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Smoothelin [R4A]
Description Smoothelin is a constituent of the smooth muscle cell cytoskeleton protein exclusively found in differentiated smooth muscle cells (SMC). Cells with SMC-like characteristics, such as myofibroblasts and myoepithelial cells, as well as skeletal and cardiac muscle do not contain smoothelin. Distinguishing between bladder muscularis mucosae (MM) and muscularis propria (MP) muscle bundles is crucial for accurate staging of bladder carcinoma. Strong smoothelin expression is nearly exclusively observed in muscularis propria. The staining pattern of MP (strongly positive) and MM (negative or weakly positive) makes this technique an attractive diagnostic tool for the sometimes difficult task of staging bladder urothelial carcinoma, such as in transurethral resection specimens of urinary bladder tumors. Differentiating between smooth muscle tumors and other mesenchymal neoplasms of the GI tract can be challenging in small biopsies. Anti-smoothelin immunostaining can be helpful in differentiating Host Mouse Application Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human, Mouse, Rat, Chicken -
Somatostatin Receptor Type 2/SSTR2 [A8]
Description Somatostatin is a peptide hormone that regulates the endocrine system and affects neurotransmission and cell proliferation via interaction with G-protein-coupled somatostatin receptors and inhibition of the release of numerous secondary hormones. This hormone has two active forms produced by alternative cleavage of a single preproprotein: somatostatin-14, composed of 14 amino acids and somatostatin-28, a prohormone composed of 28 residues. Somatostatin is secreted by D-cells of the islets of Langerhans in pancreas, endocrine cells of the gastrointestinal tract, bronchopulmonary system, thymus, and C cells of the thyroid. Somatostatin positive cells may also be present in medullary thyroid carcinomas, C cell hyperplasia, thymic tumors and pulmonary small cell carcinomas. An antibody to Somatostatin can be used to identify pancreatic islet cell hyperplasia as well as islet cell tumors, such as somatostatinomas. (Shipping Cost: €200.00) Host Mouse Application ELISA, Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human, Mouse, Rat -
Somatostatin Receptor Type 2/SSTR2 [A8]
Description Somatostatin is a peptide hormone that regulates the endocrine system and affects neurotransmission and cell proliferation via interaction with G-protein-coupled somatostatin receptors and inhibition of the release of numerous secondary hormones. This hormone has two active forms produced by alternative cleavage of a single preproprotein: somatostatin-14, composed of 14 amino acids and somatostatin-28, a prohormone composed of 28 residues. Somatostatin is secreted by D-cells of the islets of Langerhans in pancreas, endocrine cells of the gastrointestinal tract, bronchopulmonary system, thymus, and C cells of the thyroid. Somatostatin positive cells may also be present in medullary thyroid carcinomas, C cell hyperplasia, thymic tumors and pulmonary small cell carcinomas. An antibody to Somatostatin can be used to identify pancreatic islet cell hyperplasia as well as islet cell tumors, such as somatostatinomas. (Shipping Cost: €200.00) Host Mouse Application ELISA, Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human, Mouse, Rat -
STAT1/ISGF3 [EPR21057-141]
Description STAT1 (signal transducer and activator of transcription 1) or ISGF3 is involved in upregulating genes due to a signal by either type I, type II, or type III interferons. STAT1 may be a target for therapeutic treatment to restore apoptotic mechanisms and sensitivity to chemotherapy. The phosphorylated STATs dimerize, associate with ISGF3G/IRF-9 to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of interferon stimulated genes, which drive the cell in an antiviral state. The phosphorylated STAT1 is a potential predictor of interferon (IFN) response for advanced renal cell carcinoma. Mutations in the gene is associated with death at an early age due to overwhelming viral infection (complete STAT1 deficiency. (Shipping Cost: €200.00) Host Rabbit Application Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry on paraffin sections (IHC-P), Western Blot (WB) Reactivity Human, Mouse, Rat -
SUMO-1 [SM1/495]
Description The small ubiquitin-related modifier (SUMO) proteins, which include SUMO-1, SUMO-2 and SUMO-3, belong to the ubiquitin-like protein family. Like ubiquitin, the SUMO proteins are synthesized 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 protein localizes to the nuclear membrane. (Shipping Cost: €200.00) Host Mouse Application Flow cytometry (FC), Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC), Western Blot (WB) Reactivity Human, Rat -
SUMO-1 [SM1/495]
