140523 Results for: "3-Hydroxycyclobutanecarboxylic acid&"
Anti-C4A, C4B Mouse Monoclonal Antibody [clone: SPM545]
Supplier: Prosci
This mAb is specific to Complement 4d (C4d) and it reacts with the secreted as well as cell-bound C4d. C4d is a degradation product of the activated complement factor C4b. Complement 4b is typically activated by binding of Abs to specific target molecules. Following activation and degradation of the C4 molecule, thio-ester groups are exposed, which allow transient, covalent binding of the degradation product Complement 4d to endothelial cell surfaces and extracellular matrix components of vascular basement membranes near the sites of C4 activation. The presence of C4d in peritubular capillaries is a key indicator for acute humoral (i.e. antibody-mediated) rejection of kidney, heart, pancreas and lung allografts. As an established marker of antibody-mediated acute renal allograft rejection and its proclivity for endothelium, this component can be detected in peritubular capillaries in chronic renal allograft rejection as well as hyperacute rejection, acute vascular rejection, acute cellular rejection, and borderline rejection. It has been shown to be a significant predictor of transplant kidney graft survival. Anti-C4d, combined with anti-C3d, can be utilized as a tool for diagnosis of allograft rejection that may warrant a prompt and aggressive anti-rejection treatment.
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Anti-SIRT2 Rabbit Polyclonal Antibody
Supplier: Proteintech
The Silent Information Regulator (SIR2) family of genes is a highly conserved group of genes that encode nicotinamide adenine dinucleotide (NAD)-dependent protein deacetylases, also known as Class III histone deacetylases. The first discovered and best characterized of these genes is Saccharomyces cerevisiae SIR2, which is involved in silencing of mating type loci, telomere maintenance, DNA damage response, and cell aging (10545947). SirT2, a mammalian homolog of Sir2, deacetylates α-tubulin at Lys40 and histone H4 at Lys16 and has been implicated in cytoskeletal regulation and progression through mitosis (12620231,16648462). SirT2 protein is mainly cytoplasmic and is associated with microtubules and HDAC6, another tubulin deacetylase (12620231). Deacetylation of α-tubulin decreases its stability and may be required for proper regulation of cell shape, intracellular transport, cell motility, and cell division (12620231,10966460). The abundance and phosphorylation state of SirT2 increase at the G2/M transition of the cell cycle, and SirT2 relocalizes to chromatin during mitosis when histone H4 Lys16 acetylation levels decrease (16648462,12697818). Overexpression of SirT2 prolongs mitosis, while overexpression of the CDC14B phosphatase results in both decreased phosphorylation and abundance of SirT2, allowing for proper mitotic exit (12697818). Thus, the deacetylation of both histone H4 and α-tubulin by SirT2 may be critical for proper chromatin and cytoskeletal dynamics required for completion of mitosis. This antibody recognizes the 37-45 KD SIRT2 proteins. This antibody is a specific antiboy that it can't detect signal with SIRT2-KO samples.
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Anti-HA Mouse Monoclonal Antibody [clone: 1E6A7]
Supplier: Prosci
Hemagglutinin Monoclonal Antibody: Influenza A virus is a major public health threat, killing more than 30,000 people per year in the USA. Novel influenza virus strains caused by genetic drift and viral recombination emerge periodically to which humans have little or no immunity, resulting in devastating pandemics. Influenza A can exist in a variety of animals; however it is in birds that all subtypes can be found. These subtypes are classified based on the combination of the virus coat glycoproteins hemagglutinin (HA) and neuraminidase (NA) subtypes. During 1997, an H5N1 avian influenza virus was determined to be the cause of death in 6 of 18 infected patients in Hong Kong. The more recent virulent strain of H5N1 is now seen in Africa and Europe, as well as in southeast Asia. There is some evidence of human to human spread of this virus, but it is thought that the transmission efficiency was fairly low. HA interacts with cell surface proteins containing oligosaccharides with terminal sialyl residues. Virus isolated from a human infected with the H5N1 strain in 1997 could bind to oligosaccharides from human as well as avian sources, indicating its species-jumping ability. While efforts were made to use relatively conserved regions of the viral sequence as the antigen, the influenza virus genome has drifted somewhat from what was first reported. However, this antibody was able to recognize peptides derrived from viruses from Indonesian human patients infected in 2007.
