6348 Results for: "Wright\'s+stain"

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The Cell-division cycle protein 20 is an essential regulator of cell division that is encoded by the CDC20 gene in humans. To the best of current knowledge its most important function is to activate the anaphase promoting complex (APC/C), a large 11-13 subunit complex that initiates chromatid separation and entrance into anaphase. The APC/C-Cdc20 protein complex has two main downstream targets. Firstly, it targets securin for destruction, enabling the eventual destruction of cohesin and thus sister chromatid separation. It also targets S and M-phase (S/M) cyclins for destruction, which inactivates S/M cyclin-dependent kinases (Cdks) and allows the cell to exit from mitosis. A closely related protein, Cdc20homologue-1 (Cdh1) plays a complementary role in the cell cycle.

Cdc20 appears to act as a regulatory protein interacting with many other proteins at multiple points in the cell cycle. It is required for two microtubule-dependent processes: nuclear movement prior to anaphase, and chromosome separation. [Wiki].

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Mucin-1 is a large cell surface mucin glycoprotein expressed by most glandular and ductal epithelial cells and some hematopoietic cell lineages. It is expressed on most secretory epithelium, including mammary gland and some hematopoietic cells. It is expressed abundantly in lactating mammary glands and over expressed in >90% breast carcinomas and metastases. The transgenic protein has been shown to associate with all four c-erbB receptors and localize with c-erbB1 (EGFR) in lactating glands. The gene contains seven exons and produces several different alternatively spliced variants. The major expressed form of the protein uses all seven exons and is a type 1 transmembrane protein with a large extracellular tandem repeat domain. The tandem repeat domain is highly O glycosylated and alterations in glycosylation have been shown in epithelial cancer cells. Mucin-1 antibody is useful as a pan-epithelial marker for detecting early metastatic loci of carcinoma in bone marrow or liver.

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This antibody recognises a protein of 205 kDa-220 kDa, identified as CD45RA, an isoform of the human leukocyte common antigen (CD45). Human CD45 contains three exons which encode peptide segments designated A, B and C. The differential splicing of the exons generates at least five isoforms, ABC, AB, BC, B and O. This antibody reacts with ABC and BC isoforms. CD45RA is expressed on 40-50% of peripheral CD4+ Tcells, 50% of peripheral CD8+ T-cells, B-cells, and leukemic B-cell lines. T-cells expressing CD45RA are naive or virgin Tcells. T-cells expressing CD45RO are memory Tcells. CD45RA and CD45RO define complementary, predominantly non-overlapping populations of resting peripheral Tcells. This CD45RA antibody is useful in the study of the subpopulation of CD4+ or CD8+ T-cells. It is especially useful in differentiating T-cell lymphomas (CD45RO +ve) from B cell lymphomas (CD45RA +ve).

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Recognises a protein of 47-55 kDa, which is identified as FOXP3. Its precise epitope is not known, but it has been mapped to the N-terminal portion of the protein. The FOX family of transcription factors is a large group of proteins that share a common DNA binding domain termed a winged-helix or forkhead domain. During early development, FOXP1 and FOXP2 are expressed abundantly in the lung, with lower levels of expression in neural, intestinal and cardiovascular tissues, where they act as transcription repressors. FOXP1 is widely expressed in adult tissues, while neoplastic cells often exhibit a dramatic change in expression level or localization of FOXP1. Mutations in FOXP3 gene cause IPEX, a fatal, X-linked inherited disorder characterised by immune dysregulation. The FOXP3 protein is essential for normal immune homeostasis. Specifically, FOXP3 represses transcription through a DNA binding forkhead domain, thereby regulating T cell activation.

