28227 Résultats pour : "Biotium"

Supplier: Biotium

This MAb recognizes a 60 kDa antigen associated with the mitochondria in human cells. It is a part of a new panel of reagents, which recognizes subcellular organelles or compartments of human cells. These markers may be useful in identification of these organelles in cells, tissues, and biochemical preparations. This MAb recognizes an antigen associated with the mitochondria in human cells only. It can be used to stain the mitochondria in cell or tissue preparations and can be used as a mitochondrial marker in subcellular fractions. It produces a spaghetti-like pattern in normal and malignant cells and may be used to stain mitochondria of cells in fixed or frozen tissue sections. It can also be used with paraformaldehyde fixed frozen tissue or cell preparations. This MAb is an excellent marker for human cells in xenographic model research. It reacts specifically with human cells, including neurons and embryonic stem cells.

Supplier: Biotium

Anti-PNL2 is a novel monoclonal antibody, which has recently been introduced as an immunohistochemical reagent to stain melanocytes and tumors derived therefrom. The antigen recognized by PNL2 is different from Melan A and gp100. Its epitope is not destroyed by digestion with neuraminidase i.e. its epitope id not glycosylated. Anti-PNL2 may be most useful because of its high sensitivity for metastatic melanoma (87%), as opposed to 76% for anti-HMB45 and 82% for anti-MART-1. Anti-PNL2 labels intra-epidermal nevi while the dermal component of compound nevi are largely non-reactive with anti-PNL2. Antibodies against PNL2, MART-1 (Melan A) and HMB45 stain most clear cell sarcoma cells and a few cells in angio-myolipomas and lymphangioleiomyomatosis. Anti-PNL2 is a useful antibody for the identification of melanomas and clear cell sarcomas. Differential diagnosis is aided by the results from a panel of antibodies, including antibodies against HMB45, MART-1, tyrosinase, and MiTF.

Supplier: Biotium

Anti-PNL2 is a novel monoclonal antibody, which has recently been introduced as an immunohistochemical reagent to stain melanocytes and tumors derived therefrom. The antigen recognized by PNL2 is different from Melan A and gp100. Its epitope is not destroyed by digestion with neuraminidase i.e. its epitope id not glycosylated. Anti-PNL2 may be most useful because of its high sensitivity for metastatic melanoma (87%), as opposed to 76% for anti-HMB45 and 82% for anti-MART-1. Anti-PNL2 labels intra-epidermal nevi while the dermal component of compound nevi are largely non-reactive with anti-PNL2. Antibodies against PNL2, MART-1 (Melan A) and HMB45 stain most clear cell sarcoma cells and a few cells in angio-myolipomas and lymphangioleiomyomatosis. Anti-PNL2 is a useful antibody for the identification of melanomas and clear cell sarcomas. Differential diagnosis is aided by the results from a panel of antibodies, including antibodies against HMB45, MART-1, tyrosinase, and MiTF.

Supplier: Biotium

Anti-PNL2 is a novel monoclonal antibody, which has recently been introduced as an immunohistochemical reagent to stain melanocytes and tumors derived therefrom. The antigen recognized by PNL2 is different from Melan A and gp100. Its epitope is not destroyed by digestion with neuraminidase i.e. its epitope id not glycosylated. Anti-PNL2 may be most useful because of its high sensitivity for metastatic melanoma (87%), as opposed to 76% for anti-HMB45 and 82% for anti-MART-1. Anti-PNL2 labels intra-epidermal nevi while the dermal component of compound nevi are largely non-reactive with anti-PNL2. Antibodies against PNL2, MART-1 (Melan A) and HMB45 stain most clear cell sarcoma cells and a few cells in angio-myolipomas and lymphangioleiomyomatosis. Anti-PNL2 is a useful antibody for the identification of melanomas and clear cell sarcomas. Differential diagnosis is aided by the results from a panel of antibodies, including antibodies against HMB45, MART-1, tyrosinase, and MiTF.

