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Cytokeratin (keratin) K2 (AE3) Antibody- Mouse Anti-Cytokeratin (keratin) K2 (AE3)
Cytokeratins, a group of at least 29 different proteins, are characteristic of epithelial and trichocytic cells. Cytokeratins 4, 5, 6 and 8 are members of the type II neutral-to-basic subfamily. Cytokeratin peptide 4 (59 kDa) is the secondary type II keratin expressed in non cornified stratified squamous epithelia. Cytokeratin peptide 5 (58 kDa) is the primary type II keratin in stratified epithelia, while cytokeratin type 8 (52 kDa) is a major type II keratin in simple epithelia. Cytokeratin 6 (56 kDa) is a "hyperproliferation" cytokeratin expressed in tissues with natural or pathological high turnover. Cytokeratins 10, 13 and 18 are members of the type I acidic subfamily. Cytokeratin peptide 10 (56 kDa) is the secondary type I keratin expressed in cornified epithelia. Cytokeratin 13 (54 kDa) is the secondary type I keratin expressed in non-cornified stratified squamous epithelia. Cytokeratin 18 (45 kDa) is the primary type I keratin expressed in simple epithelial cells.
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Cytokeratin Antibody (keratin) K1 type I (AE1) - Mouse Anti-Cytokeratin (keratin) K1 type I (AE1) 0.2ml
Twenty human keratins are resolved with two-dimensional gel electrophoresis into acidic (pI <57) and basic (pI >60) subfamilies The acidic keratins have molecular weights of 565 55 51 50 50 48 46 45 and 40kDa The basic keratins have molecular weights of 65 - 67 64 59 58 56 and 52kDa Members of acidic and basic subfamilies are found together in pairs The composition of keratin pairs varies with cell type differentiation status and environment Many studies have shown the usefulness of keratins as markers in cancer research and tumor diagnosis
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Emerin Antibody- Rabbit Anti-Emerin
Emerin is a serine rich nuclear membrane protein and a member of the nuclear lamina associated protein family It mediates membrane anchorage to the cytoskeleton Dreifuss-Emery muscular dystrophy is an X-linked inherited degenerative myopathy resulting from mutation in the emerin gene
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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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gp210 (C-terminal) Antibody- Rabbit Anti-gp210 (C-terminal)
The nuclear pore complex is a massive structure that extends across the nuclear envelope, forming a gateway that regulates the flow of macromolecules between the nucleus and the cytoplasm. Nucleoporins are the main components of the nuclear pore complex in eukaryotic cells. GP210 is a membrane-spanning glycoprotein that is a major component of the nuclear pore complex, it is an evolutionarily conserved and has early roles in nuclear pore formation and mediates pore dilation with its tail-binding partners
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gp210 (N-terminal) Antibody- Rabbit Anti-gp210 (N-terminal)
The nuclear pore complex is a massive structure that extends across the nuclear envelope forming a gateway that regulates the flow of macromolecules between the nucleus and the cytoplasm Nucleoporins are the main components of the nuclear pore complex in eukaryotic cells GP210 is a membrane-spanning glycoprotein that is a major component of the nuclear pore complex it is an evolutionarily conserved and has early roles in nuclear pore formation and mediates pore dilation with its tail-binding partners
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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
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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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hnRNP-K/J Antibody- Mouse (monoclonal) Anti-hnRNP-K/J
Particulate complex of heterogeneous nuclear RNA (hnRNA) is a heterogeneous mixture of RNA molecules of high Mr with a rapid turnover rate that occurs in cell nuclei during protein synthesis with proteins which are cell specific and heterogeneous The protein component may play a role in the processing of the hnRNA to mRNA
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hnRNP-K/J Antibody- Mouse Anti-hnRNP-K/J
Particulate complex of heterogeneous nuclear RNA (hnRNA) is a heterogeneous mixture of RNA molecules of high Mr with a rapid turnover rate that occurs in cell nuclei during protein synthesis with proteins which are cell specific and heterogeneous The protein component may play a role in the processing of the hnRNA to mRNA
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Lamin A Antibody - Mouse Anti-Lamin A
Nuclear lamins form a network of intermediate-type filaments at the nucleoplasmic site of the nuclear membrane Two main subtypes of nuclear lamins can be distinguished ie A type lamins and B type lamins The A type lamins comprise a set of three proteins arising from the same gene by alternative splicing ie lamin A lamin C and lamin Adel 10 while the B type lamins include two proteins arising from two distinct genes ie lamin B1 and lamin B2 Recent evidence has revealed that mutations in A-type lamins give rise to a range of rare but dominant genetic disorders including Emery-Dreifuss muscular dystrophy dilated cardiomyopathy with conduction-system disease and Dunnigan-type familial partial lipodystrophy In addition the expression of A type lamins coincides with cell differentiation and as A type lamins specifically interact with chromatin a role in the regulation of differential gene expression has been suggested for A type lamins