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Pax genes contain paired domains with strong homology to genes in Drosophila, which are involved in programming early development. Lesions in the Pax-6 gene account for most cases of aniridia, a congenital malformation of the eye, chiefly characterised by iris hypoplasia, which can cause blindness. Pax-6 is involved in other anterior segment malformations besides aniridia, such as Peters anomaly, a major error in the embryonic development of the eye with corneal clouding with variable iridolenticulocorneal adhesions. The Pax-6 gene encodes a transcriptional regulator that recognises target genes through its paired-type DNA-binding domain. The paired domain is composed of two distinct DNA-binding subdomains, the amino-terminal subdomain and the carboxy-terminal subdomain, which bind respective consensus DNA sequences. The human Pax-6 gene produces two alternatively spliced isoforms that have the distinct structure of the paired domain.

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This mAb recognises an extracellular epitope of an integral membrane glycoprotein of 150 kDa, identified as CD13. This antigen is present on most cells of myeloid origin including granulocytes, monocytes, mast cells, and GM-progenitor cells. It is also expressed by the majority of Aml, Cml in myeloid blast crisis, and in a smaller fraction of lymphoid leukemias. It is absent from normal lymphocytes, platelets and erythrocytes. CD13 is also present on fibroblasts; endothelial cells, epithelial cells from renal proximal tubules and intestinal brush border, bone marrow stromal cells, osteoclasts, and cells lining bile duct canaliculi. CD13 is identical to aminopeptidase N (APN), a prominent membrane-bound metalloprotease present on the surface of intestinal brush border and renal tubules. CD13 plays a role in metabolism of biologically active peptides, in phagocytosis, and in bactericidal/tumoricidal activities. It also serves as a receptor for human coronaviruses (HCV). The lineage-restricted pattern of expression of CD13 within the hemopoietic compartment suggests that it may be important in myeloid cell differentiation.

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This mAb recognises granulocyte-colony stimulating factor (G-CSF) in the cytoplasm of mature granulocytes. It shows no reactivity with any other cell types. Markers of myeloid cells are useful in the identification of different levels of cellular differentiation. It reacts with early precursor and mature forms of myeloid cells. It is useful for the detection of myeloid leukemias and granulocytic sarcomas. It can be used as a marker of granulocytes in normal tissues or inflammatory processes.G-CSF is a pleiotropic cytokine that influences differentiation, proliferation and activation of the neutrophilic granulocyte lineage. The human G-CSF cDNA encodes a 207 amino acid precursor containing a 29 amino acid signal peptide that is proteolytically cleaved to form a 178 amino acid residue mature protein. Two G-CSF's, which are identical except for a three amino acid deletion in the amino-terminus of one form of the protein have been isolated from human cells. Murine and human G-CSF's share 73% sequence identity at the amino acid level.

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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.

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This antibody reacts with a protein of 22 kDa, identified as beta subunit of HCG. It does not cross react with the alpha subunit. HCG is a glycoprotein which is secreted in large quantities by normal trophoblasts. It is present only in trace amounts in non-pregnant urine and sera but rises sharply during pregnancy. HCG is composed of two non-identical, non-covalently linked polypeptide chains designated as the alpha and beta subunits. The alpha subunit is identical to that of thyroid stimulating hormone (TSH), follicle stimulating hormone (FSH), and luteinizing hormone (LH). HCG-beta antibody detects cells and tumors of trophoblastic origin such as choriocarcinoma. Large cell carcinoma and adenocarcinoma of the lung demonstrate antibody positivity in 90% and 60% of cases respectively; 20% of lung squamous cell carcinomas are positive. HCG expression by non-trophoblastic tumors may indicate aggressive behavior.

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This antibody reacts with a protein of 22 kDa, identified as beta subunit of HCG. It does not cross react with the alpha subunit. HCG is a glycoprotein which is secreted in large quantities by normal trophoblasts. It is present only in trace amounts in non-pregnant urine and sera but rises sharply during pregnancy. HCG is composed of two non-identical, non-covalently linked polypeptide chains designated as the alpha and beta subunits. The alpha subunit is identical to that of thyroid stimulating hormone (TSH), follicle stimulating hormone (FSH), and luteinizing hormone (LH). HCG-beta antibody detects cells and tumors of trophoblastic origin such as choriocarcinoma. Large cell carcinoma and adenocarcinoma of the lung demonstrate antibody positivity in 90% and 60% of cases respectively; 20% of lung squamous cell carcinomas are positive. HCG expression by non-trophoblastic tumors may indicate aggressive behavior.