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Anti-HA Mouse Monoclonal Antibody [clone: 4H1C10]
Supplier: Prosci
Hemagglutinin Monoclonal Antibody: Influenza A virus is a major public health threat, killing more than 30,000 people per year in the USA. Novel influenza virus strains caused by genetic drift and viral recombination emerge periodically to which humans have little or no immunity, resulting in devastating pandemics. Influenza A can exist in a variety of animals; however it is in birds that all subtypes can be found. These subtypes are classified based on the combination of the virus coat glycoproteins hemagglutinin (HA) and neuraminidase (NA) subtypes. During 1997, an H5N1 avian influenza virus was determined to be the cause of death in 6 of 18 infected patients in Hong Kong. The more recent virulent strain of H5N1 is now seen in Africa and Europe, as well as in southeast Asia. There is some evidence of human to human spread of this virus, but it is thought that the transmission efficiency was fairly low. HA interacts with cell surface proteins containing oligosaccharides with terminal sialyl residues. Virus isolated from a human infected with the H5N1 strain in 1997 could bind to oligosaccharides from human as well as avian sources, indicating its species-jumping ability. While efforts were made to use relatively conserved regions of the viral sequence as the antigen, the influenza virus genome has drifted somewhat from what was first reported. However, this antibody was able to recognize peptides derrived from viruses from Indonesian human patients infected in 2007.
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Anti-NFKB1 Rabbit Polyclonal Antibody
Supplier: Proteintech
NFkB is a pleiotropic transcription factor which is present in almost all cell types and is involved in many biological processed such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NFkB is activated by various intra- and extracellular stimuli such as cytokines, oxidant free radicals, ultraviolet irradiation, and bacterial or viral products. NFkB is a family of transcription factors that consists of homo- and heterodimers of NFkB1/p50 and RelA/p65 subunits, and controls a variety of cellular events including development and immune responses. All members share a conserved amino terminus domain that includes dimerization, nuclear localization, and DNA binding regions, and a carboxy terminal transactivation domain. Serines 529 and 536 in the transactivation domain of RelA/p65 are phosphorylated in response to several stimuli including phorbol ester, IL1 alpha and TNF alpha as mediated by IkB kinase and p38 MAPK. Phosphorylation of serines 529 and 536 is critical for RelA/p65 transcriptional activity. Activated NFkB translocates into the nucleus and stimulates the expression of genes involved in a wide variety of biological functions. Inappropriate activation of NFkB has been associated with a number of inflammatory diseases while persistent inhibition of NFkB leads to inappropriate immune cell development or delayed cell growth. NFKB1 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p105 and generation of p50 by a cotranslational processing. This antibody can bind both p105 and p50 isoforms of NFKB1.
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Anti-MUC3A Mouse Monoclonal Antibody (CF405S) [clone: M3.1]
Supplier: Biotium
This antibody recognizes a protein of HMW, identified as mucin 3 glycoprotein (MUC3). Its epitope localizes between aa SITTTE. This MAb shows no cross-reaction with human milk fat globule membranes, MUC1, or MUC2. MUC3 is distributed in colon and rectum, and is also present to a lesser extent in breast, lung and salivary gland tissues. The Mucins are a family of highly glycosylated, secreted proteins with a basic structure consisting of a variable number of tandem repeats (VNTRs) encoded by 60 base pairs (Mucin 1), 69 base pairs (Mucin 2) and 51 base pairs (Mucin 3). The number of repeats is highly polymorphic and varies among different alleles. Mucin 1 proteins are expressed as type I membrane proteins in addition to secreted forms. Mucin 1 is aberrantly expressed in epithelial tumors including breast carcinomas. Mucin 2 coats the epithelia of the intestines and airways and is associated with colonic tumors. Mucin 3 is a major component of various mucus gels and is broadly expressed in normal and tumor cells.
CF® dyes are Biotium's next-generation fluorescent dyes. CF®405S is a blue fluorescent dye (Ex/Em 404/431 nm) with superior brightness compared to other blue dyes; it is also compatible with super-resolution imaging by SIM. Note: Conjugates of blue fluorescent dyes are not recommended for detecting low abundance targets, because blue dyes have lower fluorescence and can give higher non-specific background than other dye colors.