Supplier: Biotium

This MAb reacts specifically with heat shock protein HSP27 in human and monkey tissues and cell lines such as MCF-7. HSP27, also referred to as the Estrogen-Regulated 24K protein and HSP28, is one of several small heat shock proteins produced by all organisms studied. HSP27 synthesis is induced by elevated temperature, as well as by estrogen in hormone responsive cells. Interestingly, human HSP27 also shares greater than 50% homology with low molecular weight Drosophila HSPs and mammalian α-crystalline lens protein. Because of the estrogen responsive nature of HSP27, this protein has been studied extensively in human estrogen responsive tissues such as cervix, endometrium and breast tissue. Therefore HSP27 may be useful in classifying various hormone sensitive tumors.

Supplier: Biotium

HLA-A, with HLA-B and HLA-C, belongs to major histocompatibility complex (MHC) class I antigens and expresses constitutively on all nucleated cells. MHC class I antigens play a role in class I MHC-associated antigen presentation, inhibition of NK cell cytotoxicity, tumor surveillance, and tissue allotransplantation. This MAb is useful for HLA molecular typing of peripheral blood leukocytes as well as a large number of leukemic cell lines. It reacts with an intralocus determinant present on a limited number of HLA-A locus-encoded gene products (HLA-A2, -A3, -A28, -A29, -A30, -A31 and -Aw33). Its epitope maps between aa65-to-aa80 of the α1 domain of the HLA-A. This MAb recognizes an intralocus determinant present on a limited number of HLA-A locus-encoded gene products (HLA-A2, -A3, A28, -A29, -A30, -A31 and -Aw33). Furthermore, by testing its reactivity with HLA-A2 natural variants and mutants, the importance of amino acid residues 79 and/or 80 of the α1 domain was demonstrated in the formation of an intralocus HLA-A determinant.

Supplier: Biotium

This antibody recognizes an antigen associated with the nuclear membrane in human cells. It can be used to stain the nuclear membrane in cell or tissue preparations and can be used as a marker of the nuclear membrane in subcellular fractions. It produces a ring pattern around the nucleus of cells of normal and malignant cells and may be used to stain the nuclear membrane of cells in fixed or frozen tissue sections. It can be used with paraformaldehyde fixed frozen tissue or cell preparations and formalin fixed, paraffin-embedded tissue sections.,The nuclear envelope (also known as the perinuclear envelope, nuclear membrane, nucleolemma or karyotheca) is the double membrane of the nucleus that encloses genetic material in eukaryotic cells. It separates the contents of the nucleus (DNA in particular) from the cytosol (cytoplasm). Numerous nuclear pores are present on the nuclear envelope to facilitate and regulate the exchange of materials (for example, proteins and RNA) between the nucleus and the cytoplasm. The space between the two membranes that make up the nuclear envelope is called the perinuclear space (also called the perinuclear cisterna), and is usually about 20 - 40 nm wide. Each of the two membranes is composed of a lipid bilayer. The outer membrane is continuous with the rough endoplasmic reticulum. The inner membrane is erected upon the nuclear lamina, a network of intermediate filaments made of lamin, that plays a role in mitosis and meiosis. The type of lamins present are A, B1, B2, and C. The nuclear envelope may also play a role in the disposition of chromatin inside the nucleus. The lamina acts as a site of attachment for chromosomes. It also acts like a shield for the nucleus. During prophase in mitosis, the chromatids begin condensing to form chromosomes, and the nuclear envelope begins to disintegrate. During metaphase, the nuclear envelope is completely disintegrated, and the chromosomes can be pulled apart as chromatids by the spindle fibers.

Supplier: Biotium

Smooth muscle myosin heavy chain (SM-MHC) is a cytoplasmic structural protein, which is a major component of the contractile apparatus in smooth muscle cells. Expression of smooth muscle myosin is developmentally regulated, appearing early in smooth muscle development, and is specific for smooth muscle development. Two isoforms of smooth muscle myosin heavy chain have been identified, designated MHC-1 and MHC-2. The antibody may be useful for the study of breast tumors as the presence of an intact layer of myoepithelial cells is an important feature, which may distinguish benign breast lesions and carcinoma in situ from invasive tumors.