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Recognises a protein of 55 kDa, which is identified as fascin-1. Its actin binding ability is regulated by phosphorylation. Antibody to fascin-1 is a very sensitive marker for Reed-Sternberg cells and variants in nodular sclerosis, mixed cellularity, and lymphocyte depletion Hodgkin's disease. It is uniformly negative in lymphoid cells, plasma cells, and myeloid cells. Fascin-1 is also expressed in dendritic cells. This marker may be helpful to distinguish between Hodgkin lymphoma and non-Hodgkin lymphoma in difficult cases. Also, the lack of expression of fascin-1 in the neoplastic follicles in follicular lymphoma may be helpful in distinguishing these lymphomas from reactive follicular hyperplasia in which the number of follicular dendritic cells is normal or increased. Antibody to fascin-1 has been suggested as a prognostic marker in neuroendocrine neoplasms of the lung as well as in ovarian cancer. Fascin-1 expression may be induced by Epstein-Barr virus (EBV) infection of B cells with the possibility that viral induction of fascin in lymphoid or other cell types must also be considered in EBV-positive cases.

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Cyclin B1 (CCNB1) is a regulatory protein involved in mitosis. The gene product complexes with p34 (Cdk1) to form the maturation-promoting factor (MPF). Cyclin B1 contributes to the switch-like all or none behavior of the cell in deciding to commit to mitosis. Its activation is well-regulated, and positive feedback loops ensure that once the CCNB1-Cdk1 complex is activated, it is not deactivated. CCNB1-Cdk1 is involved in the early events of mitosis, such as chromosome condensation, nuclear envelope breakdown, and spindle pole assembly. Once activated, CCNB1-Cdk1 promotes several of the events of early mitosis. The active complex phosphorylates and activates 13S condensin, which helps to condense chromosomes. Another important function of the complex is to break down the nuclear envelope. The nuclear envelope is a membranous structure containing large protein complexes supported by a network of nuclear lamins. Phosphorylation of the lamins by CCBN1-Cdk1 causes them to dissociate, compromising the structural integrity of the nuclear envelope so that it breaks down. The destruction of the nuclear envelope is important because it allows the mitotic spindle to access the chromosomes. [Wiki].

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This mAb reacts with MUC1/Mucin-1/Epithelial Marker Antigen/EMA. MUC1 is a large cell surface mucin glycoprotein expressed by most glandular and ductal epithelial cells and some hematopoietic cell lineages. It is expressed on most secretory epithelium, including mammary gland and some hematopoietic cells. It is expressed abundantly in lactating mammary glands and over expressed abundantly in >90% breast carcinomas and metastases. Transgenic MUC1 has been shown to associate with all four c-erbB receptors and localize with c-erbB1 (EGFR) in lactating glands. The MUC1 gene contains seven exons and produces several different alternatively spliced variants. The major expressed form of MUC1 uses all seven exons and is a type 1 transmembrane protein with a large extracellular tandem repeat domain. The tandem repeat domain is highly O glycosylated and alterations in glycosylation have been shown in epithelial cancer cells. Antibody to EMA is useful as a pan-epithelial marker for detecting early metastatic loci of carcinoma in bone marrow or liver.

