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  • Lipase member H is a novel secreted protein selectively upregulated in human lung adenocarcinomas and bronchioloalveolar carcinomas.

Lipase member H is a novel secreted protein selectively upregulated in human lung adenocarcinomas and bronchioloalveolar carcinomas.

Biochemical and biophysical research communications (2014-01-02)
Yasuhiro Seki, Yukihiro Yoshida, Hisako Ishimine, Aya Shinozaki-Ushiku, Yoshimasa Ito, Kenya Sumitomo, Jun Nakajima, Masashi Fukayama, Tatsuo Michiue, Makoto Asashima, Akira Kurisaki
ZUSAMMENFASSUNG

Lung cancer is one of the most frequent causes of cancer-related death worldwide. However, molecular markers for lung cancer have not been well established. To identify novel genes related to lung cancer development, we surveyed publicly available DNA microarray data on lung cancer tissues. We identified lipase member H (LIPH, also known as mPA-PLA1) as one of the significantly upregulated genes in lung adenocarcinoma. LIPH was expressed in several adenocarcinoma cell lines when they were analyzed by quantitative real-time polymerase chain reaction (qPCR), western blotting, and sandwich enzyme-linked immunosorbent assay (ELISA). Immunohistochemical analysis detected LIPH expression in most of the adenocarcinomas and bronchioloalveolar carcinomas tissue sections obtained from lung cancer patients. LIPH expression was also observed less frequently in the squamous lung cancer tissue samples. Furthermore, LIPH protein was upregulated in the serum of early- and late-phase lung cancer patients when they were analyzed by ELISA. Interestingly, high serum level of LIPH was correlated with better survival in early phase lung cancer patients after surgery. Thus, LIPH may be a novel molecular biomarker for lung cancer, especially for adenocarcinoma and bronchioloalveolar carcinoma.

MATERIALIEN
Produktnummer
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Produktbeschreibung

Sigma-Aldrich
Lipase aus Candida rugosa, Type VII, ≥700 unit/mg solid
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Lipase aus Schweinepankreas, Type II, ≥125 units/mg protein (using olive oil (30 min incubation)), 30-90 units/mg protein (using triacetin)
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Lipase-Acrylharz aus Candida antarctica, ≥5,000 U/g, recombinant, expressed in Aspergillus niger
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Lipase aus Schweinepankreas, Type VI-S, ≥20,000 units/mg protein, lyophilized powder
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Lipase B Candida antarctica, rekombinant aus Aspergillus oryzae, powder, beige, ~9 U/mg
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Lipase aus Aspergillus niger, powder (fine), ~200 U/g
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Lipase aus Aspergillus oryzae, solution, ≥100,000 U/g, white, beige
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Lipase aus Candida rugosa, lyophilized powder, ≥40,000 units/mg protein
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Lipase, immobilisiert aus Candida antarctica, beads, slightly brown, >2 U/mg
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Lipase aus Candida sp., recombinant, expressed in Aspergillus niger
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Lipase aus Rhizomucor miehei, ≥20,000 U/g
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Lipase aus Pseudomonas cepacia, powder, light beige, ≥30 U/mg
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Lipase aus Weizenkeimen, Type I, lyophilized powder, 5-15 units/mg solid
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Lipase aus Rhizopus oryzae, powder (fine), ~10 U/mg
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Lipase aus Aspergillus oryzae, lyophilized, powder, white, ~50 U/mg
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Lipase aus Pseudomonas sp., Type XIII, lyophilized powder, ≥15 units/mg solid
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Lipase aus Candida rugosa, powder, yellow-brown, ≥2 U/mg
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Lipase aus Candida rugosa, lyophilized, powder (fine), 15-25 U/mg
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Lipase aus Mucor miehei, lyophilized powder, ≥4,000 units/mg solid (using olive oil)
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Lipase aus Mucor miehei, powder, slightly brown, ~1 U/mg
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Lipase aus Rhizopus niveus, powder (fine), ≥1.5 U/mg
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Lipase aus Mucor javanicus, lyophilized powder, ≥300 units/mg solid (using olive oil)
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Lipase A Candida antarctica, rekombinant aus Aspergillus oryzae, powder, beige, ~2 U/mg