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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 -
SUMO-2/3 [SM23/496]
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), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human -
SUMO-2/3 [SM23/496]
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), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human -
Superoxide Dismutase 1/SOD1 [MD11]
Description Superoxide Dismutase (SOD) or CuZn-SOD (SOD1), a cytoplasmic and mitochondrial intermembrane space protein is located on human chromosome 21q22. It belongs to superoxide dismutase multigene family. It binds copper and zinc ions and is one of two isozymes responsible for destroying free superoxide radicals in the body. This isozyme is a soluble cytoplasmic protein, acting as a homodimer to convert naturally-occuring but harmful superoxide radicals to molecular oxygen and hydrogen peroxide. The other isozyme is a mitochondrial protein. Mutations in this gene have been implicated as causes of familial amyotrophic lateral sclerosis. Rare transcript variants have been reported for this gene. (Shipping Cost: €200.00) Host Mouse Application ELISA, Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human -
Superoxide Dismutase 1/SOD1 [MD11]
Description Superoxide Dismutase (SOD) or CuZn-SOD (SOD1), a cytoplasmic and mitochondrial intermembrane space protein is located on human chromosome 21q22. It belongs to superoxide dismutase multigene family. It binds copper and zinc ions and is one of two isozymes responsible for destroying free superoxide radicals in the body. This isozyme is a soluble cytoplasmic protein, acting as a homodimer to convert naturally-occuring but harmful superoxide radicals to molecular oxygen and hydrogen peroxide. The other isozyme is a mitochondrial protein. Mutations in this gene have been implicated as causes of familial amyotrophic lateral sclerosis. Rare transcript variants have been reported for this gene. (Shipping Cost: €200.00) Host Mouse Application ELISA, Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human -
Surfactant/SP-B [1B9]
Description ProSP-B is glycosylated in the Golgi apparatus and undergoes carboxy- and amino-terminal proteolysis by a cathepsin D-like protease. Pulmonary surfactant is a complex mixture of phospholipids and proteins that is secreted from type II cells in alveoli and reduces the surface tension at the alveolar air-liquid interface, providing alveolar stability necessary for normal ventillation. Four distinct proteins isolated from pulmonary surfactant are termed surfactant proteins A, B, C, and D. SP-A (28-36kDa) and SP-D (43kDa) are collagenous carbohydrate-binding proteins, whereas SP-B (8-9kDa) and SP -C (4kDa) are non-collagenous hydrophobic proteins. SP-B is expressed in pulmonary adenocarcinomas with acinar, papillary, bronchioloalveolar, and solid growth patterns. Squamous cell and large cell carcinomas of the lung and nonpulmonary adenocarcinomas do not express SP-B. (Shipping Cost: €200.00) Host Mouse Application Immunocytochemistry (ICC), Immunofluorescence (IF), Immunohistochemistry (IHC), Western Blot (WB) Reactivity Human -
Surfactant/SP-B [1B9]
Description ProSP-B is glycosylated in the Golgi apparatus and undergoes carboxy- and amino-terminal proteolysis by a cathepsin D-like protease. Pulmonary surfactant is a complex mixture of phospholipids and proteins that is secreted from type II cells in alveoli and reduces the surface tension at the alveolar air-liquid interface, providing alveolar stability necessary for normal ventillation. Four distinct proteins isolated from pulmonary surfactant are termed surfactant proteins A, B, C, and D. SP-A (28-36kDa) and SP-D (43kDa) are collagenous carbohydrate-binding proteins, whereas SP-B (8-9kDa) and SP -C (4kDa) are non-collagenous hydrophobic proteins. SP-B is expressed in pulmonary adenocarcinomas with acinar, papillary, bronchioloalveolar, and solid growth patterns. Squamous cell and large cell carcinomas of the lung and nonpulmonary adenocarcinomas do not express SP-B. (Shipping Cost: €200.00) Host Mouse Application Immunocytochemistry (ICC), Immunofluorescence (IF), Immunohistochemistry (IHC), Western Blot (WB) Reactivity Human -
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