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This antibody recognises a 67 kDa transmembrane protein, which is identified as CD5. The CD5 antigen is found on 95% of thymocytes and 72% of peripheral blood lymphocytes. In lymph nodes, the main reactivity is observed in T cell areas. antibody to CD5 is a pan T-cell marker that also reacts with a range of neoplastic B-cells, e.g. chronic lymphocytic leukemia/small lymphocytic lymphoma (CLL/SLL), mantle cell lymphoma, and a subset (~10%) of diffuse large B-cell lymphoma. CD5 aberrant expression is useful in making a diagnosis of mature T-cell neoplasms. CD5 antibody detection is diagnostic in CLL/SLL within a panel of other B-cell markers, especially one that includes anti-CD23. CD5 antibody is also very useful in differentiating among mature small lymphoid cell malignancies. In addition, antibody to CD5 can be used in distinguishing thymic carcinoma (+) from thymoma (-). CD5 antibody does not react with granulocytes or monocytes.

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Thyroglobulin is a 660 kDa dimeric pre-protein with mutiple glycosylation sites, detected at ~300 kDa in western blot. It is produced by and processed within the thyroid gland to produce the hormone thyroxine and triiodothyronine. Prior to forming dimers, thyroglobulin monomers undergo conformational maturation in the endoplasmic reticulation. The vast majority of follicular carcinomas of the thyroid will give positive immunoreactivity for thyroglobulin antibody even though sometimes only focally. Poorly differentiated carcinomas of the thyroid are frequently thyroglobulin antibody negative. Adenocarcinomas of other-than-thyroid origin do not react with this antibody. This antibody is useful in identification of thyroid carcinoma of the papillary and follicular types. Presence of thyroglobulin in metastatic lesions establishes the thyroid origin of tumor. Thyroglobulin antibody, combined with calcitonin antibody, can identify medullary carcinomas of the thyroid. Furthermore, thyroglobulin antibody, combined with TTF1 antibody, can be a reliable marker to differentiate between primary thyroid and lung neoplasms.

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This mAb reacts with a 58 kDa protein identified as vimentin. It shows no cross-reaction with other closely related intermediate filament proteins (IFPs) such as desmin, keratin, neurofilament, and glial fibrillary acid protein. Anti-vimentin alone is of limited value as a diagnostic tool; however, when used in panels with other antibodies, it is useful for the sub-classification of a given tumor. Expression of vimentin, when used in conjunction with anti-keratin, is helpful when distinguishing melanomas from undifferentiated carcinomas and large cell lymphomas. All melanomas and Schwannomas react strongly with anti-vimentin. It labels a variety of mesenchymal cells, including melanocytes, lymphocytes, endothelial cells, and fibroblasts. Non-reactivity of anti-vimentin is often considered more useful than its positive reactivity, since there are a few tumors that do not contain vimentin, e.g. hepatoma and seminoma. Anti-vimentin is also useful as a tissue process control reagent.

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This antibody reacts with both SUMO2 and SUMO3. The small ubiquitin-related modifier (SUMO) proteins, which include SUMO1, 2 and 3, belong to the ubiquitin-like protein family. Like ubiquitin, the SUMO proteins are synthesised as precursors that undergo processing before conjugation to target proteins. Also, both utilize the E1, E2 and E3 cascade enzymes for conjugation. However, SUMO and ubiquitin differ with respect to targeting. Ubiquitination predominantly targets proteins for degradation, whereas sumoylation targets for a variety of cellular processing, including nuclear transport, transcriptional regulation, apoptosis and protein stability. The unconjugated SUMO1/2/3 proteins localize to the nuclear membrane, nuclear bodies and cytoplasm, respectively. SUMO1 utilizes Ubc9 for conjugation to several targets, which include MDM2, p53, Pml and RanGap1. SUMO2/3 contribute to a greater percentage of protein modification than does SUMO1 and they can form polymeric chains. In addition, SUMO3 regulates beta-Amyloid generation and may be critical in the onset or progression of Alzheimer’s disease.

