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Cathelicidin antimicrobial peptide Antibody - Mouse Anti-human neutrophil CAP-18 0.1ml
Cathelicidin antimicrobial protein is an antimicrobial protein found in specific granules of polymorphonuclear leukocytes (PMNs)
£226.00

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GAD65 Antibody- Mouse Anti-GAD65
Glutamic Acid Decarboxylase (GAD) catalyzes the conversion of L glutamate to g-aminobutyric acid (GABA), the principal inhibitory neurotransmitter in the brain, and a putative paracrine signal molecule in pancreatic islets. GAD has a restricted tissue distribution. It is highly expressed in the cytoplasm of GABAergic neurons in the central nervous system (CNS) and pancreatic beta cells. It is also present in other non-neuronal tissues such as testis, oviduct and ovary. GAD is also transiently expressed in non-GABAergic cells of the embryonic and adult nervous system, suggesting its involvement in development and plasticity. GAD exists as two isoforms, GAD65 and GAD67 (molecular masses of 65 and 67 kD, respectively) that are encoded by two different genes. GAD65 is an ampiphilic, membraneanchored protein, (585 amino acid residues) and is encoded on human chromosome 10. GAD67 is a cytoplasmic protein (594 amino acid residues) and is encoded on chromosome 2. There is 64% amino acid identity between the two isoforms, with the highest diversity located at the N terminus, which in GAD65 is required for targeting the enzyme to GABA-containing secretory vesicles. The two isoforms appear to have distinct intraneuronal distribution in the brain. GAD65 has been identified as an autoantigen in insulindependent diabetes mellitus (IDDM) and stiff-man syndrome (SMS), IDDM is an autoimmune disease that results from T cell mediated destruction of pancreatic insulin-secreting beta cells. Islet-reactive T cells and antibodies primarily to GAD65 (also named beta cell autoantigen) can be detected in peripheral blood of 80% of recent-onset IDD patients and in pre-diabetic high-risk subjects before onset of clinical symptoms. This suggests that GAD may be an important marker in the early stages of the disease. Also, autoantibodies to GAD65 and GAD67 are detected in animal models of IDDM, including the non-obese diabetes (NOD) mouse. In the NOD mouse, T cell reactivity is initially restricted to the C terminal regions of GAD65, but later spreads to other parts of GAD65. Stiff-man syndrome (SMS), a rare disorder of the CNS, is characterized by progressive rigidity of the body musculature with painful spasms, due to impairment of the GABAergic neurotransmission. High-titer autoantibodies directed against GAD 65 and GABAergic neurons (nerve terminals) have been detected in the serum and cerebrospinal fluid (CSF) in 60% of patients with the syndrome. Strikingly, many of the SMS patients also developed late-onset IDDM.
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HEF 1/Cas-L (NEDD9)Antibody - Mouse Anti-HEF-1/Cas-L
HEF1 is a multifunctional protein involved in integrin-based signaling that affects cell motility growth apoptosis and oncogenic transformation The Cas family of docking proteins have been the subject of intense research because of their role in cell motility growth apoptosis and oncogenic transformation These proteins are substrates of focal adhesion kinase (FAK) and the Src family of tyrosine kinases two active targets for drug development HEF1 protein production increases levels of mRNA transcripts that encode proteins associated with motility cell transformation and invasiveness including several metalloproteinases MLCK p160ROCK and ErbBi HEF1 overproduction also mediates apoptosis in epithelial-derived cell lines including MCF7 and HeLa cells Recent clinical studies at another institution have found that overexpression of BCAR1 (p130Cas) a related protein is associated with tamoxifen resistance This highlights the importance of studying the role of this family of proteins in cancer prognosis
£226.00

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HEF-1/ Cas-L Antibody- Mouse Anti-HEF-1/ Cas-L
HEF1 is a multifunctional protein involved in integrin-based signaling that affects cell motility growth apoptosis and oncogenic transformation The Cas family of docking proteins have been the subject of intense research because of their role in cell motility growth apoptosis and oncogenic transformation These proteins are substrates of focal adhesion kinase (FAK) and the Src family of tyrosine kinases two active targets for drug development HEF1 protein production increases levels of mRNA transcripts that encode proteins associated with motility cell transformation and invasiveness including several metalloproteinases MLCK p160ROCK and ErbBi HEF1 overproduction also mediates apoptosis in epithelial-derived cell lines including MCF7 and HeLa cells Recent clinical studies at another institution have found that overexpression of BCAR1 (p130Cas) a related protein is associated with tamoxifen resistance This highlights the importance of studying the role of this family of proteins in cancer prognosis
£183.00