Description The small ubiquitin-related modifier (SUMO) proteins, which include SUMO-1, SUMO-2 and SUMO-3, belong to the ubiquitin-like protein family. Like ubiquitin, the SUMO proteins are synthesized 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 protein localizes to the nuclear membrane. (Shipping Cost: €200.00) Host Mouse Application Flow cytometry (FC), Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC), Western Blot (WB) Reactivity Human, Rat -
Survivin [D8]
Description Survivin is a unique member of the inhibitor of apoptosis (IAP) protein family that interferes with post-mitochondrial events including activation of caspases. Survivin regulates the cell cycle and is expressed in most tumors, but it is barely detectable in terminally differentiated normal cells and tissues. Survivin is expressed in the G2/M phase of the cell cycle. At the beginning of mitosis, survivin associates with microtubules of the mitotic spindle in a specific and saturable reaction that is regulated by microtubule dynamics. Disruption of survivin-microtubule interactions results in loss of survivin's anti-apoptotic function and increased caspase-3 activity, a mechanism involved in cell death during mitosis. Nuclear-cytoplasmic shuttling of survivin is controlled by nuclear export signal (NES), which is necessary for the anti-apoptotic function of survivin. Inhibition of the NES makes cells more susceptible to chemotherapy- or radiotherapy-induced apoptosis. The association of Host Mouse Application ELISA, Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human, Mouse, Rat -
Survivin [D8]
Description Survivin is a unique member of the inhibitor of apoptosis (IAP) protein family that interferes with post-mitochondrial events including activation of caspases. Survivin regulates the cell cycle and is expressed in most tumors, but it is barely detectable in terminally differentiated normal cells and tissues. Survivin is expressed in the G2/M phase of the cell cycle. At the beginning of mitosis, survivin associates with microtubules of the mitotic spindle in a specific and saturable reaction that is regulated by microtubule dynamics. Disruption of survivin-microtubule interactions results in loss of survivin's anti-apoptotic function and increased caspase-3 activity, a mechanism involved in cell death during mitosis. Nuclear-cytoplasmic shuttling of survivin is controlled by nuclear export signal (NES), which is necessary for the anti-apoptotic function of survivin. Inhibition of the NES makes cells more susceptible to chemotherapy- or radiotherapy-induced apoptosis. The association of Host Mouse Application ELISA, Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human, Mouse, Rat -
Tartarate Resistant Acid Phosphatase (TRAcP/TRAP5) [ACP5/1070]
Description Tartrate resistant acid phosphatase (TRAcP) is a basic, iron-binding protein with high activity towards phosphoproteins, ATP and 4 nitrophenyl phosphate. Expression of TRAcP is reported to be increased in the spleen and monocytes of individuals with Gaucher’s disease, splenocytes and circulating white cells of individuals with hairy cell leukemia, spleens of individuals with Hodgkin disease, and the sera of individuals undergoing active bone turnover. Elevated levels are also reported to be associated with various B-cell and T-cell leukemias and lymphomas, placental decidual cells, syncytiotrophoblasts, and some macrophages distributed throughout maternal and embryonic tissues. The histochemical identification of hairy cell leukemia via tartrate-resistant acid phosphatase assay has been a standard for over two decades. Anti-TRAcP labels the cells of hairy cell leukemia (HCL) with a high degree of sensitivity and specificity. Worthy also of mention in this regard are anti-annexin A1 and Host Mouse Application Flow cytometry (FC), Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC) Reactivity Human, Mouse,Rat -
Tartarate Resistant Acid Phosphatase (TRAcP/TRAP5) [ACP5/1070]
Description Tartrate resistant acid phosphatase (TRAcP) is a basic, iron-binding protein with high activity towards phosphoproteins, ATP and 4 nitrophenyl phosphate. Expression of TRAcP is reported to be increased in the spleen and monocytes of individuals with Gaucher’s disease, splenocytes and circulating white cells of individuals with hairy cell leukemia, spleens of individuals with Hodgkin disease, and the sera of individuals undergoing active bone turnover. Elevated levels are also reported to be associated with various B-cell and T-cell leukemias and lymphomas, placental decidual cells, syncytiotrophoblasts, and some macrophages distributed throughout maternal and embryonic tissues. The histochemical identification of hairy cell leukemia via tartrate-resistant acid phosphatase assay has been a standard for over two decades. Anti-TRAcP labels the cells of hairy cell leukemia (HCL) with a high degree of sensitivity and specificity. Worthy also of mention in this regard are anti-annexin A1 and Host Mouse Application Flow cytometry (FC), Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC) Reactivity Human, Mouse,Rat