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Mucin-1 is a large cell surface mucin glycoprotein expressed by most glandular and ductal epithelial cells and some hematopoietic cell lineages. It is expressed on most secretory epithelium, including mammary gland and some hematopoietic cells. It is expressed abundantly in lactating mammary glands and over expressed in >90% breast carcinomas and metastases. The transgenic protein has been shown to associate with all four c-erbB receptors and localize with c-erbB1 (EGFR) in lactating glands. The gene contains seven exons and produces several different alternatively spliced variants. The major expressed form of the protein uses all seven exons and is a type 1 transmembrane protein with a large extracellular tandem repeat domain. The tandem repeat domain is highly O glycosylated and alterations in glycosylation have been shown in epithelial cancer cells. Mucin-1 antibody is useful as a pan-epithelial marker for detecting early metastatic loci of carcinoma in bone marrow or liver. The specific epitope of this Mucin-1 antibody has not yet been determined.

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This mAb recognises granulocyte-colony stimulating factor (G-CSF) in the cytoplasm of mature granulocytes. It shows no reactivity with any other cell types. Markers of myeloid cells are useful in the identification of different levels of cellular differentiation. It reacts with early precursor and mature forms of myeloid cells. It is useful for the detection of myeloid leukemias and granulocytic sarcomas. It can be used as a marker of granulocytes in normal tissues or inflammatory processes.G-CSF is a pleiotropic cytokine that influences differentiation, proliferation and activation of the neutrophilic granulocyte lineage. The human G-CSF cDNA encodes a 207 amino acid precursor containing a 29 amino acid signal peptide that is proteolytically cleaved to form a 178 amino acid residue mature protein. Two G-CSFs, which are identical except for a three amino acid deletion in the amino-terminus of one form of the protein have been isolated from human cells. Murine and human G-CSF s share 73% sequence identity at the amino acid level.

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This mAb recognises granulocyte-colony stimulating factor (G-CSF) in the cytoplasm of mature granulocytes. It shows no reactivity with any other cell types. Markers of myeloid cells are useful in the identification of different levels of cellular differentiation. It reacts with early precursor and mature forms of myeloid cells. It is useful for the detection of myeloid leukemias and granulocytic sarcomas. It can be used as a marker of granulocytes in normal tissues or inflammatory processes.G-CSF is a pleiotropic cytokine that influences differentiation, proliferation and activation of the neutrophilic granulocyte lineage. The human G-CSF cDNA encodes a 207 amino acid precursor containing a 29 amino acid signal peptide that is proteolytically cleaved to form a 178 amino acid residue mature protein. Two G-CSF's, which are identical except for a three amino acid deletion in the amino-terminus of one form of the protein have been isolated from human cells. Murine and human G-CSF's share 73% sequence identity at the amino acid level.

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This mAb is specific to heavy chain of IgA and shows minimal cross-reaction with heavy chains of other immunoglobulins. It is reactive with all subclasses of Alpha heavy chain. Immunoglobulins are four-chain, Y-shaped, monomeric structures comprised of two identical heavy chains and two identical light chains held together through inter-chain disulfide bonds. The chains form two domains, the Fab (antigen binding) fragment and the Fc (constant) fragment. Immunoglobulin A (IgA) is the main protein of the mucosal immune system. It is generated by B-cells in gut-associated lymphoid tissues. Daily production of IgA exceeds that of any of the other immunoglobulins. IgA exists mainly in dimers but can also exist as polymers or as monomers. Dimers and polymers contain a joining (J) chain that can be bound by the polymeric immunoglobulin receptor (pIgR) for transportation of the molecule to mucosal surfaces. The most common feature of plasmacytomas, and certain non-Hodgkin s lymphomas is the restricted expression of a single heavy chain class. Demonstration of clonality in lymphoid infiltrates indicates that the infiltrate is clonal and therefore malignant.

