"Biosensis"

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High-mobility group proteins were named originally since they are abundand relatively low molecular weight proteins which run quickly on SDS-PAGE gels. High-mobility group protein box 1 (HMGB1, Amphoterin) is one of these. The "bx" in the name refers to the so-called high mobility group (HMG) box, a compact domain involved in DNA binding and protein-protein interactions. the HMGB1 molecule has two of these HMG domains. The protein is alslo called amphoterin, this name being derived from the presence of two highly charged regions in the molecule, a relatively neutrally charged N-terminus and a very negatively charged C-terminus. In fact the molecule is very unusually charged throughout, the human sequence consisting of 16.7% Glutamic acid, 9.3% Aspartic acid, 20% lysine and 9.3% Arginine. HMGB1 can bind Toll like receptor 4 (TLR4) and the Receptor for Advanced Glycation End products (RAGE). TLRs are components of the innate immune system, first recognized as a family of receptors which recognize "Pathogen Associated Molecular Pattern molecules (PAMPs). PAMPs are common components of bacteria and when TLRs bind these a strong inflammatory response is activated. More recently it has been recognized that TLRs can also be activated by Damage Associated Molecular Pattern molecules (DAMPs), which are endogenous substances released from damaged and diseased cells which also bind to TLR family receptors and also activate inflammation. HMGB1 is such a DAMP, binding to TLR4, and much evidence suggests that HMGB1 is a strong activator of inflammation. Interestingly, HMGB1 is released by necrotic cells but not by apoptotic cells (1).

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Fox3 is one of a family of mammalian homologues of Fox-1. The Fox proteins are about 46kDa in size, and each includes a central highly conserved RRM type RNA recognition motif. Much interest has focused on Fox3 as a result of the recent finding that this protein corresponds to NeuN, a neuronal nuclear antigen. NeuN/Fox-3 has a function in RNA splicing and is expressed heavily and specifically in neuronal nuclei and cytoplasm. Our antibody was raised against the N-terminal 100 amino acids of human Fox3 as expressed in and purified from E. coli. We did not use full length Fox3 as immunogen since the three mammalian Fox homologues, namely Fox1, Fox2 and Fox3, include virtually identical RRM motifs. The N-terminal region of the three molecules are much more variable in the three molecules so antibodies specific for each of the three molecules can therefore be generated.

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Protein DJ-1 has many roles including protecting cells against oxidative stress and cell death (Ref: SwissProt). Mutations in the DJ-1 gene have been associated with rare forms of autosomal recessive early-onset Parkinson's disease.

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Recognizes native and denatured forms of Cyan Fluorescent Protein (CFP) and its variants: Enhanced Green Fluorescent Protein (EGFP), Yellow Fluorescent Protein (YFP), Enhanced Yellow Fluorescent Protein (EYFP) and Cyan Fluorescent Protein (CFP).

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Monoclonal antibody MC192 against the rat low affinity nerve growth factor receptor (p75NTR) is derived from the fusion of Sp2/0-Ag 14 myeloma cells with mouse immune splenocytes. MC192 monoclonal antibody was originally generated by Chandlers et al. p75NTR was originally discovered as a low affinity nerve growth factor receptor. Later it was found that it was the receptor for all neurotrophins. It mediates signals of neurotrophins for neuronal survival, apoptosis, neurite outgrowth and synaptic plasticity. Recently, it has been revealed that p75NTR is not only acts as the receptor for neurotrophins but also the receptor for many other pathological ligands such as prions, rabies virus and amyloid beta. p75NTR also acts as a co-receptor for NOGO which mediates inhibitory signals of myelin associated protein. p75NTR is highly expressed in a number of non-neuronal and neuronal cells including motor neurons during development and also in damaged neurons. MC192 recognizes the extracellular domain of the neurotrophin receptor p75NTR in rat. MC192 antibody may be used for immunocytochemical localisation of rat cells expressing p75NTR, ELISA and western blot. This antibody has also been used for the construction of the MC192-saporin immunotoxin for specific elimination of neuronal populations in basal forebrain cholinergic neurons to generate an animal model for Alzheimer's disease. Using Flow Cytometry, this antibody has frequently been employed for panning to isolate p75NTR-expressing rat cells. MC192 has a potential use as the ligand for gene delivery into p75NTR-expressing rat cells via a receptor-mediated mechanism. FUNCTION: Low affinity receptor which can bind to NGF, BDNF, NT-3, and NT-4. Can mediate cell survival as well as cell death of neural cells. SUBUNIT: Homodimer; disulfide-linked. Interacts with p75NTR-associated cell death executor. Interacts with NGFRAP1/BEX3. Interacts with TRAF2, TRAF4, TRAF6, PTPN13 and RANBP9. Interacts through TRAF6 with SQSTM1 which bridges NGFR to NTRK1 (By similarity). Interacts with BEX1. SUBCELLULAR LOCATION: Membrane; single-pass type I membrane protein. DOMAIN: Death domain is responsible for interaction with RANBP9. PTM: N- and O-glycosylated. PTM: Phosphorylated on serine residues. SIMILARITY: Contains 1 death domain. SIMILARITY: Contains 4 TNFR-Cys repeats.