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Anti-HA Mouse Monoclonal Antibody [clone: 7B9B2]
Supplier: Prosci
Hemagglutinin Monoclonal Antibody: Influenza A virus is a major public health threat, killing more than 30,000 people per year in the USA. Novel influenza virus strains caused by genetic drift and viral recombination emerge periodically to which humans have little or no immunity, resulting in devastating pandemics. Influenza A can exist in a variety of animals; however it is in birds that all subtypes can be found. These subtypes are classified based on the combination of the virus coat glycoproteins hemagglutinin (HA) and neuraminidase (NA) subtypes. During 1997, an H5N1 avian influenza virus was determined to be the cause of death in 6 of 18 infected patients in Hong Kong. The more recent virulent strain of H5N1 is now seen in Africa and Europe, as well as in southeast Asia. There is some evidence of human to human spread of this virus, but it is thought that the transmission efficiency was fairly low. HA interacts with cell surface proteins containing oligosaccharides with terminal sialyl residues. Virus isolated from a human infected with the H5N1 strain in 1997 could bind to oligosaccharides from human as well as avian sources, indicating its species-jumping ability. While efforts were made to use relatively conserved regions of the viral sequence as the antigen, the influenza virus genome has drifted somewhat from what was first reported. However, this antibody was able to recognize peptides derrived from viruses from Indonesian human patients infected in 2007.
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Anti-GDNF Chicken Polyclonal Antibody
Supplier: Biosensis
GDNF is a glycosylated, disulfide-bonded homodimer molecule. It was first discovered as a potent survival factor for midbrain dopaminergic neurons and was then shown to rescue these neurons in animal models of Parkinson's disease. GDNF is about 100 times more efficient survival factor for spinal motor neurons than the neurotrophins. FUNCTION: Neurotrophic factor that enhances survival and morphological differentiation of dopaminergic neurons and increases their high-affinity dopamine uptake. SUBUNIT: Homodimer; disulfide-linked. SUBCELLULAR LOCATION: Secreted protein. ALTERNATIVE PRODUCTS: 2 named isoforms produced by alternative splicing. DISEASE: Defects in GDNF may be a cause of Hirschsprung disease (HSCR). In association with mutations of RET gene, defects in GDNF may be involved in Hirschsprung disease. This genetic disorder of neural crest development is characterized by the absence of intramural ganglion cells in the hindgut, often resulting in intestinal obstruction. DISEASE: Defects in GDNF are a cause of congenital central hypoventilation syndrome (CCHS); also known as congenital failure of autonomic control or Ondine curse. CCHS is a rare disorder characterized by abnormal control of respiration in the absence of neuromuscular or lung disease, or an identifiable brain stem lesion. A deficiency in autonomic control of respiration results in inadequate or negligible ventilatory and arousal responses to hypercapnia and hypoxemia. SIMILARITY: Belongs to the TGF-beta family. GDNF subfamily.
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Anti-HDAC4 Rabbit Polyclonal Antibody
Supplier: Prosci
DNA is wrapped around histone proteins to form nucleosomes and chromatin fiber, a higher-order structure. Chromatin can become alternatively revealed to or concealed from transcription factors. Acetylation of lysine residues induces conformational changes in core histones by destabilizing nucleosomes and allowing transcription factors access to recognition elements in DNA. Deacetylation of histones by histone deacetylases (HDACs) reseals the chromosomal package, leading to a repression of transcription. HDAC4 does not bind DNA directly, but rather through MEF2C and MEF2D. Binding of the N terminus of HDAC4 to MEF2C represses MEF2C transcription activity. The catalytic domain of HDAC4 interacts with HDAC3 via the transcriptional corepressor NCOR2. Experimental conditions leading to the suppression of HDAC4 binding to NCOR2 and to HDAC3 result in loss of enzymatic activity associated with HDAC4, indicating regulation of transcription by bridging the enzymatically active NCOR2-HDAC3 complex and select transcription factors. HDAC4 and MITR contain calmodulin-binding domains that overlap with their MEF2 binding domains. Binding of calmodulin to HDAC4 leads to its dissociation from MEF2, relieving MEF2 from the transcriptional repression by HDAC4. Together, HDAC4, MITR, and CABIN1 constitute a family of calcium-sensitive transcriptional repressors of MEF2. In murine studies, HDAC4, which is expressed in prehypertrophic chondrocytes, interacts with and inhibits the activity of Runx2 in mice, a transcription factor necessary for chondrocyte hypertrophy, establishing HDAC4 as a central regulator of chondrocyte hypertrophy and skeletogenesis.