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HEF-1/ Cas-L Antibody- Mouse Anti-HEF-1/ Cas-L
HEF1 is a multifunctional protein involved in integrin-based signaling that affects cell motility growth apoptosis and oncogenic transformation The Cas family of docking proteins have been the subject of intense research because of their role in cell motility growth apoptosis and oncogenic transformation These proteins are substrates of focal adhesion kinase (FAK) and the Src family of tyrosine kinases two active targets for drug development HEF1 protein production increases levels of mRNA transcripts that encode proteins associated with motility cell transformation and invasiveness including several metalloproteinases MLCK p160ROCK and ErbBi HEF1 overproduction also mediates apoptosis in epithelial-derived cell lines including MCF7 and HeLa cells Recent clinical studies at another institution have found that overexpression of BCAR1 (p130Cas) a related protein is associated with tamoxifen resistance This highlights the importance of studying the role of this family of proteins in cancer prognosis
£226.00

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HEF-1/Cas-L (NEDD9) Antibody- Mouse Anti-HEF-1/Cas-L
HEF1 is a multifunctional protein involved in integrin-based signaling that affects cell motility growth apoptosis and oncogenic transformation The Cas family of docking proteins have been the subject of intense research because of their role in cell motility growth apoptosis and oncogenic transformation These proteins are substrates of focal adhesion kinase (FAK) and the Src family of tyrosine kinases two active targets for drug development HEF1 protein production increases levels of mRNA transcripts that encode proteins associated with motility cell transformation and invasiveness including several metalloproteinases MLCK p160ROCK and ErbBi HEF1 overproduction also mediates apoptosis in epithelial-derived cell lines including MCF7 and HeLa cells Recent clinical studies at another institution have found that overexpression of BCAR1 (p130Cas) a related protein is associated with tamoxifen resistance This highlights the importance of studying the role of this family of proteins in cancer prognosis
£183.00

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Ndfip1 Antibody- Hamster Anti-Ndfip1
Ndfip1 belongs to a small group of evolutionarily conserved proteins with three transmembrane domains. It is a potential target for ubiquitination by the Nedd4 family of proteins. This protein is thought to be part of a family of integral Golgi membrane proteins
£183.00

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Ndfip1 Antibody- Hamster Anti-Ndfip1
Ndfip1 belongs to a small group of evolutionarily conserved proteins with three transmembrane domains. It is a potential target for ubiquitination by the Nedd4 family of proteins. This protein is thought to be part of a family of integral Golgi membrane proteins
£226.00

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NEK2 Antibody- Sheep Anti-NEK2
NEK2 is closely related in its catalytic domain to the serine/threonineprotein kinase NIMA of Aspergillus nidulans which is required for entry into mitosis and may function in parallel to the universal mitotic inducer p34cdc2. Like NIMA, the Nek2 protein is almost undetectable during G1 but accumulates progressively throughout S, reaching maximal levels in late G2. These observations demonstrate that NEK2 resembles Aspergillus NIMA, both in its catalytic domain, and cell cycle-dependent expression. Recombinant NEK2 is active as a serine/threonine-specific protein kinase and may undergo autophosphorylation. Both human NEK2 and fungal NIMA phosphorylate a similar, but not identical, set of proteins and synthetic peptides. NEK2 is shown to be expressed most abundantly in adult testis and there is increasing evidence that NEK2 is abnormally expressed in a wide variety of human cancers
£226.00