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Nerve growth factor receptor (NGFR) is also referred to as p75(NTR) due to its molecular mass and its ability to bind at low affinity not only NGF (see 162030), but also other neurotrophins, including brain-derived neurotrophic factor (BDNF; 113505), neurotrophin-3 (NTF3; 162660), and neurotrophin-4/5 (NTF5; 162662). At the time of its discovery, NGFR was considered a unique type of protein. Subsequently, however, a large superfamily of tumor necrosis factor receptors were found to share the overall structure of NGFR (4 extracellular ligand-binding, cysteine-rich repeats, or CRs, and signaling through association with, or disassociation from, cytoplasmic interactors). The identification of this superfamily helped elucidate some of the biologic functions of NGFR, including its ultimate involvement in the nuclear factor kappa-B (NFKB; see 164011) and apoptosis pathways. As a monomer, NGFR binds NGF with low affinity. Higher affinity binding is achieved by association with higher molecular mass, low-affinity neurotrophin receptors, namely the tropomyosin receptor kinases, TRKA (NTRK1; 191315), TRKB (NTRK2; 600456), and TRKC (NTRK3; 191316). TRKA, TRKB, and TRKC are specific for or 'preferred by' NGF, NTF5 and BDNF, and NTF3, respectively (Ip et al., 1993). NTF3 also binds to TRKA and TRKB, but with significantly lower affinity

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Nerve growth factor receptor (NGFR) is also referred to as p75(NTR) due to its molecular mass and its ability to bind at low affinity not only NGF (see 162030), but also other neurotrophins, including brain-derived neurotrophic factor (BDNF; 113505), neurotrophin-3 (NTF3; 162660), and neurotrophin-4/5 (NTF5; 162662). At the time of its discovery, NGFR was considered a unique type of protein. Subsequently, however, a large superfamily of tumor necrosis factor receptors were found to share the overall structure of NGFR (4 extracellular ligand-binding, cysteine-rich repeats, or CRs, and signaling through association with, or disassociation from, cytoplasmic interactors). The identification of this superfamily helped elucidate some of the biologic functions of NGFR, including its ultimate involvement in the nuclear factor kappa-B (NFKB; see 164011) and apoptosis pathways. As a monomer, NGFR binds NGF with low affinity. Higher affinity binding is achieved by association with higher molecular mass, low-affinity neurotrophin receptors, namely the tropomyosin receptor kinases, TRKA (NTRK1; 191315), TRKB (NTRK2; 600456), and TRKC (NTRK3; 191316). TRKA, TRKB, and TRKC are specific for or 'preferred by' NGF, NTF5 and BDNF, and NTF3, respectively. NTF3 also binds to TRKA and TRKB, but with significantly lower affinity.

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Nestin is a member of the class IV intermediate filament protein family which is expressed in neuronal stem cells. The molecular weight of human Nestin as determined by SDS-PAGE mobility is about 240kDa. However the real molecular weight is considerably less than this, at 177kDa, the disparity being likely due to the highly charged region of the C-terminal segment. Nestin is relatively poorly conserved in protein sequence across species boundaries, so that the mouse and human proteins have an overall identity of only 62%. As a result antibodies to the human protein often fail to recognize the rodent homologue and vice versa. However this antibody stains both rodent and human Nestin. Antibodies to Nestin are widely used to identify neural stem cells.

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The D-tag system utilises a short hydrophilic peptide (DYKDDDDK) that is fused to either the N- or C-terminus of the protein of interest. It can be used in conjunction with other tags such as the 6X His tag.

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GST (Glutathione S-Transferase) is a 26 kDa protein encoded by the Schistosoma japonicum.

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The Human influenza hemagglutin (HA) tag corresponds to a region (98-106 amino acids) from the HA molecule.

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The 6X His tag is a short peptide sequence of 6 histidine residues. Epitopes such as the 6X His tag are often included with the target DNA at the time of cloning to produce fusion proteins containing the tag sequence. This allows anti-epitope tag antibodies such as this one to serve as a universal detection reagent for any recombinant protein containing this tag. Anti-epitope antibodies are a useful alternative to generating antibodies to identify a specific recombinant protein. The 6X His motif is often used as a tag on recombinant proteins to facilitate purification with immobilized metal-affinity chromatography.

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The Myc tag contains the amino acids Glu-Gln-Lys-Leu-Ile-Ser-Glu-Glu-Asp-Leu (E-Q-K-L-I-S-E-E-D-L) corresponding to amino acids 410-419 of human Myc. This tag is widely used for monitoring expression of recombinant proteins in bacteria, insect and mammalian cells.

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Designed to detect Red Fluorescent Protein (RFP) and its variants in ELISA (sandwich or capture), immunoblotting, immunoprecipitation and immunohistochemistry.

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The V5 epitope corresponds to a region from Simian Virus Type 5 (SV5).

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Recognizes native and denatured forms of Green Fluorescent Protein (GFP) and its variants: Enhanced Green Fluorescent Protein (EGFP), Yellow Fluorescent Protein (YFP), Enhanced Yellow Fluorescent Protein (EYFP) and Cyan Fluorescent Protein (CFP).