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Anti-KRT8 Mouse Monoclonal Antibody [clone: TS1]
Supplier: Prosci
Cytokeratin 8 is the product of the KRT8 gene and one of the most abundant keratins. The KRT8 gene is a member of the type II keratin family clustered on the long arm of chromosome 12. Cytokeratin 8 participates in cellular differentiation and signal transduction, protects against apoptosis, stress and injury, and helps maintain cellular structural integrity. It is primarily found in the non-squamous epithelia and is present in majority of adenocarcinomas and ductal carcinomas. It is absent in squamous cell carcinomas. Specific combinations of cytokeratins are associated with certain epithelial cells, and therefore useful in the characterization of poorly differentiated carcinoma. Hepatocellular carcinomas are defined by the use of antibody that recognizes only cytokeratin 8 and 18. Keratin 8 exists on several types of normal and neoplastic epithelia, including many ductal and glandular epithelia such as colon, stomach, small intestine, trachea, and esophagus as well as in transitional epithelium. Antibody to Cytokeratin 8 does not react with skeletal muscle or nerve cells. Epithelioid sarcoma, chordoma, and adamantinoma show strong positivity corresponding to that of simple epithelia (with antibodies against Keratin 8, 18 and 19). Reportedly, Cytokeratin 8 antibody is useful for the differentiation of lobular (ring-like, perinuclear) from ductal (peripheral-predominant) carcinoma of the breast.
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Anti-GNAT3 Rabbit Polyclonal Antibody
Supplier: Prosci
Guanine nucleotide-binding protein (G protein) alpha subunit playing a prominent role in bitter and sweet taste transduction as well as in umami (monosodium glutamate, monopotassium glutamate, and inosine monophosphate) taste transduction. Transduction by this alpha subunit involves coupling of specific cell-surface receptors with a cGMP-phosphodiesterase; Activation of phosphodiesterase lowers intracellular levels of cAMP and cGMP which may open a cyclic nucleotide-suppressible cation channel leading to influx of calcium, ultimately leading to release of neurotransmitter. Indeed, denatonium and strychnine induce transient reduction in cAMP and cGMP in taste tissue, whereas this decrease is inhibited by GNAT3 antibody. Gustducin heterotrimer transduces response to bitter and sweet compounds via regulation of phosphodiesterase for alpha subunit, as well as via activation of phospholipase C for beta and gamma subunits, with ultimate increase inositol trisphosphate and increase of intracellular Calcium. GNAT3 can functionally couple to taste receptors to transmit intracellular signal: receptor heterodimer TAS1R2/TAS1R3 senses sweetness and TAS1R1/TAS1R3 transduces umami taste, whereas the T2R family GPCRs act as bitter sensors. Functions also as lumenal sugar sensors in the gut to control the expression of the Na+-glucose transporter SGLT1 in response to dietaty sugar, as well as the secretion of Glucagon-like peptide-1, GLP-1 and glucose-dependent insulinotropic polypeptide, GIP. Thus, may modulate the gut capacity to absorb sugars, with implications in malabsorption syndromes and diet-related disorders including diabetes and obesity.
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Anti-HA Mouse Monoclonal Antibody [clone: 1E7D8]
Supplier: Prosci
Hemagglutinin Monoclonal Antibody: Influenza A virus is a major public health threat, killing more than 30,000 people per year in the USA. Novel influenza virus strains caused by genetic drift and viral recombination emerge periodically to which humans have little or no immunity, resulting in devastating pandemics. Influenza A can exist in a variety of animals; however it is in birds that all subtypes can be found. These subtypes are classified based on the combination of the virus coat glycoproteins hemagglutinin (HA) and neuraminidase (NA) subtypes. During 1997, an H5N1 avian influenza virus was determined to be the cause of death in 6 of 18 infected patients in Hong Kong. The more recent virulent strain of H5N1 is now seen in Africa and Europe, as well as in southeast Asia. There is some evidence of human to human spread of this virus, but it is thought that the transmission efficiency was fairly low. HA interacts with cell surface proteins containing oligosaccharides with terminal sialyl residues. Virus isolated from a human infected with the H5N1 strain in 1997 could bind to oligosaccharides from human as well as avian sources, indicating its species-jumping ability. While efforts were made to use relatively conserved regions of the viral sequence as the antigen, the influenza virus genome has drifted somewhat from what was first reported. However, this antibody was able to recognize peptides derrived from viruses from Indonesian human patients infected in 2007.