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Lamin A/C Antibody- Mouse Anti-Lamin A/C
Nuclear Lamins form a network of intermediate-type filaments at the nucleoplasmic site of the nuclear membrane Two main subtypes of nuclear lamins can be distinguished ie A-type Lamins and B-type Lamins The A-type Lamins comprise a set of three proteins arising from the same gene by alternative splicing ie Lamin A Lamin C and Lamin Adel 10 while the B-type Lamins include two proteins arising from two distinct genes ie Lamin B1 and Lamin B2 Recent evidence has revealed that mutations in A-type Lamins give rise to a range of rare but dominant genetic disorders including Emery-Dreifuss muscular dystrophy dilated cardiomyopathy with conduction-system disease and Dunnigan-type familial partial lipodystrophy In addition the expression of A-type Lamins coincides with cell differentiation and as A-type Lamins specifically interact with chromatin a role in the regulation of differential gene expression has been suggested for A-type Lamins
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Lamin A/C Antibody- Mouse Anti-Lamin A/C
Nuclear Lamins form a network of intermediate-type filaments at the nucleoplasmic site of the nuclear membrane Two main subtypes of nuclear lamins can be distinguished ie A-type Lamins and B-type Lamins The A-type Lamins comprise a set of three proteins arising from the same gene by alternative splicing ie Lamin A Lamin C and Lamin Adel 10 while the B-type Lamins include two proteins arising from two distinct genes ie Lamin B1 and Lamin B2 Recent evidence has revealed that mutations in A-type Lamins give rise to a range of rare but dominant genetic disorders including Emery-Dreifuss muscular dystrophy dilated cardiomyopathy with conduction-system disease and Dunnigan-type familial partial lipodystrophy In addition the expression of A-type Lamins coincides with cell differentiation and as A-type Lamins specifically interact with chromatin a role in the regulation of differential gene expression has been suggested for A-type Lamins
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Lamin B1 + B2 Antibody- Mouse Anti-Lamin B1 + B2
Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin.
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Lamin B1 Antibody- Mouse Anti-Lamin B1
An important part of the nucleus is formed by nuclear lamina Nuclear lamins form a network of filaments at the nucleoplasmic site of the nuclear membrane Two main subtypes of nuclear lamins can be distinguished ie A type lamins and B type lamins The A type lamins comprise a set of three proteins arising from the same gene by alternative splicing ie lamin A lamin C and lamin Adel10 while the B-type lamins include two proteins arising from two distinct genes ie lamin B1 and lamin B2 The nuclear lamins comprise a unique subclass of the intermediate filament protein family They share a molecular domain organisation with the other intermediate filament proteins in that they are fibrous molecules that have an aminoterminal globular head a central rod of alpha helices and a carboxy terminal globular domain Many biochemical and molecular features of lamins have been studied but their functions remain still largely undetermined One of the functions ascribed to the lamina is the maintenance of the structural integrity of the nucleus Besides interactions with the nuclear membrane and other intermediate filaments lamins interact with the nuclear chromatin Eukaryotic chromatin is organised into loops which are attached to the nuclear matrix This organisation is thought to contribute to compaction of the chromatin and regulation of gene expression Lamins as part of the nuclear matrix may be involved in these processes since chromatin binding sites have been detected in both A and B type lamins
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Lamin C Antibody- Rabbit Anti-Lamin C
An important part of the cell nucleus is formed by nuclear lamina Nuclear lamins form a network of filaments at the nucleoplasmic site of the nuclear membrane Two main subtypes of nuclear lamins can be distinguished ie A-type lamins and B-type lamins The A-type lamins comprise a set of three proteins arising from the same gene by alternative splicing ie lamin A lamin C and lamin Adel10 while the B-type lamins include two proteins arising from two distinct genes ie lamin B1 and lamin B2 The nuclear lamins comprise a unique subclass of the intermediate filament protein family They share a molecular domain organisation with the other intermediate filament proteins in that they are fibrous molecules that have an aminoterminal globular head a central rod of a-helices and a carboxyterminal globular domain Many biochemical and molecular features of lamins have been studied but their functions remain still largely undetermined One of the functions ascribed to the lamina is the maintenance of the structural integrity of the nucleus Besides interactions with the nuclear membrane and other intermediate filaments lamins interact with the nuclear chromatin Eukaryotic chromatin is organised into loops which are attached to the nuclear matrix This organisation is thought to contribute to compaction of the chromatin and regulation of gene expression Lamins as part of the nuclear matrix may be involved in these processes since chromatin binding sites have been detected in both A- and B-type lamins
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