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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
ABSTRACT

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.

MATERIALS
Product Number
Brand
Product Description

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