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Anti-FGF13 Mouse Monoclonal Antibody (PerCP (Peridinin-Chlorophyll Protein Complex)) [clone: S235-22]
Supplier: Rockland Immunochemical
FGF13(Fibroblast growth factor 13), also called FHF2 is a protein that in humans is encoded by the FGF13 gene.The protein encoded by this gene is a member of the fibroblast growth factor (FGF) family. FGF13is a large gene, extending over approximately 200 kb in Xq26.3, and contains at least 7 exons. By cytogenetic, FISH, and database analysis, Gecz et al. (1999) localized the FGF13 gene within a 400-kb duplication interval on chromosome Xq26.3. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth, and invasion. Other areas of interests and use for researchers include cancer, borjeson-forssman-lehmann syndrome, regulation of actin cytoskeleton pathways, apoptosis, GPCR pathways, TGF-Beta pathways, and Rho familty GTPase pathways. This gene is located to a region associated with Borjeson-Forssman-Lehmann syndrome (BFLS), a syndromal X-linked mental retardation, which suggests it may be a candidate gene for familial cases of the BFL syndrome. The function of this gene has not yet been determined. Two alternatively spliced transcripts encoding different isoforms have been described for this gene.
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Anti-TNF Mouse Monoclonal Antibody [clone: SPM543]
Supplier: Prosci
Tumor Necrosis Factor Alpha (TNF alpha) is a protein secreted by lipopolysaccharide-stimulated macrophages, and causes tumor necrosis when injected into tumor bearing mice. TNF alpha is believed to mediate pathogenic shock and tissue injury associated with endotoxemia. TNF alpha exists as a multimer of two, three, or five non-covalently linked units, but shows a single 17kDa band following SDS PAGE under non-reducing conditions. TNF alpha is closely related to the 25kDa protein Tumor Necrosis Factor beta (lymphotoxin), sharing the same receptors and cellular actions. TNF alpha causes cytolysis of certain transformed cells, being synergistic with interferon gamma in its cytotoxicity. Although it has little effect on many cultured normal human cells, TNF alpha appears to be directly toxic to vascular endothelial cells. Other actions of TNF alpha include stimulating growth of human fibroblasts and other cell lines, activating polymorphonuclear neutrophils and osteoclasts, and induction of interleukin 1, prostaglandin E2 and collagenase production. TNF alpha is currently being evaluated in treatment of certain cancers and AIDS Related Complex.
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Anti-PINK1 Mouse Monoclonal Antibody (PerCP) [Clone: S4-15]
Supplier: Rockland Immunochemical
PINK1 (PTEN induced putative kinase 1) is a mitochondrial serine/threonine kinase which maintains mitochondrial function/integrity, provides protection against mitochondrial dysfunction during cellular stress, potentially by phosphorylating mitochondrial proteins, and is involved in the clearance of damaged mitochondria via selective autophagy (mitophagy). PINK1 is synthesized as a 63 kD protein which undergoes proteolyt processing to generate at least two cleaved forms (55 kD and 42 kD). PINK1 and its substrates have been found in the cytosol as well as in different sub-mitochondrial compartments, and according to the recent reports; PINK1 may be targeted to OMM (outer mitochondrial membrane) with its kinase domain facing the cytosol, providing a possible explanation for the observed physical interaction with the cytosolic E3 ubiquitin ligase Parkin.
Defective PINK1 may cause alterations in processing, stability, localization and activity as well as binding to substrates/interaction-partners which ultimately leads to differential effects on mitochondrial function and morphology. Mutations in PINK1 are linked to autosomal recessive early onset Parkinson's disease, and are associated with loss of protective function, mitochondrial dysfunction, aggregation of alpha-synuclein, as well as proteasome dysfunction. Areas of interest and use for researchers include Neuroscience, mitochondrial function, and CDK-mediated phosphorylation pathways.
