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Catalog Number: (BOSSBS-1967R-A647)
Supplier: Bioss
Description: Kallikrein 9, also known as Kallikrein-Like 3 (KLK-L3), is a chymotrypsin-like serine proteinase. Kallikrein 9 was discovered as the locus for kallikreins on chromosome 19 was more fully mapped and found by similarity to the other tissue kallikreins. Kallikrein 9 has been found in the ovary, thymus, testis, prostate, skin, breast and neuronal tissues and is made by many cell lines in culture. Kallikrein 9 levels in breast cancer and uterine cancer patients have been reported to drop as the disease progresses, thus hK9 might be considered a favorable prognostic marker. Different splice variants of hK9 have been reported, although it is not yet known if they produce functional proteins. The full length Kallikrein 9 encodes for a 250 amino acid protein, with a predicted mass of 27.5 kDa and a pI of 7.53. The 234 amino acid form predicts a protein of 26 kDa with a pI of 9.76 and this quite basic pI might give the shorter form a very different function or localization. The shorter sequence also diverges before the catalytic serine residue, making it unlikely to be proteolytically active. Pre-pro-kallikrein 9 has the 17 amino acid signal sequence is removed before secretion, and the Pro-kallikrein 9 is activated to Kallikrein 9 by removal of the 5 amino acid propeptide domain.
UOM: 1 * 100 µl


Catalog Number: (BSENC-1700-100)
Supplier: Biosensis
Description: The heat shock proteins were discovered, as the name suggests, since they are heavily upregulated when cells are stressed by temperatures above the normal physiological range. They are expressed in unstressed cells also and have a normal function as chaperones, helping other proteins to fold correctly, and are required in much greater amounts if the cell or tissue is stressed by heat. The increased levels are generated transcriptionally under the influence of a powerful transcription factor, the heat shock factor 1 (HSF1). The different heat shock proteins were originally named based on their SDS-PAGE mobility, so HSP27 has an apparent molecular weight of 27kDa. It is an abundant protein even under non-stress conditions and frequently shows up as a major spot on 2 dimensional gels of cells or tissues. It is known to associate with a variety of other proteins such as actin, intermediate filament subunits and ubiquitin and is found both in the cytoplasm and the nucleus of cells. HSP27 can become heavily phosphorylated under the influence of multiple protein kinases particularly as a result of activation of the p38/SAPK pathway. Upregulation of this protein is protective against neurodegenerative diseases at least in certain mouse models (1). Point mutations in the HSP27 gene are associated with two neurological diseases, Charcot-Marie-Tooth disease type 2F and distal hereditary motor neuropathy IIB (2). These diseases are associated with axonal loss apparently following defects in the transport of neurofilaments.
UOM: 1 * 100 µl


Catalog Number: (PRSI4293)
Supplier: ProSci Inc.
Description: DISC1 Antibody: Disrupted in schizophrenia 1 (DISC1) is a candidate gene for susceptibility to schizophrenia. It was discovered through chromosomal analysis of a large Scottish family whose members exhibited schizophrenia and related psychiatric disorders. Through yeast two-hybrid screening, it was discovered that DISC1 interacts with many members of the centrosome and cytoskeletal system including MAP1A and Nudel. More recently, DISC1 has been found to regulate the transport of a complex containing Nudel, the lissencephaly-1 (LIS1) protein, and 14-3-3epsilon from neuronal cell bodies to the axons by the action of the microtubule-dependent directed motor protein kinesin-1, also known as KIF5A. Decreased expression of DISC1 in neurons caused an accelerated rate of neuronal integration, resulting in aberrant morphological development, suggesting that DISC1 plays a role in dendritic development and synapse formation. DISC1 has at least four known isoforms.
UOM: 1 * 100 µG


Catalog Number: (PRSI6649)
Supplier: ProSci Inc.
Description: SFTS Virus HB29 Antibody: Severe fever with thrombocytopenia syndrome (SFTS) is an emerging infectious disease caused by SFTS virus, a newly discovered bunyavirus that can cause high rates of fatalities. This disease is thought to be transmitted through blood contact. The SFTS virus HB29 membrane glycoprotein polyprotein mRNA encodes two glycoproteins termed Phlebovirus glycoprotein G1 and G2 respectively. This antibody will detect the non-cleaved glycoprotein.
UOM: 1 * 100 µG


Catalog Number: (PRSIXP-5195)
Supplier: ProSci Inc.
Description: Interleukin 6 (IL-6) is a multifunctional 24 kDa protein originally discovered in the medium of RNA stimulated fibroblastoid cells. It is upregulated by IL1, TNF, PDGF, IFN beta, TNF alpha, NGF, IL17 and downregulated by glucocorticoids IL4, TGF beta. IL-6 appears to be directly involved in the responses that occur after infection and cellular injury, and it may prove to be as important as IL1 and TNF alpha in regulating the acute phase response. IL-6 has also been implicated in regulating adipose mass.
UOM: 1 * 100 µG


