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Immunohistochemistry (frozen sections)

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CCR9 Antibody - Rat Anti CCR9 1ml
The protein encoded by this gene is a member of the beta chemokine receptor family It is predicted to be a seven transmembrane protein similar to G protein coupled receptors Chemokines and their receptors are key regulators of the thymocytes migration and maturation in normal and inflammation conditions This gene is expressed in a range of tissues and hemopoietic cells The expression of this receptor in lymphatic endothelial cells and overexpression in vascular tumors suggested its function in chemokine-driven recirculation of leukocytes and possible chemokine effects on the development and growth of vascular tumors This receptor appears to bind the majority of beta-chemokine family members however its specific function remains unknown The specific ligand of this receptor is CCL25 It has been found that this gene is differentially expressed by T lymphocytes of small intestine and colon suggested a role in the thymocytes recruitment and development that may permit functional specialization of immune responses in different segment of the gastrointestinal tract This gene is mapped to chromosome 3p213 a region that includes a cluster of chemokine receptor genes Two alternatively spliced transcript variants have been described
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CD34 Antibody - Mouse Anti-Human CD34
Possible adhesion molecule with a role in early hematopoiesis by mediating the attachment of stem cells to the bone marrow extracellular matrix or directly to stromal cells. Could act as a scaffold for the attachment of lineage specific glycans, allowing stem cells to bind to lectins expressed by stromal cells or other marrow components. Presents carbohydrate ligands to selectins
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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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EPCAM; CD326 Antibody- Rat Anti-EPCAM
Epithelial Cell Adhesion Molecule (EpCAM) is a 40 kDa cell surface antigen. This antigen has been identified independently by a number of groups, and has been known by a variety of names. Several monoclonal antibodies have been raised against EpCAM, many of which have been described as tumour specific molecules on carcinomas. EpCAM is a Type 1 transmembrane glycoprotein. It is expressed on the basolateral membrane of cells by the majority of epithelial tissues, with the exception of adult squamous epithelium and some specific epithelial cell types including hepatocytes and gastric epithelial cells. EpCAM expression has been reported to be a possible marker of early malignancy, with expression being increased in tumour cells, and de novo expression being seen in dysplastic squamous epithelium
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Fibronectin Antibody - Mouse Anti-Human Fibronectin
Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape.Anastellin binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling
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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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Insulin Like Growth Factor Antibody - Mouse Anti-Insulin Like Growth Factor (IGF-1)
Insulin is a pancreatic hormone that regulates glucose uptake and the synthesis of protein and fat. The insulin like growth factors, isolated from plasma, are structurally and functionally related to insulin but have a much higher growth promoting activity. IGF1 (Insulin Like Growth Factor I) is a polypeptide growth factor, which stimulates the proliferation of a wide range of cell types including muscle, bone, and cartilage tissue. IGF1 functions as an autocrine regulator of growth
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Kallikrein 2 (Hk2) Antibody- Mouse Anti-Kallikrein 2 (Hk2)
Kallikreins (KLKs) are a subgroup of trypsin-like serine proteases and are implicated in carcinogenesis Kallikrein 2 is most closely related to Kallikrein 3 (PSA) with 78 identity and with kallikrein 1 at 68 identity Like Kallikrein 3 Kallikrein 2 is found in greatest abundance in the prostate but at much lower levels than Kallikrein 3 In addition Kallikrein 2 seems to be more labile than Kallikrein 1 or Kallikrein 3 and is often found in a cleaved form Kallikrein 2 is inhibited by Protein C Inhibitor (PCI)
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Kallikrein 2 (Hk2) Antibody- Mouse Anti-Kallikrein 2 (Hk2)
Kallikreins (KLKs) are a subgroup of trypsin-like serine proteases and are implicated in carcinogenesis Kallikrein 2 is most closely related to Kallikrein 3 (PSA) with 78 identity and with kallikrein 1 at 68 identity Like Kallikrein 3 Kallikrein 2 is found in greatest abundance in the prostate but at much lower levels than Kallikrein 3 In addition Kallikrein 2 seems to be more labile than Kallikrein 1 or Kallikrein 3 and is often found in a cleaved form Kallikrein 2 is inhibited by Protein C Inhibitor (PCI)
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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 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 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 B2 Antibody- Mouse Anti-Lamin B2
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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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
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Podoplanin/gp36 Antibody- Hamster Anti-Podoplanin/gp36
May be involved in cell migration and/or actin cytoskeleton organization. When expressed in keratinocytes, induces changes in cell morphology with transfected cells showing an elongated shape, numerous membrane protrusions, major reorganization of the actin cytoskeleton, increased motility and decreased cell adhesion. Required for normal lung cell proliferation and alveolus formation at birth. Induces platelet aggregation. Does not have any effect on folic acid or amino acid transport. Does not function as a water channel or as a regulator of aquaporin-type water channels
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Retinal S-antigen (arrestin) Antibody- Mouse Anti- Retinal S-antigen
Arrestin is one of the major proteins of the ros (retinal rod outer segments); it binds to photoactivated-phosphorylated rhodopsin, thereby apparently preventing the transducin-mediated activation of phosphodiesterase.
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