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Recognises a 67 kDa transmembrane protein, which is identified as CD5. The CD5 antigen is found on 95% of thymocytes and 72% of peripheral blood lymphocytes. In lymph nodes, the main reactivity is observed in T cell areas. Anti-CD5 is a pan T-cell marker that also reacts with a range of neoplastic B-cells, e.g. chronic lymphocytic leukemia/small lymphocytic lymphoma (CLL/SLL), mantle cell lymphoma, and a subset (~10%) of diffuse large B-cell lymphoma. CD5 aberrant expression is useful in making a diagnosis of mature T-cell neoplasms. Anti-CD5 detection is diagnostic in CLL/SLL within a panel of other B-cell markers, especially one that includes anti-CD23. Anti-CD5 is also very useful in differentiating among mature small lymphoid cell malignancies. In addition, anti-CD5 can be used in distinguishing thymic carcinoma (+) from thymoma (-). Anti-CD5 does not react with granulocytes or monocytes.

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This mAb is specific to heavy chain of IgA and shows minimal cross-reaction with heavy chains of other immunoglobulins. It is reactive with both IgA1 and IgA2 subclasses of Alpha heavy chain. It reacts with the third constant domain (CH3) of the alpha chain of IgA molecules. Immunoglobulins are four-chain, Y-shaped, monomeric structures comprised of two identical heavy chains and two identical light chains held together through inter-chain disulfide bonds. The chains form two domains, the Fab (antigen binding) fragment and the Fc (constant) fragment. Immunoglobulin A (IgA) is the main protein of the mucosal immune system. It is generated by B-cells in gut-associated lymphoid tissues. Daily production of IgA exceeds that of any of the other immunoglobulins. IgA exists mainly in dimers but can also exist as polymers or as monomers. Dimers and polymers contain a joining (J) chain that can be bound by the polymeric immunoglobulin receptor (pIgR) for transportation of the molecule to mucosal surfaces. The most common feature of plasmacytomas, and certain non-Hodgkin's lymphomas is the restricted expression of a single heavy chain class. Demonstration of clonality in lymphoid infiltrates indicates that the infiltrate is clonal and therefore malignant.

Supplier: ProSci Inc.

This mAb is specific to heavy chain of IgA and shows minimal cross-reaction with heavy chains of other immunoglobulins. It is reactive with both IgA1 and IgA2 subclasses of Alpha heavy chain. It reacts with the third constant domain (CH3) of the alpha chain of IgA molecules. Immunoglobulins are four-chain, Y-shaped, monomeric structures comprised of two identical heavy chains and two identical light chains held together through inter-chain disulfide bonds. The chains form two domains, the Fab (antigen binding) fragment and the Fc (constant) fragment. Immunoglobulin A (IgA) is the main protein of the mucosal immune system. It is generated by B-cells in gut-associated lymphoid tissues. Daily production of IgA exceeds that of any of the other immunoglobulins. IgA exists mainly in dimers but can also exist as polymers or as monomers. Dimers and polymers contain a joining (J) chain that can be bound by the polymeric immunoglobulin receptor (pIgR) for transportation of the molecule to mucosal surfaces. The most common feature of plasmacytomas, and certain non-Hodgkin s lymphomas is the restricted expression of a single heavy chain class. Demonstration of clonality in lymphoid infiltrates indicates that the infiltrate is clonal and therefore malignant.

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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 recognises 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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Recognises a disaccharide epitope, Gal1-3GalNAc, of Thomsen-Friedenreich (TF) antigen. It is specific for both anomeric forms of the disaccharide (TF and TF, including related structures on the glycolipid) and shows no cross-reactivity with sialylated glycophorin. The Thomsen-Friedenreich antigen acts as an oncofetal antigen, with low expression in normal adult tissues but increasing to fetal levels of expression in hyperplasia or malignancy. It is considered as a pan-carcinoma marker. During metastasis, the ability of malignant cells to form multicellular aggregates via homotypic or heterotypic aggregation and their adhesion to the endothelium are critical. The tumor-associated carbohydrate Thomsen-Friedenreich antigen (Gal-GalNAc) is involved in tumor cell adhesion and tissue invasion. It also causes an immune response, and overexpression of the antigen causes cancer cells to be more sensitive to natural killer cell lysis. The Thomsen-Friedenreich antigen is suppressed in normal healthy cells and represents one of the few chemically well-defined antigens associated with tumor malignancy. The presence of the Thomsen-Friedenreich antigen on the surface of cancer cells may result from a divergence from the normal pathway for O-linked glycosylation in these cells, most likely caused by inappropriate localization of the enzymes involved in synthesis of the disaccharide.