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XPert™ Balance Enclosures, Labconco®
Supplier: Labconco
These low-profile enclosures provide user protection by keeping powders, particulates, and fumes contained during weighing procedures
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Anti-TNFRSF13B Rabbit Polyclonal Antibody
Supplier: Prosci
Simultaneously four different laboratories identified a a new member of the tumor necrosis factor (TNF) family. This has been named as TALL-1 , THANK (TNF homologue that activates apoptosis, nuclear factor-kappaB, and c-Jun NH2-terminal kinase , BAFF (for B cell activating factor belonging to the TNF family) and BlyS (B lymphocyte stimulator). Membrane-bound BAFF is processed and secreted through the action of a protease whose specificity matches that of the furin family of proprotein convertases. The receptor for BlyS/BAFF appears to be expressed predominantly on B cells and activated T cells. Recently two orphan receptors TACI and BCMA (,8) have been shown to be receptors for BlyS/BAFF (6-9). TACI is expressed on B cells and signals through CAML, activating the transcription factors NF-AT, NF-κB, and AP-1. TACI is one of three know receptors for BLys. Members in the TNF superfamily regulate immune responses and induce apoptosis. Two novel members in the TNF family were recently identified and designated BAFF/BLyS/TALL-1/THANK/zTNF4 and April/TALL-2, respectively. BAFF was characterized as a B cell activator since it induced B cell proliferation and immunoglobulin secretion. April regulates immunological and non-immunological cell growth. Three receptors, BCMA, TACI, and BAFF-R, for BAFF and April were recently identified. TACI, like BCMA, binds BAFF and April. TACI and its ligands regulate humoral immune responses, activate NF-κB and c-jun N-terminal kinase, and are involved in B cell associated autoimmune diseases.
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Anti-APEX1 Rabbit Polyclonal Antibody
Supplier: Proteintech
APEX1, also named as APE, APE1, HAP1 and REF-1, belongs to the DNA repair enzymes AP/ExoA family. It is a multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 are in DNA repair and redox regulation of transcriptional factors. APEX nuclease is a DNA repair enzyme having apurinic/apyrimidinic (AP) endonuclease, 3-prime,5-prime-exonuclease, DNA 3-prime repair diesterase, and DNA 3-prime-phosphatase activities. On the other hand, APEX1 also exerts reversible nuclear redox activity to regulate DNA binding affinity and transcriptional activity of transcriptional factors by controlling the redox status of their DNA-binding domain, such as the FOS/JUN AP-1 complex after exposure to IR. APEX1 is involved in calcium-dependent down-regulation of parathyroid hormone (PTH) expression by binding to negative calcium response elements (nCaREs). When acetylated at Lys-6 and Lys-7, APEX1 stimulates the YBX1-mediated MDR1 promoter activity, leading to drug resistance. It also acts as an endoribonuclease involved in the control of single-stranded RNA metabolism. It plays a role in regulating MYC mRNA turnover by preferentially cleaving in between UA and CA dinucleotides of the MYC coding region determinant (CRD). In association with NMD1, APEX1 plays a role in the rRNA quality control process during cell cycle progression. 10203-1-AP is a rabbit polyclonal antibody raised against full length APE1 of human origin.
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Anti-NFKB1 Rabbit Polyclonal Antibody
Supplier: Proteintech
NFkB is a pleiotropic transcription factor which is present in almost all cell types and is involved in many biological processed such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NFkB is activated by various intra- and extracellular stimuli such as cytokines, oxidant free radicals, ultraviolet irradiation, and bacterial or viral products. NFkB is a family of transcription factors that consists of homo- and heterodimers of NFkB1/p50 and RelA/p65 subunits, and controls a variety of cellular events including development and immune responses. All members share a conserved amino terminus domain that includes dimerization, nuclear localization, and DNA binding regions, and a carboxy terminal transactivation domain. Serines 529 and 536 in the transactivation domain of RelA/p65 are phosphorylated in response to several stimuli including phorbol ester, IL1 alpha and TNF alpha as mediated by IkB kinase and p38 MAPK. Phosphorylation of serines 529 and 536 is critical for RelA/p65 transcriptional activity. Activated NFkB translocates into the nucleus and stimulates the expression of genes involved in a wide variety of biological functions. Inappropriate activation of NFkB has been associated with a number of inflammatory diseases while persistent inhibition of NFkB leads to inappropriate immune cell development or delayed cell growth. NFKB1 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p105 and generation of p50 by a cotranslational processing. This antibody can bind p105 isoforms of NFKB1.