Supplier: Biotium

The MUC6 gastric mucin is a secreted glycoprotein that plays an essential role in epithelial cyto-protection from acid, proteases, pathogenic microorganisms, and mechanical trauma in the gastrointestinal tract. Mucin 6 expression is highest in the stomach and gall bladder, with lower expression in the terminal ileum and right colon. In gastric cancer, Mucin 6 has an altered expression. In normal stomach, Mucin 6 is associated with Lewis type 2; Mucin 6 is also expressed in gastric metaplasia, duodenum and pancreas. Mucin 6 is a secretory mucin, located in the deeper mucosal folds of human gall bladder, and its expression is altered with increasing degrees of inflammation.

Supplier: Biotium

In Western blotting, this antibody recognizes proteins in MW range of 265-400 kDa, identified as different glycoforms of EMA. This MAb reacts with the DTRP epitope in the tandem repeats. The α subunit has cell adhesive properties. It can act both as an adhesion and an anti-adhesion protein. EMA may provide a protective layer on epithelial cells against bacterial and enzyme attack. The β subunit contains a C-terminal domain, which is involved in cell signaling, through phosphorylations and protein-protein interactions. In immunohistochemical assays, it superbly stains routine formalin/paraffin carcinoma tissues. Antibody to EMA is useful as a pan-epithelial marker for detecting early metastatic loci of carcinoma in bone marrow or liver.

Supplier: Biotium

The MUC6 gastric mucin is a secreted glycoprotein that plays an essential role in epithelial cyto-protection from acid, proteases, pathogenic microorganisms, and mechanical trauma in the gastrointestinal tract. Mucin 6 expression is highest in the stomach and gall bladder, with lower expression in the terminal ileum and right colon. In gastric cancer, Mucin 6 has an altered expression. In normal stomach, Mucin 6 is associated with Lewis type 2; Mucin 6 is also expressed in gastric metaplasia, duodenum and pancreas. Mucin 6 is a secretory mucin, located in the deeper mucosal folds of human gall bladder, and its expression is altered with increasing degrees of inflammation.

Supplier: Biotium

The MUC6 gastric mucin is a secreted glycoprotein that plays an essential role in epithelial cyto-protection from acid, proteases, pathogenic microorganisms, and mechanical trauma in the gastrointestinal tract. Mucin 6 expression is highest in the stomach and gall bladder, with lower expression in the terminal ileum and right colon. In gastric cancer, Mucin 6 has an altered expression. In normal stomach, Mucin 6 is associated with Lewis type 2; Mucin 6 is also expressed in gastric metaplasia, duodenum and pancreas. Mucin 6 is a secretory mucin, located in the deeper mucosal folds of human gall bladder, and its expression is altered with increasing degrees of inflammation.

Supplier: Biotium

Smooth muscle myosin heavy chain (SM-MHC) is a cytoplasmic structural protein, which is a major component of the contractile apparatus in smooth muscle cells. Expression of smooth muscle myosin is developmentally regulated, appearing early in smooth muscle development, and is specific for smooth muscle development. Two isoforms of smooth muscle myosin heavy chain have been identified, designated MHC-1 and MHC-2. The antibody may be useful for the study of breast tumors as the presence of an intact layer of myoepithelial cells is an important feature, which may distinguish benign breast lesions and carcinoma in situ from invasive tumors.

Supplier: Biotium

Smooth muscle myosin heavy chain (SM-MHC) is a cytoplasmic structural protein, which is a major component of the contractile apparatus in smooth muscle cells. Expression of smooth muscle myosin is developmentally regulated, appearing early in smooth muscle development, and is specific for smooth muscle development. Two isoforms of smooth muscle myosin heavy chain have been identified, designated MHC-1 and MHC-2. The antibody may be useful for the study of breast tumors as the presence of an intact layer of myoepithelial cells is an important feature, which may distinguish benign breast lesions and carcinoma in situ from invasive tumors.