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Nesprin 1 Antibody- Rabbit Anti-Human Nesprin 1
There are two genes encoding members of a new family of type II integral membrane proteins Both are ubiquitously expressed and tissue-specific alternative mRNA initiation and splicing generate at least two major isoforms of each protein with the smaller isoforms being truncated at the N-terminusThese proteins are called Nesprin l and 2 for nuclear envelope spectrin repeat as they are characterized by the presence of multiple clustered spectrin repeats bipartite nuclear localization sequences and a conserved C-terminal single transmembrane domain Transient transfection of EGFP-fusion expression constructs demonstrated their localization to the nuclear membrane with a novel C-terminal TM domain-containing sequence essential for perinuclear localization Nesprin l is developmentally regulated in both smooth and skeletal muscle and is relocalized from the nuclear envelope to the nucleus and cytoplasm during C2Cl2 myoblast differentiation Nesprins may function as dystrophins of the nucleus to maintain nuclear organization and structural integrity There are two genes encoding members of a new family of type II integral membrane proteins Both are ubiquitously expressed and tissue-specific alternative mRNA initiation and splicing generate at least two major isoforms of each protein with the smaller isoforms being truncated at the N-terminusThese proteins are called Nesprin l and 2 for nuclear envelope spectrin repeat as they are characterized by the presence of multiple clustered spectrin repeats bipartite nuclear localization sequences and a conserved C-terminal single transmembrane domain Transient transfection of EGFP-fusion expression constructs demonstrated their localization to the nuclear membrane with a novel C-terminal TM-domain-containing sequence essential for perinuclear localization Nesprin l is developmentally regulated in both smooth and skeletal muscle and is relocalized from the nuclear envelope to the nucleus and cytoplasm during C2Cl2 myoblast differentiation Nesprins may function as dystrophins of the nucleus to maintain nuclear organization and structural integrity
£226.00

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Nesprin1 Antibody - Mouse Anti-Nesprin1
There are two genes encoding members of a new family of type II integral membrane proteins. Both are ubiquitously expressed, and tissue-specific alternative mRNA initiation and splicing generate at least two major isoforms of each protein, with the smaller isoforms being truncated at the N-terminus.These proteins are called Nesprin l and 2 for nuclear envelope spectrin repeat, as they are characterized by the presence of multiple, clustered spectrin repeats, bipartite nuclear localization sequences and a conserved C-terminal, single transmembrane domain. Transient transfection of EGFP-fusion expression constructs demonstrated their localization to the nuclear membrane with a novel C-terminal, TM domain-containing sequence essential for perinuclear localization. Nesprin l is developmentally regulated in both smooth and skeletal muscle and is relocalized from the nuclear envelope to the nucleus and cytoplasm during C2Cl2 myoblast differentiation. Nesprins may function as "dystrophins of the nucleus" to maintain nuclear organization and structural integrity. There are several different isoforms
£226.00

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Nesprin2 Antibody - Mouse Anti-Nesprin2
Nesprin 2 is involved in the maintenance of nuclear organization and structural integrity. It interacts with the nuclear envelope and with F-actin in the cytoplasm, thereby connecting nuclei to the cytoskeleton
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Nesprin2 Antibody - Rabbit Anti-Nesprin2
Nesprin 2 is involved in the maintenance of nuclear organization and structural integrity. It interacts with the nuclear envelope and with F-actin in the cytoplasm, thereby connecting nuclei to the cytoskeleton
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Nesprin3 Antibody - Rabbit Anti-Nesprin3
Component of SUN-protein-containing multivariate complexes also called LINC complexes which link the nucleoskeleton and cytoskeleton by providing versatile outer nuclear membrane attachment sites for cytoskeletal filaments. Involved in the maintenance of nuclear organization and structural integrity. Probable anchoring protein which tethers the nucleus to the cytoskeleton by binding PLEC which can associate with the intermediate filament system
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Nestin Antibody- Mouse Anti-Nestin
Nestin is a Class VI intermediate filament expressed in the developing central nervous system (CNS) in early embryonic neuroepithelial stem cells This protein has been widely used as a predominant marker for stem / progenitor cells glioma cells and tumor endothelial cells in the mammalian CNS Furthermore it is a superior angiogenic marker to evaluate neovascularity of endothelial cells in tumor This highly specific antibody to human nestin can aid in characterizing progenitor cells differentiating into distinct lineages in enhancing the therapeutic potential of human neural stem/progenitor cells in the treatment of CNS diseases or injury and in identifying neuroepithelial tumor cells
£183.00

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Neurocan Antibody- Mouse Anti-Neurocan
Neurocan is the major soluble chondroitin sulfate proteoglycan in the brain It is thought to play a functional role in axonal growth and guidance and in the establishment of specific neural pathways during embryonic brain development Neurocan expression in the brain is developmentally regulated Early on the major form of neurocan consists of a 245kD core protein with approximately two chondroitin sulfate glycosoaminoglycan chains of 22kD each Later neurocan comprises a 180kD core protein Both forms of neurocan contain only chondroitin 4-sulfate glycosoaminoglycan chains By virtue of their high expression at sites of neural damage and trauma chondroitin sulfate proteoglycans including neurocan are thought to inhibit successful nerve regeneration
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