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Tubulin III Beta [UBB3/3732]
Description Tubulin is a major cytoskeleton component that has five distinct forms, designated α, β, γ, δ and ε tubulin. α and β Tubulins form heterodimers which multimerize to form a microtubule filament. Multiple β Tubulin isoforms (β1, β2, β3, β4, β5, β6 and β8) have been characterized and are expressed in mammalian tissues. β1 and β4 are present throughout the cytosol, β2 is present in the nuclei and nucleoplasm, and β3 is a neuron-specific cytoskeletal protein. γ Tubulin forms the gammasome, which is required for nucleating microtubule filaments at the centrosome. Both δ Tubulin and ε Tubulin are associated with the centrosome. δ Tubulin is a homolog of the Chlamydomonas δ Tubulin Uni3 and is found in association with the centrioles, whereas ε Tubulin localizes to the pericentriolar material. ε Tubulin exhibits a cell cycle-specific pattern of localization; first associ-ating with only the older of the centrosomes in a newly duplicated pair, and later associating with both centrosomes. (Shipp Host Mouse Application Immunocytochemistry (ICC),Immunofluorescence (IF), Immunoprecipitation (IP), Immunohistochemistry (IHC), Western Blot (WB) Reactivity Human, Rat, Mouse, Bovine -
Tubulin III Beta [UBB3/3732]
Description Tubulin is a major cytoskeleton component that has five distinct forms, designated α, β, γ, δ and ε tubulin. α and β Tubulins form heterodimers which multimerize to form a microtubule filament. Multiple β Tubulin isoforms (β1, β2, β3, β4, β5, β6 and β8) have been characterized and are expressed in mammalian tissues. β1 and β4 are present throughout the cytosol, β2 is present in the nuclei and nucleoplasm, and β3 is a neuron-specific cytoskeletal protein. γ Tubulin forms the gammasome, which is required for nucleating microtubule filaments at the centrosome. Both δ Tubulin and ε Tubulin are associated with the centrosome. δ Tubulin is a homolog of the Chlamydomonas δ Tubulin Uni3 and is found in association with the centrioles, whereas ε Tubulin localizes to the pericentriolar material. ε Tubulin exhibits a cell cycle-specific pattern of localization; first associ-ating with only the older of the centrosomes in a newly duplicated pair, and later associating with both centrosomes. (Shipp Host Mouse Application Immunocytochemistry (ICC),Immunofluorescence (IF), Immunoprecipitation (IP), Immunohistochemistry (IHC), Western Blot (WB) Reactivity Human, Rat, Mouse, Bovine -
Tumor necrosis factor/TNF alpha [TNFA/1172]
Description Tumor necrosis factor alpha (TNF-alpha) is a protein secreted by lipopolysaccharide-stimulated macrophages, and causes tumor necrosis when injected into tumor bearing mice. TNF-alpha is believed to mediate pathogenic shock and tissue injury associated with endotoxemia. TNFalpha exists as a multimer of two, three, or five non-covalently linked units, but shows a single 17kDa band following SDS-PAGE under non-reducing conditions. TNF-alpha is closely related to the 25kDa protein tumor necrosis factor beta (lymphotoxin), sharing the same receptors and cellular actions. TNF-alpha causes cytolysis of certain transformed cells, being synergistic with interferon gamma in its cytotoxicity. Although it has little effect on many cultured normal human cells, TNF-alpha appears to be directly toxic to vascular endothelial cells. Other actions of TNFalpha include stimulating growth of human fibroblasts and other cell lines, activating polymorphonuclear neutrophils and osteoclasts, and induction of i Host Mouse Application Flow cytometry (FC), Immunofluorescence (IF), Immunohistochemistry (IHC) Reactivity Human, Mouse, Rat, Rabbit, Cat, Dog -
Tumor necrosis factor/TNF alpha [TNFA/1172]
Description Tumor necrosis factor alpha (TNF-alpha) is a protein secreted by lipopolysaccharide-stimulated macrophages, and causes tumor necrosis when injected into tumor bearing mice. TNF-alpha is believed to mediate pathogenic shock and tissue injury associated with endotoxemia. TNFalpha exists as a multimer of two, three, or five non-covalently linked units, but shows a single 17kDa band following SDS-PAGE under non-reducing conditions. TNF-alpha is closely related to the 25kDa protein tumor necrosis factor beta (lymphotoxin), sharing the same receptors and cellular actions. TNF-alpha causes cytolysis of certain transformed cells, being synergistic with interferon gamma in its cytotoxicity. Although it has little effect on many cultured normal human cells, TNF-alpha appears to be directly toxic to vascular endothelial cells. Other actions of TNFalpha include stimulating growth of human fibroblasts and other cell lines, activating polymorphonuclear neutrophils and osteoclasts, and induction of i Host Mouse Application Flow cytometry (FC), Immunofluorescence (IF), Immunohistochemistry (IHC) Reactivity Human, Mouse, Rat, Rabbit, Cat, Dog -