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Human Kallikrein 3/PSA Quantitative ELISA (Ultra-Sensitive)
Supplier: ReVacc Scientific
This kit is developed to measure the levels of human Kallikrein 3/Prostate Specific Antigen (KLK3/PSA) concentrations in cell culture supernates, serum, plasma or biological fluids.
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Anti-SPTAN1 Rabbit Polyclonal Antibody
Supplier: Biosensis
The spectrin family of proteins were originally discovered as major components of the submembraneous cytoskeleton of osmotically lysed red blood cells (1). The lysed blood cells could be seen as clear red blood cell shaped objects in the light microscope and were referred to as red cell "ghosts". The major proteins of these ghosts proved to be actin, ankyrin, band 4.1 and several other proteins, including two major bands running at about 240kDa and 260kDa on SDS-PAGE gels. This pair of bands was named "spectrin" since they were discovered in these red blood cell ghosts (1). Later work showed that similar high molecular bands were seen in membrane preparations from other eukaryotic cell types. Work by Levine and Willard described a pair of about ~240-260kDa molecular weight bands which were transported at the slowest rate along mammalian axons (2). They named these proteins "fodrin" as antibody studies showed that they were localized in the sheath under the axonal membrane, but not in the core of the axon (2; fodros is Greek for sheath). Subsequently fodrin was found to be a member of the spectrin family of proteins, and the spectrin nomenclature is now normally used (3). Spectrins form tetramers of two alpha and two beta subunits, with the alpha corresponding to the lower molecular weight ~240kDa band and the beta corresponding to the ~260kDa or in some case much larger band. The alpha-II subunit is widely expressed in tissues but, in the nervous system, is found predominantly in neurons. The antibody can therefore be used to identify neurons and fragments derived from neuronal membranes in cells in tissue culture and in sectioned material.
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CENCO® Mechanics System Kits, 1 and 2
Supplier: Wards
The CENCO® Mechanics System Kits include activities in mechanics and fluid mechanics topics.
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TRITON™ X-100 (Polyethylene glycol tert-octylphenyl ether)
Supplier: MP Biomedicals
Triton® X-100 is an alkylaryl polyether alcohol. It is a nonionic surfactant prepared by the reaction of octylphenol with ethylene oxide. The number ("-100") relates only indirectly to the number of ethylene oxide units in the structure.
Triton X-100 is a non-ionic surfactant and emulsifier which is often used in biochemical applications to solubilize proteins. Triton X-100 has no antimicrobial properties. It is considered as a comparatively mild detergent, non-denaturing, and is reported in numerous references as a routinely added reagent. It does absorb in the ultraviolet region of the spectrum, however, so can interfere with protein quantitation.
The principal uses of Triton® X-100 is in industrial and household detergent applications and in emulsifying agents. It is employed in almost every type of liquid, paste, and powdered cleaning compound, ranging from heavy-duty industrial products to gentle detergents for fine fabrics. It is also important ingredient of primary emulsifier mixtures used in the manufacture of emulsion polymers, stabilizers in latex polymers, and emulsifiers for agricultural emulsion concentrates, and wettable powders.
Widely used non-ionic surfactant for recovery of membrane components under mild non-denaturing conditions.
Store at Room Temperature(15-30 °C)
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Anti-BDNF Mouse Monoclonal Antibody [clone: 4C8]
Supplier: Biosensis
BDNF belongs to the neurotrophin family and promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it. It is a major regulator of synaptic transmission and plasticity at adult synapses in many regions of the CNS. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (LTP), long-term depression (LTD), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability. The alterations in BDNF expression induced by various kinds of brain insult including stress, ischemia, seizure activity and hypoglycemia, may contribute to some pathologies such as depression, epilepsy, Alzheimer's, and Parkinson's disease. Microglia release BDNF that may contribute to neuroinflammation and neuropathic pain. SUBUNIT: Monomers and homodimers. Binds to NTRK2/TRKB. SUBCELLULAR LOCATION: Secreted protein. POst translation modification: Converted into mature BDNF by plasmin (PLG). SIMILARITY: Belongs to the NGF-beta family. Antibody reacts with human, mouse, rat, guinea pig BDNF. Expected to detect BDNF from other species due to sequence homology.