Supplier: Biotium

Smooth muscle myosin heavy chain (SM-MHC) is a cytoplasmic structural protein, which is a major component of the contractile apparatus in smooth muscle cells. Expression of smooth muscle myosin is developmentally regulated, appearing early in smooth muscle development, and is specific for smooth muscle development. Two isoforms of smooth muscle myosin heavy chain have been identified, designated MHC-1 and MHC-2. The antibody may be useful for the study of breast tumors as the presence of an intact layer of myoepithelial cells is an important feature, which may distinguish benign breast lesions and carcinoma in situ from invasive tumors.

Supplier: Biotium

This antibody recognizes an antigen associated with the nuclear membrane expressed in human cells. It can be used to stain the nuclear membrane in cell or tissue preparations and can be used as a marker of the nuclear membrane in subcellular fractions. It produces a ring pattern around the nucleus of cells of normal and malignant cells and may be used to stain the nuclear membrane of cells in fixed or frozen tissue sections. ,The nuclear envelope (also known as the perinuclear envelope, nuclear membrane, nucleolemma or karyotheca) is the double membrane of the nucleus that encloses genetic material in eukaryotic cells. It separates the contents of the nucleus (DNA in particular) from the cytosol (cytoplasm). Numerous nuclear pores are present on the nuclear envelope to facilitate and regulate the exchange of materials (for example, proteins and RNA) between the nucleus and the cytoplasm. The space between the two membranes that make up the nuclear envelope is called the perinuclear space (also called the perinuclear cisterna), and is usually about 20 - 40 nm wide. Each of the two membranes is composed of a lipid bilayer. The outer membrane is continuous with the rough endoplasmic reticulum. The inner membrane is erected upon the nuclear lamina, a network of intermediate filaments made of lamin, that plays a role in mitosis and meiosis. The type of lamins present are A, B1, B2, and C. The nuclear envelope may also play a role in the disposition of chromatin inside the nucleus. The lamina acts as a site of attachment for chromosomes. It also acts like a shield for the nucleus. During prophase in mitosis, the chromatids begin condensing to form chromosomes, and the nuclear envelope begins to disintegrate. During metaphase, the nuclear envelope is completely disintegrated, and the chromosomes can be pulled apart as chromatids by the spindle fibers.

Supplier: Biotium

Recognizes a 27 kDa protein, identified as the p27Kip1, a cell cycle regulatory mitotic inhibitor. Its epitope spans between aa 83-204 of p27. It is highly specific and shows no cross-reaction with other related mitotic inhibitors. p27Kip1 functions as a negative regulator of G1 progression and has been proposed to function as a possible mediator of TGF- induced G1 arrest. p27Kip1 is a candidate tumor suppressor gene. This MAb co-precipitates cdk4 in complex p27Kip1 and is excellent for staining of formalin-fixed tissues.

Supplier: Biotium

This MAb recognizes a 27 kDa protein, identified as the p27Kip1, a cell cycle regulatory mitotic inhibitor. It is highly specific and shows no cross-reaction with other related mitotic inhibitors. p27Kip1 functions as a negative regulator of G1 progression and has been proposed to function as a possible mediator of TGF- induced G1 arrest. p27Kip1 is a candidate tumor suppressor gene. This MAb is excellent for staining of formalin-fixed tissues.

