
Katalognummer: 544 - MBS1569199-5x01mg
Produktkategori: Företag och industri > Vetenskap och laboratorium
Storlek: 5x0.1mg
| Storage and shipping | Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Store at +4 degree C short term (1-2 weeks). Store at -20 degree C 12 months. Store at -80 degree C long term. |
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101-M612
Advanced glycation endproducts (AGE) are adducts formed by the nzymatic glycation or oxidation of macromolecules. AGE forms during aging and its formation is accelerated under pathophysiologic states such as diabetes, Alzheimer’s disease, renal failure and immune/inflammatory disorders. Receptor for Advanced Glycation Endoproducts (RAGE), named for its ability to bind AGE, is a multiligand receptor belonging the immunoglobulin (Ig) superfamily. Besides AGE, RAGE binds amyloid βpeptide, S100/calgranulin family proteins, high mobility group B1 (HMGB1, also know as amphoterin) and leukocyte integrins. The human RAGE gene encodes a 404 amino acid residues (aa) type I transmembrane glycoprotein with a 22 aa signal peptide, a 320 aa extracellular domain containing an Ig-like V-type domain and two Ig like Ce-type domains, a 21 aa transmembrane domain and a 41 aa cytoplasmic domain. The V type domain and the cytoplasmic domain are important for ligand binding and for intracellular signaling, respectively. Two alternative splice variants, lacking the Vtype domain or the cytoplasmic tail, are known. RAGE is highly expressed in the embryonic central nervous system. In adult tissues, RAGE is expressed at low levels in multiple tissues including endothelial and smooth muscle cells, mononuclear phagocytes, pericytes, microglia, neurons, cardiac myocytes and hepatocytes. The expression of RAGE is upregulated upon ligand interaction. Depending on the cellular context and interacting ligand, RAGE activation can trigger differential signaling pathways that affect divergent pathways of gene expression. RAGE activation modulates varied essential cellular responses (including inflammation, immunity, proliferation, cellular adhesion and migration) that contribute to cellular dysfunction associated with chronic diseases such as diabetes, cancer, amyloidoses and immune or inflammatory disorders.
101-M342
C-Reactive Protein (CRP) is a member of the Pentraxin family of proteins that are characterized by a cyclic, non-covalent, pentameric structure. IL-6, IL-1 beta, and glucocorticoids induce hepatic C-Reactive Protein synthesis and release. In humans, C-Reactive Protein is a major acute phase protein, increasing by 1,000-fold within 24 to 48 hours of infection, inflammation or tissue damage. C-Reactive Protein exhibits calcium-dependent binding of its principle ligand, phosphocholine, a constituent of bacterial and fungal cell walls. Upon ligand binding, C-Reactive Protein initiates the activation of the complement cascade and binds Fc gamma RI (CD64) and Fc gamma RIIA (CD32a) on phagocytes to activate phagocytic responses. In mouse, C-Reactive Protein is expressed at very low levels and is not an acute phase reactant.
101-M374
DAN (differential screening-selected gene aberrative in neuroblastoma) was initially identified as a gene whose expression is downregulated in src-transformed rat fibroblasts. Human DAN was isolated from a normal lung cDNA library using mouse DAN as a probe. DAN has now been shown to be a prototypical member of the DAN family of secreted glycoproteins that are putative antagonists for TGFβ superfamily proteins. DAN family members share a cysteine-rich domain that is structurally related to the cysteine-knot motif found in TGFβ superfamily ligands. There are at least five mammalian DAN family members including DAN, Gremlin/DRM, Cer1 (Cerberusrelated), Dante and PRDC (protein related to DAN and cereberus). Additional DAN family members include Xenopus Cerberus, chick Caronte and C. elegans CeCan 1. The DAN family of proteins are thought to act as antagonists by binding TGFβ family ligands and preventing their interactions with signaling receptor complexes. Recombinant human DAN preparationss have been shown to bind BMP4 in a functional ELISA and to inhibit BMP4 mediated bioactivity in ATDC 5 chrondrogenic cells. It is likely the various DAN family members and other TGFβ BMP antagonists including Noggin, Chordin, Follistatin and TSG can selectively antagonize the activities of different subsets of TGFβ superfamily ligands. These antagonists represent one of the many elaborate regulatory mechanisms that have evolved to control the bioactivities of the TGFβ superfamily ligands.
101-M383
Dtk (also called Sky, Tyro3, Rse, Brt), Axl (Ufo, Ark) and Mer (human and mouse homologues of chicken cEyk) constitute a receptor tyrosine kinase subfamily. The extracellular domain of these proteins contain two Ig-like motifs and two fibronectin type III motifs. This characteristic topology is also found in neural cell adhesion molecules and in receptor tyrosine phosphatases. All three receptors bind the vitamin K-dependent protein growth-arrest specific gene 6 (Gas6) which is structurally related to the anticoagulation factor protein S. The binding affinities for Gas6 is in the order of Axl > Dtk > Mer. Gas6 binding induces tyrosine phosphorylation and downstream signaling pathways that can lead to cell proliferation, migration, or the prevention of apoptosis. Dtk is widely expressed during embryonic development. In adults, Dtk is predominantly expressed in neurons in restricted regions of the brain.

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