Tumor necrosis factor/TNF beta/Lymphotoxin/LT alpha [9B9]
Description Lymphotoxin alpha or tumor necrosis beta, a member of the tumor necrosis factor family, is a cytokine produced by lymphocytes. LTA is highly inducible, secreted, and exists as homotrimeric molecule. LTA forms heterotrimers with lymphotoxin-beta which anchors lymphotoxin-alpha to the cell surface. LTA mediates a large variety of inflammatory, immunostimulatory, and antiviral responses. LTA is also involved in the formation of secondary lymphoid organs during development and plays a role in apoptosis. (Shipping Cost: €200.00) Host Mouse Application Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC), Western Blot (WB) Reactivity Human -
Tyrosinase [T311 + OCA1/812]
Description Tyrosinase is a key enzyme involved in the initial stages of melanin biosynthesis. Tyrosinase catalyzes the hydroxylation of tyrosine to 3,4-dihydroxyphenylalanine (DOPA). Oxidation reactions of DOPA to L-Dopaquinone and 5,6-dihydroxyindole (DHI) to indole-quinone occur spontaneously at physiological pH. Tyrosinase is expressed in melanin-producing cells such as melanocytes, which are primarily localized in the skin, hair bulbs and eyes. Low levels of tyrosinase mRNA was also detected in the human substantia nigra, but immunohistochemically unreactive. Since melanomas arise from melanocytes, there is evidence that tyrosinase is expressed in malignant melanomas. Studies have shown that tyrosinase is a sensitive and reliable marker to assess melanocytic lesions in paraffin-embedded tissue (Shipping Cost: €200.00) Host Mouse Application Flow cytometry (FC), Immunofluorescence (IF), Immunohistochemistry (IHC) Reactivity Human -
Uroplakin II [EPR18799]
Description Uroplakin II is a 15 kDa protein component of urothelial plaques. Studies have shown Uroplakin II mRNA was highly specific and was expressed in both bladder cancer tissues and peripheral blood of patients with primary and metastatic urothelial carcinoma of the bladder. Uroplakin II is a highly specific and may be useful in identifying tumors of urothelial origin. (Shipping Cost: €200.00) Host Rabbit Application Immunohistochemistry (IHC) Reactivity Human -
Uroplakin II [EPR18799]
Description Uroplakin II is a 15 kDa protein component of urothelial plaques. Studies have shown Uroplakin II mRNA was highly specific and was expressed in both bladder cancer tissues and peripheral blood of patients with primary and metastatic urothelial carcinoma of the bladder. Uroplakin II is a highly specific and may be useful in identifying tumors of urothelial origin. (Shipping Cost: €200.00) Host Rabbit Application Immunohistochemistry (IHC) Reactivity Human -
Uroplakin III [EPR14420]
Description Uroplakins (UPs) are a family of transmembrane proteins (UPs Ia, Ib, II and III) that are specific differentiation products of urothelial cells. In non-neoplastic mammalian urothelium, UPs are expressed in the luminal surface plasmalemma of superficial (umbrella) cells, forming complexes of 16 nm crystalline particles. Moll et al. reported that UPIII was detectable immunohistochemically in 29 of 55 primary (53%) and 23 of 35 metastatic (66%) urothelial carcinomas, whereas many non- urothelial carcinomas were UPIII-negative. The authors concluded that anti-UPIII should be a valuable marker, especially for the specific identification of urothelial carcinomas in patients with metastases of unknown primary site. Subsequently, Olsburgh et al. studied UP gene expression in normal urothelium and bladder cancer specimens, and found that expression was absent after malignant transformation. Ohtsuka et al. concluded in their studies that UPIII expression was strongly associated with lower tumor Host Rabbit Application Flow cytometry (FC), Immunohistochemistry (IHC) Reactivity Human -
Uroplakin III [EPR14420]
Description Uroplakins (UPs) are a family of transmembrane proteins (UPs Ia, Ib, II and III) that are specific differentiation products of urothelial cells. In non-neoplastic mammalian urothelium, UPs are expressed in the luminal surface plasmalemma of superficial (umbrella) cells, forming complexes of 16 nm crystalline particles. Moll et al. reported that UPIII was detectable immunohistochemically in 29 of 55 primary (53%) and 23 of 35 metastatic (66%) urothelial carcinomas, whereas many non- urothelial carcinomas were UPIII-negative. The authors concluded that anti-UPIII should be a valuable marker, especially for the specific identification of urothelial carcinomas in patients with metastases of unknown primary site. Subsequently, Olsburgh et al. studied UP gene expression in normal urothelium and bladder cancer specimens, and found that expression was absent after malignant transformation. Ohtsuka et al. concluded in their studies that UPIII expression was strongly associated with lower tumor Host Rabbit Application Flow cytometry (FC), Immunohistochemistry (IHC) Reactivity Human