Supplier: Biotium

This antibody recognizes an intra-cytoplasmic antigen, which shows a very high degree of specificity for plasma cells. This antigen is present in normal as well as neoplastic plasma cells. Plasma cells, which are large lymphocytes derived from an antigen-specific B cell, secrete antibodies and are responsible for humoral immunity. Plasma cells differentiate from B cells upon stimulation by CD4 lymphocytes. The B cell acts as an antigen-presenting cell (APC), consuming an offending pathogen, which is taken up by the B cell by phagocytosis and broken down within proteosomes. Plasma cells contain basophilic cytoplasm; their nucleus contains heterochromatin organized in a characteristic cartwheel arrangement. This MAb superbly recognizes normal and neoplastic plasma cells in routine formalin-fixed, paraffin-embedded tissue sections. It is of potential value in identifying myeloma or plasmacytoma in bone marrow or other tissues. It also helps differentiate lympho-plasmacytoid lymphoma from lymphocytic and follicular lymphoma. Note that this MAb is not suitable for staining frozen tissues.

Supplier: Biotium

This antibody recognizes a protein of 70 kDa, identified as prolactin receptor. Prolactin is a pituitary hormone involved in the stimulation of milk production, salt and water regulation, growth, development and reproduction. The initial step in its action is the binding to a specific membrane receptor (prolactin receptor), which belongs to the superfamily of class 1 cytokine receptors. The function of the prolactin receptor is mediated, at least in part, by two families of signaling molecules: Janus kinases and signal transducers and activators of transcription.

Supplier: Biotium

This MAb recognizes a 27 kDa protein, identified as the p27Kip1, a cell cycle regulatory mitotic inhibitor. It is highly specific and shows no cross-reaction with other related mitotic inhibitors. p27Kip1 functions as a negative regulator of G1 progression and has been proposed to function as a possible mediator of TGF- induced G1 arrest. p27Kip1 is a candidate tumor suppressor gene. This MAb is excellent for staining of formalin-fixed tissues.

Supplier: Biotium

This MAb recognizes a 27 kDa protein, identified as the p27Kip1, a cell cycle regulatory mitotic inhibitor. It is highly specific and shows no cross-reaction with other related mitotic inhibitors. In Western blotting of cell lysates from 7 human breast cancer cell lines (ZR75-1, ZR75-30, MCF-7, MDAMB453, T47D, CAL51, 734B), the antibody labels a single band corresponding to p27Kip1. It functions as a negative regulator of G1 progression and has been proposed to function as a possible mediator of TGF- induced G1 arrest. p27Kip1 is a candidate tumor suppressor gene. Reportedly, low p27 expression has been associated with unfavorable prognosis in renal cell carcinoma, colon carcinoma, breast carcinomas, non-small-cell lung carcinoma, hepatocellular carcinoma, multiple myeloma, and lymph node metastases in papillary carcinoma of the thyroid, as well as a more aggressive phenotype in carcinoma of the cervix.

Supplier: Biotium

The onset of angiogenesis is believed to be an early event in tumorigenesis and may facilitate tumor progression and metastasis. Several growth factors with angiogenic activity have been described. These include Fibroblast Growth Factor (FGF), Platelet Derived Growth Factor (PDGF), Vascular Endothelial Growth Factor (VEGF) and Placenta Growth Factor (PLGF). Placenta growth factor (PLGF) is a secreted protein primarily produced by placental trophoblasts but also expressed in other endothelial cells and tumors. There are three isoforms, PLGF-1, PLGF-2, and PLGF-3. PLGF-2 is expressed up until week 8 in the placenta; the placental tissues continuously express PLGF-1 and PLGF-3 but only PLGF-1 is found in colon and mammary carcinomas. PLGF acts to stimulate angiogenesis, endothelial growth and migration. PLGF is a powerful promoter of tumor growth and is upregulated in some cancers, and PLGF is thought to aid in atherosclerotic lesions and neovascular growth surrounding the lesion. Also, PLGF appears to aid aldosterone mediated atherosclerosis. Serum levels of PLGF in some cases are used as a potential biomarker for disease or genetic defect. Recent research indicates that PLGF levels are lower in mothers with Down syndrome fetuses. Evidence has suggested VEGF to be an obligatory component in PLGF signaling. While VEGF homodimers and VEGF/PLGF heterodimers function as potent mediators of mitogenic and chemotactic responses in endothelial cells, PLGF homodimers are effectual only at extremely high concentrations. Indeed, many of the physiological effects attributed to VEGF may actually be a result of VEGF/PLGF. VEGF and PLGF share a common receptor, Flt-1, and may also activate Flk-1/KDR.