Catalog Number: (PRSI91-933)
Supplier: ProSci Inc.
Description: CD320 antigen is also known as 8D6 antigen,FDC-signaling molecule 8D6,Transcobalamin receptor and 8D6A. It is a single-pass type I membrane protein and containing two LDL-receptor class A domains. CD320 has been recently discovered and reported as a follicular dendritic cell (FDC) protein. CD320 can augments the proliferation of plasma cells precursors generated by IL-10. CD320 also founctions a receptor for the cellular uptake of transcobalamin bound cobalamin. Defects in CD320 are the cause of methylmalonic aciduria type TCblR (MMATC) which is a metabolic disorder.
UOM: 1 * 50 µG


Catalog Number: (PRSI7515)
Supplier: ProSci Inc.
Description: AIMP2 was initially identified as a part of an aminoacyl-tRNA synthesase complex. It was later discovered to be a cofactor and substrate of Parkin, a Ring-type E3 ubiquitin ligase that is important for the survival of dopamine neurons in Parkinson’s disease; accumulation of AIMP2 in these cells lead to catecholaminergic cell death. AIMP2 can also bind to TRAF2, a key player in the TNF-alpha signaling pathway, causing the ubiquitination of TRAF2 by cIAP1, leading to TNF-alpha-dependent apoptosis. Finally, AIMP2 has been suggested to function as a tumor suppressor.
UOM: 1 * 100 µG


Catalog Number: (BOSSBS-13157R-A555)
Supplier: Bioss
Description: Src is the human homolog of the v-Src gene of the rous sarcoma virus, also designated avian sarcoma virus or ASV. Src was the first proto-oncogenic non-receptor tyrosine kinase characterized in human. The Src family, which has common structural motifs, is composed of nine members in vertebrates, including Src, Yes, Fgr, Frk, Fyn, Lyn, Hck, Lck and Blk. Src-family kinases transduce signals that are involved in the control of a variety of cellular processes, including proliferation, differentiation, motility and adhesion. Src-family ki-nases contain an amino-terminal cell membrane anchor followed by an SH3 domain and an SH2 domain, which are involved in modular association and activation, respectively. Src-family kinases, which are normally maintained in an inactive state and can be activated transiently during cellular events such as mitosis. Different subcellular localizations of Src-family kinases may be important for the regulation of specific cellular processes such as mitogenesis, cytoskeletal organization and membrane trafficking. c-Fgr is a human non-receptor tyrosine kinase family member that was discovered by using a probe toward the v-Fgr portion of the cell-derived domain of Gardner-Rasheed feline sarcoma virus. The human c-Fgr gene encodes a 529 amino acid protein.
UOM: 1 * 100 µl


Catalog Number: (PRSI6651)
Supplier: ProSci Inc.
Description: SFTS Virus HB29 Antibody: Severe fever with thrombocytopenia syndrome (SFTS) is an emerging infectious disease caused by SFTS virus, a newly discovered bunyavirus that can cause high rates of fatalities. This disease is thought to be transmitted through blood contact. The SFTS virus HB29 membrane glycoprotein polyprotein mRNA encodes two glycoproteins termed Phlebovirus glycoprotein G1 and G2 respectively. This antibody will detect the glycoprotein G2.
UOM: 1 * 100 µG


Catalog Number: (ENZOALX210279R100)
Supplier: ENZO LIFE SCIENCES
Description: SNAP-25 (synaptosomal associated protein of 25kDa) is a soluble protein of 25kDa which plays a key role in vesicle membrane fusion events with the plasma membrane. This protein was originally discovered to be enriched in subsets of neurons in the brain and displays a presynaptic pattern of expression. The membrane proteins SNAP-25, synaptobrevin, and syntaxin form the core of a ubiquitous membrane fusion machine that interacts with the soluble proteins NSF and α-SNAP. Functional interactions have been demonstrated to exist between SNAP-25, syntaxin, and the synaptic protein interaction site on voltage-sensitive L- and N-type Ca2+ channels. SNAP-25 has been shown to be required for synaptic vesicle fusion with the plasma membrane during release of NGF. Regulated exocytosis of cortical granule secretion in fertilized eggs and membrane fusion events in neurons and endocrine cells is mediated by SNAP-25 in a Ca2+-dependent mechanism. SNAP-25 protein levels have been shown to be elevated in prolactinoma and GH/PRL tumor cells while reduced SNAP-25 protein expression has been observed between schizophrenic and normal hippocampal cells. Altered patterns of SNAP-25 expression have also been observed in the inferior temporal cortex and prefrontal association cortex between normal brains and brains from individuals affected with schizophrenia. SNAP-25 accumulation due to cytoskeletal dysfunction is also observed in the swollen axons of the white matter of individuals with severe Alzheimer's dementia.
UOM: 1 * 100 µl


Catalog Number: (PRSI3809)
Supplier: ProSci Inc.
Description: TIM-1 Antibody: The human form of TIM-1 was initially discovered as a membrane glycoprotein through which the hepatitis A virus can gain entry into a cell. It was also identified as kidney injury molecule 1 (Kim-1), a predicted adhesion molecule that is upregulated on the surfaces of kidney epithelia. It is also expressed on T helper 2 (Th2) cells of the immune system, and following the binding of its natural ligand TIM-4, stimulates T cell expansion and cytokine production in response to viral challenge. It has been suggested that hyperactivation of TIM-1 leads to an increased level of Th2 responsiveness and asthma susceptibility, and antibodies to TIM-1 may therefore be a novel approach to treating asthma.
UOM: 1 * 100 µG