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Anti-BDNF Mouse Monoclonal Antibody [clone: 4C8]
Supplier: Biosensis
BDNF belongs to the neurotrophin family and promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it. It is a major regulator of synaptic transmission and plasticity at adult synapses in many regions of the CNS. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (LTP), long-term depression (LTD), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability. The alterations in BDNF expression induced by various kinds of brain insult including stress, ischemia, seizure activity and hypoglycemia, may contribute to some pathologies such as depression, epilepsy, Alzheimer's, and Parkinson's disease. Microglia release BDNF that may contribute to neuroinflammation and neuropathic pain. SUBUNIT: Monomers and homodimers. Binds to NTRK2/TRKB. SUBCELLULAR LOCATION: Secreted protein. POst translation modification: Converted into mature BDNF by plasmin (PLG). SIMILARITY: Belongs to the NGF-beta family. Antibody reacts with human, mouse, rat, guinea pig BDNF. Expected to detect BDNF from other species due to sequence homology.
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Zirconyl chloride octahydrate 98%
Supplier: Thermo Scientific Chemicals
2.5KG
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Anti-Kv2.1 Polyclonal Antibody
Supplier: Boster Biological Technology
Polyclonal antibody for KV2.1/KCNB1 detection. Host: Rabbit.Size: 100μg/vial. Tested applications: IHC-P. Reactive species: Human. KV2.1/KCNB1 information: Molecular Weight: 95878 MW; Subcellular Localization: Cell membrane . Perikaryon . Cell projection, axon . Cell projection, dendrite . Membrane; Multi-pass membrane protein. Cell junction, synapse, postsynaptic cell membrane . Cell junction, synapse . Cell junction, synapse, synaptosome . Lateral cell membrane . Cell membrane, sarcolemma . Localizes to high-density somatodendritic clusters and non-clustered sites on the surface of neocortical and hippocampal pyramidal neurons in a cortical actin cytoskeleton-dependent manner (PubMed:24477962). Localizes also to high-density clusters in the axon initial segment (AIS), at ankyrin-G-deficient sites, on the surface of neocortical and hippocampal pyramidal neurons (PubMed:24477962). KCNB1-containing AIS clusters localize either in close apposition to smooth endoplasmic reticulum cisternal organelles or with GABA-A receptor-containing synapses of hippocampal and cortical pyramidal neurons, respectively (PubMed:24477962). Localizes to high-density clusters on the cell surface of atrial and ventricular myocytes and at the lateral plasma membrane in epithelial cells. Localizes both to the axial and transverse tubules (T tubule) and sarcolemma in ventricular myocytes. Associated with lipid raft domains. In cortical neurons, apoptotic injuries induce de novo plasma membrane insertion in a SNARE-dependent manner causing an apoptotic potassium current surge; Tissue Specificity: Expressed in neocortical pyramidal cells (PubMed:24477962). Expressed in pancreatic beta cells (at protein level) (PubMed:12403834, PubMed:14988243). Expressed in brain, heart, lung, liver, colon, kidney and adrenal gland (PubMed:19074135). Expressed in the cortex, amygdala, cerebellum, pons, thalamus, hypothalamus, hippocampus and substantia nigra (PubMed:19074135).
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VICTOR® Nivo™ Plate Readers, Multi-Mode
Supplier: REVVITY HEALTH SCIENCES, INC.
The VICTOR® Nivo™ system packs all popular detection modes into the industry’s smallest multimode reader footprint. The perfect microplate reader for everyday biochemical assays, cell-based assays, molecular biology and immunoassays. Its software interface is easy to learn and use, and lets you control the instrument from almost any device – perfect for multiuser labs. The VICTOR Nivo is a high-performance multimode microplate reader that can be equipped with all major detection technologies: Absorbance, Luminescence, Fluorescence, Time-Resolved Fluorescence, TR-FRET, Fluorescence Polarization, and Alpha Technology.
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SP Scientific miVac Concentrator Chambers, Pumps, and Traps, Genevac
Supplier: Genevac
miVac Centrifugal Evaporation Systems provide a compact, high performing solution for removing water and organic solvents from a variety of sample formats. Configure a system to meet your application requirements.
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L(+)-Histidine monohydrochloride monohydrate cell culture reagent
Supplier: Thermo Scientific Chemicals
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