Supplier: Biotium

The onset of angiogenesis is believed to be an early event in tumorigenesis and may facilitate tumor progression and metastasis. Several growth factors with angiogenic activity have been described. These include Fibroblast Growth Factor (FGF), Platelet Derived Growth Factor (PDGF), Vascular Endothelial Growth Factor (VEGF) and Placenta Growth Factor (PLGF). Placenta growth factor (PLGF) is a secreted protein primarily produced by placental trophoblasts but also expressed in other endothelial cells and tumors. There are three isoforms, PLGF-1, PLGF-2, and PLGF-3. PLGF-2 is expressed up until week 8 in the placenta; the placental tissues continuously express PLGF-1 and PLGF-3 but only PLGF-1 is found in colon and mammary carcinomas. PLGF acts to stimulate angiogenesis, endothelial growth and migration. PLGF is a powerful promoter of tumor growth and is upregulated in some cancers, and PLGF is thought to aid in atherosclerotic lesions and neovascular growth surrounding the lesion. Also, PLGF appears to aid aldosterone mediated atherosclerosis. Serum levels of PLGF in some cases are used as a potential biomarker for disease or genetic defect. Recent research indicates that PLGF levels are lower in mothers with Down syndrome fetuses. Evidence has suggested VEGF to be an obligatory component in PLGF signaling. While VEGF homodimers and VEGF/PLGF heterodimers function as potent mediators of mitogenic and chemotactic responses in endothelial cells, PLGF homodimers are effectual only at extremely high concentrations. Indeed, many of the physiological effects attributed to VEGF may actually be a result of VEGF/PLGF. VEGF and PLGF share a common receptor, Flt-1, and may also activate Flk-1/KDR.

Supplier: Biotium

This antibody recognizes a polypeptide of 6.5 kDa, identified as pS2 estrogen-regulated protein. Its epitope is localized between aa57-84 of human pS2 protein. pS2 is a trefoil peptide. Trefoil peptides are protease resistant molecules secreted throughout the gut that play a role in mucosal healing. These peptides contain three intra-chain disulfide bonds, forming the trefoil motif, or P-domain. pS2 is known to form dimers and this dimerization is thought to play a role in its protective and healing properties. About 60% of breast carcinomas are positive for pS2. Staining is cytoplasmic, often with localization to the Golgi apparatus. pS2 is shown to be localized in normal stomach mucosa, gastric fluid, goblet cells in the colon and small intestine, and in ulcerations of the gastrointestinal tract. Several studies have shown that pS2 is primarily expressed in estrogen receptor-positive breast tumors and it may define a subset of estrogen-dependent tumors that displays an increased likelihood of response to endocrine therapy.

Supplier: Biotium

The onset of angiogenesis is believed to be an early event in tumorigenesis and may facilitate tumor progression and metastasis. Several growth factors with angiogenic activity have been described. These include Fibroblast Growth Factor (FGF), Platelet Derived Growth Factor (PDGF), Vascular Endothelial Growth Factor (VEGF) and Placenta Growth Factor (PLGF). Placenta growth factor (PLGF) is a secreted protein primarily produced by placental trophoblasts but also expressed in other endothelial cells and tumors. There are three isoforms, PLGF-1, PLGF-2, and PLGF-3. PLGF-2 is expressed up until week 8 in the placenta; the placental tissues continuously express PLGF-1 and PLGF-3 but only PLGF-1 is found in colon and mammary carcinomas. PLGF acts to stimulate angiogenesis, endothelial growth and migration. PLGF is a powerful promoter of tumor growth and is upregulated in some cancers, and PLGF is thought to aid in atherosclerotic lesions and neovascular growth surrounding the lesion. Also, PLGF appears to aid aldosterone mediated atherosclerosis. Serum levels of PLGF in some cases are used as a potential biomarker for disease or genetic defect. Recent research indicates that PLGF levels are lower in mothers with Down syndrome fetuses. Evidence has suggested VEGF to be an obligatory component in PLGF signaling. While VEGF homodimers and VEGF/PLGF heterodimers function as potent mediators of mitogenic and chemotactic responses in endothelial cells, PLGF homodimers are effectual only at extremely high concentrations. Indeed, many of the physiological effects attributed to VEGF may actually be a result of VEGF/PLGF. VEGF and PLGF share a common receptor, Flt-1, and may also activate Flk-1/KDR.

