Anti-Human RAGE Antibody

101-M612

Anti-Human RAGE Antibody

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.

748.5 €

MBS1569199-01mg

Anti-Human RAGE Antibody (XT-M4)

701.38 €

MBS1569199-5x01mg

Anti-Human RAGE Antibody (XT-M4)

2123 €

101-M78

Anti-Human MIG Antibody

MIG, a CXC chemokine, is produced by IFN stimulated monocytes, macrophages and endothelial cells. It signals through the CXCR3 receptor. MIG selectively chemoattracts Th1 lymphocytes, and also exerts other activities including inhibition of tumor growth, angiogenesis, and inhibition of colony formation of hematopoietic progenitors. Human MIG is active on murine cells. Recombinant murine MIG is a 12.2 kDa protein containing 105 amino acid residues, including the four highly conserved cysteine residues present in CXC chemokines.

520.12 €

101-M83

Anti-Human SCF Antibody

Stem cell factor (SCF), also known as c-kit ligand (KL), mast cell growth factor (MGF), and steel factor (SLF), is a widely expressed 28 - 40 kDa type I transmembrane glycoprotein. It promotes the survival, differentiation, and mobilization of multiple cell types including myeloid, erythroid, megakaryocytic, lymphoid, germ cell, and melanocyte progenitors. SCF is a primary growth and activation factor for mast cells and eosinophils. Mature human SCF consists of a 189 amino acid (aa) extracellular domain (ECD), a 23 aa transmembrane segment, and a 36 aa cytoplasmic tail. The ECD shows both N-linked and O-linked glycosylation. Proteolytic cleavage at two alternate sites in the extracellular juxtamembrane region releases a 25 kDa soluble molecule which is comparable to the only form produced by Steel-dickie mutant mice. An alternately spliced isoform of human SCF lacks 28 aa that encompasses the primary proteolytic recognition site. Within the ECD of the short isoform (corresponding to this recombinant protein), human SCF shares 75 - 83% aa sequence identity with canine, feline, mouse, and rat SCF. Rat SCF is active on mouse and human cells, but human SCF is only weakly active on mouse cells. Noncovalent dimers of transmembrane or soluble SCF interact with the receptor tyrosine kinase SCF-R/c-kit to trigger receptor dimerization and signaling. SCF assists in the recovery of cardiac function following myocardial infarction by increasing the number of cardiomyocytes and vascular channels.

520.12 €

102-P06

Anti-Human EGF Antibody

Epidermal growth factor (EGF) is the founding member of the EGF family that also includes TGFα, amphiregulin (AR), betacellulin (BTC), epiregulin (EPR), heparin-binding EGF-like growth factor (HB-EGF), epigen, and the neuregulins (NRG)1 through 6. Members of the EGF family share a structural motif, the EGF-like domain, which is characterized by three intramolecular disulfide bonds that are formed by six similarly spaced conserved cysteine residues. All EGF family members are synthesized as type I transmembrane precursor proteins that may contain several EGF domains in the extracellular region. The mature proteins are released from the cell surface by regulated proteolysis. The 1207 amino acid (aa) human EGF precursor contains nine EGF domains and nine LDLR class B repeats. The mature protein consists of 53 aa and is generated by proteolytic excision of the EGF domain proximal to the transmembrane region. Mature human EGF shares 70% aa sequence identity with mature mouse and rat EGF. EGF is present in various body fluids, including blood, milk, urine, saliva, seminal fluid, pancreatic juice, cerebrospinal fluid, and amniotic fluid. Four ErbB (HER) family receptor tyrosine kinases including EGFR/ErbB1, ErbB2, ErbB3 and ErbB4, mediate responses to EGF family members.

518.55 €