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This mAb reacts with both SUMO-2 and SUMO-3. The small ubiquitin-related modifier (SUMO) proteins, which include SUMO-1, 2 and 3, belong to the ubiquitin-like protein family. Like ubiquitin, the SUMO proteins are synthesised as precursor proteins that undergo processing before conjugation to target proteins. Also, both utilize the E1, E2 and E3 cascade enzymes for conjugation. However, SUMO and ubiquitin differ with respect to targeting. Ubiquitination predominantly targets proteins for degradation, whereas sumoylation targets proteins to a variety of cellular processing, including nuclear transport, transcriptional regulation, apoptosis and protein stability. The unconjugated SUMO-1, 2 and 3 proteins localize to the nuclear membrane, nuclear bodies and cytoplasm, respectively. SUMO-1 utilizes Ubc9 for conjugation to several target proteins, which include MDM2, p53, Pml and RanGap1. SUMO-2 and 3 contribute to a greater percentage of protein modification than does SUMO-1 and unlike SUMO-1, they can form polymeric chains. In addition, SUMO-3 regulates beta-Amyloid generation and may be critical in the onset or progression of Alzheimer s disease.

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GLOVE NEOPRENE BLACK THICK 5/10 S.9 1 * 30 items

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This antibody recognises a protein of 33-37 kDa, identified as CD20 (Workshop V; Code CD20.12). The antibody recognises the extracellular domain of the protein. The epitope is similar to or identical to that recognized by other CD20 antibodies including Leu-16 and B1. This antibody can be used for immunophenotyping of leukemia and malignant cells, B lymphocyte detection in peripheral blood, Bcell localization in tissues and B lymphocyte purification by immunosorbent methods. CD20 is a non-Ig differentiation antigen of Bcells and its expression is restricted to normal and neoplastic Bcells, being absent from all other leukocytes and tissues. It is expressed by pre Bcells and persists during all stages of Bcell maturation but is lost upon terminal differentiation into plasma cells. Protein passes through the membrane 4 times with both ends in cytoplasm and exposes one short and one longer loop to the external environment. CD20 is not glycosylated in resting Bcells and its cytoplasmic domains are differentially phosphorylated upon activation. It acts as a calcium channel involved in Bcell activation and cell cycle progression.

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Recognises an epitope on the extracellular domain of gonadotropin releasing hormone (GnRH) receptor or luteinizing hormone receptor (LHCGR). Lutropin (also designated luteinizing hormone) plays a role in spermatogenesis and ovulation by stimulating the testes and ovaries to produce steroids. Gonadotropin (also designated choriogonadotropin) production in the placenta maintains estrogen and progesterone levels during the first trimester of pregnancy. Ovaries and testes abundantly express luteinizing hormone/choriogonadotropin receptor. GnRH receptor contains seven hydrophobic transmembrane domains connected by hydrophilic extracellular and intracellular loops characteristic of G-protein coupled receptors. GnRH stimulates the gonadotrophs of the anterior pituitary to secrete luteinizing hormone (LH) as well as follicle-stimulating hormone (FSH). GnRH influences the protective effect of pregnancy and Gonadotropin against breast cancer. The expression of GnRH on breast carcinoma correlates in part to the degree of tumor differentiation. GnRH-positive breast tumors occur more frequently in tumors with greater cell differentiation in premenopausal women. GnRH is present in luteal and granulosa cells as well as in ovarian cell membrane preparations.