Supplier: Biotium

This antibody recognizes a polypeptide of 6.5 kDa, identified as pS2 estrogen-regulated protein. Its epitope is localized between aa57-84 of human pS2 protein. pS2 is a trefoil peptide. Trefoil peptides are protease resistant molecules secreted throughout the gut that play a role in mucosal healing. These peptides contain three intra-chain disulfide bonds, forming the trefoil motif, or P-domain. pS2 is known to form dimers and this dimerization is thought to play a role in its protective and healing properties. About 60% of breast carcinomas are positive for pS2. Staining is cytoplasmic, often with localization to the Golgi apparatus. pS2 is shown to be localized in normal stomach mucosa, gastric fluid, goblet cells in the colon and small intestine, and in ulcerations of the gastrointestinal tract. Several studies have shown that pS2 is primarily expressed in estrogen receptor-positive breast tumors and it may define a subset of estrogen-dependent tumors that displays an increased likelihood of response to endocrine therapy.

Supplier: Biotium

Recognizes a 34 kDa protein, which is identified as cyclin dependent kinase 1 (cdk1) or p34cdc2 protein kinase. cdk1 / p34cdc2 plays a crucial role during cell division and is most active during mitosis. It is predominantly localized in the nucleus. It is a serine/threonine kinase, which is activated by cyclin, presumably by de-phosphorylation of tyrosine residues. Activated cdk1 / p34cdc2 performs specific functions during mitosis, including nuclear envelope breakdown and chromosome condensation.

Supplier: Biotium

This antibody recognizes a polypeptide of 6.5 kDa, identified as pS2 estrogen-regulated protein. Its epitope is located in the c-terminus of human pS2 protein. pS2 is a trefoil peptide. Trefoil peptides are protease resistant molecules secreted throughout the gut that play a role in mucosal healing. These peptides contain three intra-chain disulfide bonds, forming the trefoil motif, or P-domain. pS2 is known to form dimers and this dimerization is thought to play a role in its protective and healing properties. About 60% of breast carcinomas are positive for pS2. Staining is cytoplasmic, often with localization to the Golgi apparatus. pS2 is shown to be localized in normal stomach mucosa, gastric fluid, goblet cells in the colon and small intestine, and in ulcerations of the gastrointestinal tract. Several studies have shown that pS2 is primarily expressed in estrogen receptor-positive breast tumors and it may define a subset of estrogen-dependent tumors that displays an increased likelihood of response to endocrine therapy.

Supplier: Biotium

By immunohistochemistry, this antibodyspecifically recognizes a protein in melanocytes and melanomas. This MAb reacts with junctional and blue nevus cells and variably with fetal and neonatal melanocytes. Intradermal nevi, normal adult melanocytes, and non-melanocytic cells are negative. It does not stain tumor cells of epithelial, lymphoid, glial, or mesenchymal origin. Metastatic amelanotic melanoma can often be confused with a variety of poorly differentiated carcinomas, large cell lymphomas, and sarcomas using H & E stains alone. It is also difficult to differentiate melanoma from spindle cell carcinomas and various types of mesenchymal neoplasms. This MAb stains fetal and neonatal melanocytes, junctional and blue nevus cells, and malignant melanoma. This MAb also stains Angiomyolipoma (PEComa).