Sample type Serum, Plasma, Cell Culture Supernatant, Other liquid samples
Components
Break apart microtiter test strips each coated single wells
8 x 12 (96 Total)
Lyophilized Standard
2 x vial
Biotin-labeled Antibody(Concentrated, 100X)
120 uL
HRP-Streptavidin Conjugate(Concentrated, 100X)
120 uL
Washing solution concentrate (25X)
30 mL
Sample Dilution buffer
20 mL
Antibody Dilution buffer
10 mL
Streptavidin Dilution buffer
10 mL
Stopping solution
10 mL
TMB Substrate (ready-to-use)
10 mL
Plate seals
3
Storage Store at 2-8°C.
target relevance
anti-XT-M4 antibody Anti-drug antibodies (ADAs) generated in subjects following administration of XT-M4.
XT-M4 XT-M4 biologic drug binds Homo sapiens AGER Advanced glycosylation end product-specific receptor
Homo sapiens AGER Advanced glycosylation end product-specific receptor
Protein names Advanced glycosylation end product-specific receptor
Alternative names Receptor for advanced glycosylation end products
Gene names AGER
Function Cell surface pattern recognition receptor that senses endogenous stress signals with a broad ligand repertoire including advanced glycation end products, S100 proteins, high-mobility group box 1 protein/HMGB1, amyloid beta/APP oligomers, nucleic acids, histones, phospholipids and glycosaminoglycans (PubMed:27572515, PubMed:28515150, PubMed:34743181, PubMed:35974093, PubMed:24081950). Advanced glycosylation end products are nonenzymatically glycosylated proteins which accumulate in vascular tissue in aging and at an accelerated rate in diabetes (PubMed:21565706). These ligands accumulate at inflammatory sites during the pathogenesis of various diseases including diabetes, vascular complications, neurodegenerative disorders and cancers, and RAGE transduces their binding into pro-inflammatory responses. Upon ligand binding, uses TIRAP and MYD88 as adapters to transduce the signal ultimately leading to the induction of inflammatory cytokines IL6, IL8 and TNFalpha through activation of NF-kappa-B (PubMed:21829704, PubMed:33436632). Interaction with S100A12 on endothelium, mononuclear phagocytes, and lymphocytes triggers cellular activation, with generation of key pro-inflammatory mediators (PubMed:19386136). Interaction with S100B after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling (By similarity). Contributes to the translocation of amyloid-beta peptide (ABPP) across the cell membrane from the extracellular to the intracellular space in cortical neurons (PubMed:19906677). ABPP-initiated RAGE signaling, especially stimulation of p38 mitogen-activated protein kinase (MAPK), has the capacity to drive a transport system delivering ABPP as a complex with RAGE to the intraneuronal space. Participates in endothelial albumin transcytosis together with HMGB1 through the RAGE/SRC/Caveolin-1 pathway, leading to endothelial hyperpermeability (PubMed:27572515). Mediates the loading of HMGB1 in extracellular vesicles (EVs) that shuttle HMGB1 to hepatocytes by transferrin-mediated endocytosis and subsequently promote hepatocyte pyroptosis by activating the NLRP3 inflammasome (PubMed:34743181). Binds to DNA and promotes extracellular hypomethylated DNA (CpG DNA) uptake by cells via the endosomal route to activate inflammatory responses (PubMed:24081950, PubMed:28515150). Mediates phagocytosis by non-professional phagocytes (NPP) and this is enhanced by binding to ligands including RNA, DNA, HMGB1 and histones (PubMed:35974093). Promotes NPP-mediated phagocytosis of Saccharomyces cerevisiae spores by binding to RNA attached to the spore wall (PubMed:35974093). Also promotes NPP-mediated phagocytosis of apoptotic cells (PubMed:35974093). Following DNA damage, recruited to DNA double-strand break sites where it colocalizes with the MRN repair complex via interaction with double-strand break repair protein MRE11 (By similarity). Enhances the endonuclease activity of MRE11, promoting the end resection of damaged DNA (By similarity). Promotes DNA damage repair in trophoblasts which enhances trophoblast invasion and contributes to placental development and maintenance (PubMed:33918759). Protects cells from DNA replication stress by localizing to damaged replication forks where it stabilizes the MCM2-7 complex and promotes faithful progression of the replication fork (PubMed:36807739). Mediates the production of reactive oxygen species (ROS) in human endothelial cells (PubMed:25401185)
Subcellular location Cell membrane
Structure Constitutive homodimer; disulfide-linked (PubMed:24081950). Forms homooligomers (PubMed:24081950). Interacts with S100A1 and APP (By similarity). Interacts with S100B, S100A12 and S100A14. Interacts with TIRAP (PubMed:21829704). Interacts with HMGB1 (PubMed:34743181). Interacts with LGP2; this interaction plays an important role in AGER-mediated pro-inflammatory responses and cytokine release (PubMed:33436632). Interacts with double-strand break repair protein MRE11 which is a core component of the MRN complex (PubMed:33918759). The interaction enhances MRE11 endonuclease activity and promotes DNA repair (By similarity). Interacts with the MCM2-7 complex via interaction with complex member MCM2; the interaction is increased following DNA replication stress and stabilizes the MCM2-7 complex at replication forks (PubMed:36807739). Interacts with longistatin, a protein from the saliva of the tick, Haemaphysalis longicornis; the interaction attenuates AGER-mediated production of reactive oxygen species (ROS), activation of NF-kappa-B and expression of adhesion molecules and cytokines in human endothelial cells (PubMed:25401185)
Post-translational modification Phosphorylated on its cytoplasmic domain by PKCzeta/PRKCZ upon ligand binding (PubMed:21829704). Phosphorylated by ATM following DNA damage (By similarity) Targeted by the ubiquitin E3 ligase subunit FBXO10 to mediate its ubiquitination and degradation
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Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from the PubMed database provided by the United States National Library of Medicine at the National Institutes of Health.
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