Catalog Number: (BOSSBS-7594R-A750)
Supplier: Bioss
Description: Ankyrins are a family of proteins that link the integral membrane proteins to the underlying spectrin-actin cytoskeleton and play key roles in activities such as cell motility, activation, proliferation, contact and the maintenance of specialised membrane domains. Multiple isoforms of ankyrin with different affinities for various target proteins are expressed in a tissue-specific, developmentally regulated manner. Most ankyrins are typically composed of three structural domains: an amino-terminal domain containing multiple ankyrin repeats; a central region with a highly conserved spectrin binding domain; and a carboxy-terminal regulatory domain which is the least conserved and subject to variation. Ankyrin 1, the prototype of this family, was first discovered in the erythrocytes, but since has also been found in brain and muscles. Mutations in erythrocytic ankyrin 1 have been associated in approximately half of all patients with hereditary spherocytosis. Complex patterns of alternative splicing in the regulatory domain, giving rise to different isoforms of ankyrin 1 have been described. Truncated muscle-specific isoforms of ankyrin1 resulting from usage of an alternate promoter have also been identified.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-7594R-CY5)
Supplier: Bioss
Description: Ankyrins are a family of proteins that link the integral membrane proteins to the underlying spectrin-actin cytoskeleton and play key roles in activities such as cell motility, activation, proliferation, contact and the maintenance of specialized membrane domains. Multiple isoforms of ankyrin with different affinities for various target proteins are expressed in a tissue-specific, developmentally regulated manner. Most ankyrins are typically composed of three structural domains: an amino-terminal domain containing multiple ankyrin repeats; a central region with a highly conserved spectrin binding domain; and a carboxy-terminal regulatory domain which is the least conserved and subject to variation. Ankyrin 1, the prototype of this family, was first discovered in the erythrocytes, but since has also been found in brain and muscles. Mutations in erythrocytic ankyrin 1 have been associated in approximately half of all patients with hereditary spherocytosis. Complex patterns of alternative splicing in the regulatory domain, giving rise to different isoforms of ankyrin 1 have been described. Truncated muscle-specific isoforms of ankyrin1 resulting from usage of an alternate promoter have also been identified. [provided by RefSeq, Dec 2008].
UOM: 1 * 100 µl


Catalog Number: (BSENM-026-50-AT)
Supplier: Biosensis
Description: 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 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 has a potential use as the ligand for gene delivery into p75NTR-expressing rat cells via a receptor-mediated mechanism.
This antibody reacts with rat only. Does not react with mouse or human NGFR
UOM: 1 * 50 µG


Catalog Number: (BOSSBS-8682R-HRP)
Supplier: Bioss
Description: The activation of RaP1 by cAMP is independent of PKA and is mediated by recently discovered family of guanine nucleotide exchange factors (GEFs) called cAMP-GEFs or Epacs. The Epac signaling therefore represents a novel mechanism for cAMP signaling with in the cAMP cascade. There are 2 members of the Epac family, Epac1 and Epac 2. Both proteins are multidomain proteins containing an autoinhibitory cAMP-binding domain that inhibits the catalytic region and a DEP domain (dishevelled, Egl-10 and pleckstrin homology domain) targeting the membrane anchors. EPAC2 has an additional cAMP-binding site in its N-terminus that binds cAMP with low affinity. EPAC1 mRNA is broadly expressed, with particularly high levels occurring in the thyroid, ovary, kidney and certain brain regions, whereas expression of EPAC2 mRNA appears to be restricted to the brain and adrenal glands. Epac 1 and Epac 2 also interact with light chain 2 (LC2) or MAP1A that serves as a scaffolding structure to stabilize the signal transduction complex. The Epac 1-selective were generated against unique antigenic sequences form near N-terminus and between RasGEFN and Ras GEF domains. The to Epac 1are affinity purified over immobilized antigen based chromatography.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-0022R-CY5)
Supplier: Bioss
Description: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK1/ERK2 and MAPK3/ERK1 are the 2 MAPKs which play an important role in the MAPK/ERK cascade. They participate also in a signaling cascade initiated by activated KIT and KITLG/SCF. Depending on the cellular context, the MAPK/ERK cascade mediates diverse biological functions such as cell growth, adhesion, survival and differentiation through the regulation of transcription, translation, cytoskeletal rearrangements. The MAPK/ERK cascade plays also a role in initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors. About 160 substrates have already been discovered for ERKs. Many of these substrates are localized in the nucleus, and seem to participate in the regulation of transcription upon stimulation. However, other substrates are found in the cytosol as well as in other cellular organelles, and those are responsible for processes such as translation, mitosis and apoptosis. Moreover, the MAPK/ERK cascade is also involved in the regulation of the endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC); as well as in the fragmentation of the Golgi apparatus during mitosis.
UOM: 1 * 100 µl


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