding RNAs. SRA was originally described as the first functional noncoding RNA able to specifically coactivate the activity of steroid receptors. Specifically, SRA exists as both an RNA transcript that forms a complex with steroid receptor coactivator-1 and as a stably expressed protein. Its expression is strongly up-regulated in many human tumors of the breast, uterus, and ovary, suggesting a potential role in pathogenesis. Although coactivation of steroid-dependent transcription by SRA is accompanied by a proliferative response, overexpression is not in itself sufficient to induce turmorigenesis.

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FUNCTION: Multifunctional protein found in plasma, ascitic fluid, cerebrospinal fluid, and urine and on the surface of many cell types. In plasma, it carries the vitamin D sterols and prevents polymerization of actin by binding its monomers. DBP associates with membrane-bound immunoglobulin on the surface of B-lymphocytes and with IgG Fc receptor on the membranes of T-lymphocytes.

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Monoclonal antibody Respiratory Syncytial Virus Host: Mouse Clone no: 681 Species reactivity: Virus isotype: IgG2b Tested application: ELISA, IF, Neutralization

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Monoclonal antibody Cytomegalovirus -FITC Host: Mouse Clone no: 887 Species reactivity: Virus isotype: IgG1 Tested application: ELISA, WB, IF

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TBC1D4 Antibody: TBC1D4, also known as the Akt substrate AS160, was initially identified as an Akt substrate containing a GTPase-activating domain that regulates GLUT4 trafficking, with activation following insulin stimulation. TBC1D4 truncations in humans is a major cause of dominant inherited insulin resistance. The loss of TBC1D4 results in the accumulation of GLUT4 in compartments that are primed for fusion in basal adipocytes.

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ERGIC53 peptide is used for blocking the activity of ERGIC53 antibody.

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Transmembrane protein 107 (TMEM 107) is critical for cilia formation and embryonic patterning. It is a 139 amino acid transmembrane protein encoded by a gene that maps to human chromosome 17 which is associated with two key tumor suppressor genes p53 and BRCA1. TMEM107 is required for normal Sonic hedgehog (Shh) signaling in the neural tube and acts in combination with Gli2 and Gli3 to pattern ventral and intermediate neuronal cell types. TMEM107 is also a strong candidate gene for central areolar choroidal dystrophy (CACD).

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TREM1 Antibody: TREM1 (triggering receptor expressed on myeloid cells 1) is a receptor belonging to the Ig superfamily that amplifies neutrophil and monocyte-mediated inflammatory responses triggered by bacterial and fungal infections by stimulating release of pro-inflammatory chemokines and cytokines, as well as increased surface expression of cell activation markers. It is thought that TREM1 other related TREM proteins such as TREM2 act to modulate the inflammatory response. TREM1 has also been linked to inflammatory bowel disease resulting in enhanced production of TNF, IL-6, IL-8, and MCP-1.

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RIP1 Antibody: RIP1 (Receptor Interacting Protein), also known as RIPK1, is a crucial 74 kD adaptor kinase in several of stress-induced signaling pathways and on the crossroad of a cell’s decision to live or die. RIP1 contains an N-terminal region with homology to protein kinases, an intermediate domain capable of association with MAPKKK and a C-terminal region containing a death domain motif present in the Fas and TNFR1 intracellular domains. Full length RIP1 is important for signallling to NF-kappa-B, MAPKs and necrosis, whereas caspase-8 generates a C-terminal RIP1 cleavage fragment, promoting TNF-induced apoptosis. It is required for TNFRSF1A-mediated and TLR3-induced NF-kappa-B activation. RIP1-deficient mice fail to thrive, displaying extensive apoptosis in both lymphoid and adipose tissues and dying at 1-3 days of age.

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Brain tissue lysate (7 Days Old) was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin

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Monoclonal antibody Hepatitis A Virus Host: Mouse Clone no: 1881 Species reactivity: virus isotype: IgG1 Tested application: E, IHC, IF

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IGF1R(insulin-like growth factor 1 receptor), a transmembrane receptor tyrosine kinase, is widely expressed in many cell types within fetal and postnatal tissues, and in many cell lines. Upon binding to its ligands, IGF-I and IGF-II, receptor autophosphorylation occurs. The triple tyrosine cluster within the kinase domain (Tyr1131, Tyr1135 and Tyr1136) is the earliest major site of autophosphorylation. Phosphorylation of these three tyrosine residues is necessary for kinase activation.Insulin receptors (IRs) share significant similarity with IGF1 receptors in both structure and function,including an equivalent triple tyrosine cluster within the activation loop of the kinase domain (Tyr1146, Tyr1150 and Tyr1151).Tyrosine autophosphorylation of insulin receptor is one of the earliest cellular responses to insulin stimulation. Autophosphorylation begins with phosphorylation of Tyr1146 and either Tyr1150 or Tyr1151. Full kinase activation requires the triple tyrosine phosphorylation.

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Appears to have a function in striated muscle development and regeneration.

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Myc proto-oncogene encodes nuclear DNA-binding phosphoproteins that are involved in the regulation of gene expression and DNA replication during cell growth and differentiation. Myc encodes a protein of 65 kDa which is expressed in almost all normal and transformed cells. The expression correlates with the proliferation state of the cells. Transcription is repressed in quiescent or terminally differentiated cells. Expression of Myc is generally induced after mitogenic stimulation of cells or serum induction. Myc therefore is an important positive regulator of cell growth and proliferation. Myc has been demonstrated also to be a potent inducer of apoptosis when expressed in the absence of serum or growth factors. Apoptosis may serve also as a protective mechanism to prevent tumorigenicity elicited by deregulated Myc expression. Sequences of the Myc oncogene have been highly conserved throughout evolution, from Drosophila to vertebrates

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Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity. The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both. Axonal polarity is predetermined by tau localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization.

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Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. The alpha and alpha' chains contain the catalytic site. Participates in Wnt signaling. CK2 phosphorylates 'Ser-392' of p53/TP53 following UV irradiation.

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Monoclonal, Host: Mouse, Clone: [1256], Species Reactivity: Virus, Isotype: Mouse IgG2a, Tested Applications: ELISA, IF

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Monoclonal, Host: Mouse, Clone: [7721], Species Reactivity: Bacteria, Isotype: Mouse IgG1, Tested Applications: ELISA, Western blotting

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Polyclonal, Host: Goat, Species Reactivity: Virus, Immunogen: Recombinant E2 (genotype 1a), Tested Applications: Western blotting

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Monoclonal, Clone: [1D4], Host: mouse; Species Reactivity: Mam, Amp; Bovine rhodopsin; Isotype: IgG1; Tested Applications: WB, IHC

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Neuromedin U Receptor 2 is a Neuromedin Receptor. NMU2R may mediate the contractile activity of neuromedin U in the uterus.

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Monoclonal, Host: mouse, Clone: PC10, Species Reactivity: Human, Immunogen: PCNA Monoclonal antibody was raised against recombinant, Isotype: IgG2a, Tested Application: Western blotting, Immuno Histo chemistry, IP, FACS.

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Polyclonal, Host: Goat, Species reacivity: human, Immunogen: Produced from sera of goats pre-immunized with highly pure (>98%) recombinant hVEGF (human VEGF), Tested application: ELISA, WB