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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 -
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 -
SPINK5/LEKTI [E9]
Description Serine peptidase inhibitor Kazal type 5 (SPINK5), also known Lympho-epithelial Kazal-type inhibitor (LEKTI) which is highly expressed in the thymus and stratum corneum, protects mucous epithelia against microbial attack and inflammation. SPINK5 is found in the oral mucosa, parathyroid gland, Bartholin's glands, tonsils, and vaginal epithelium. Very low levels are detected in lung, kidney, and prostate. SPINK5 is a marker of epithelial differentiation and expresses strongly in the granular and uppermost spinous layers of the epidermis and differentiated layers of stratified epithelia. Defects in SPINK5 are the cause of Netherton syndrome (NETH), a severe autosomal recessive disorder characterized by atopic dermatitis, hayfever and other conditions. (Shipping Cost: €200.00) Host Mouse Application Flow cytometry (FC), Immunohistochemistry (IHC) Reactivity Human, Mouse, Rat -
SPINK5/LEKTI [E9]
Description Serine peptidase inhibitor Kazal type 5 (SPINK5), also known Lympho-epithelial Kazal-type inhibitor (LEKTI) which is highly expressed in the thymus and stratum corneum, protects mucous epithelia against microbial attack and inflammation. SPINK5 is found in the oral mucosa, parathyroid gland, Bartholin's glands, tonsils, and vaginal epithelium. Very low levels are detected in lung, kidney, and prostate. SPINK5 is a marker of epithelial differentiation and expresses strongly in the granular and uppermost spinous layers of the epidermis and differentiated layers of stratified epithelia. Defects in SPINK5 are the cause of Netherton syndrome (NETH), a severe autosomal recessive disorder characterized by atopic dermatitis, hayfever and other conditions. (Shipping Cost: €200.00) Host Mouse Application Flow cytometry (FC), Immunohistochemistry (IHC) Reactivity Human, Mouse, Rat -
Substance P [SP-DE4-21]
Description Substance P (SP) is an active peptide, known as a Tachykinin, that affects diverse functions including blood pressure regulation, peristalsis of the gut, salivation and the modulation of cellular immunity. Fragments of Substance P have differential binding capacities for Substance P receptors and have varying biological activities. Substance P, Neurokinin A, Neuropeptide K, and Neuropeptide gamma are all generated by post-translation cleavage of the precursor Protachykinin-1. Substance P forms the major endogenous ligand for Neurokinin 1 Receptor. The pharmacology of Substance P has been associated with a number of neurological and psychiatric disorders, namely nociception, migraine, asthma, nausea, inflammatory bowel syndrome, urinary incontinence, anxiety and depression. It has also been linked to obesity. (Shipping Cost: €200.00) Host Mouse Application ELISA, Immunofluorescence (IF), Immunohistochemistry (IHC) 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