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  • The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment.

The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment.

Genome research (2003-09-17)
Hilary F Clark, Austin L Gurney, Evangeline Abaya, Kevin Baker, Daryl Baldwin, Jennifer Brush, Jian Chen, Bernard Chow, Clarissa Chui, Craig Crowley, Bridget Currell, Bethanne Deuel, Patrick Dowd, Dan Eaton, Jessica Foster, Christopher Grimaldi, Qimin Gu, Philip E Hass, Sherry Heldens, Arthur Huang, Hok Seon Kim, Laura Klimowski, Yisheng Jin, Stephanie Johnson, James Lee, Lhney Lewis, Dongzhou Liao, Melanie Mark, Edward Robbie, Celina Sanchez, Jill Schoenfeld, Somasekar Seshagiri, Laura Simmons, Jennifer Singh, Victoria Smith, Jeremy Stinson, Alicia Vagts, Richard Vandlen, Colin Watanabe, David Wieand, Kathryn Woods, Ming-Hong Xie, Daniel Yansura, Sothy Yi, Guoying Yu, Jean Yuan, Min Zhang, Zemin Zhang, Audrey Goddard, William I Wood, Paul Godowski, Alane Gray
要旨

A large-scale effort, termed the Secreted Protein Discovery Initiative (SPDI), was undertaken to identify novel secreted and transmembrane proteins. In the first of several approaches, a biological signal sequence trap in yeast cells was utilized to identify cDNA clones encoding putative secreted proteins. A second strategy utilized various algorithms that recognize features such as the hydrophobic properties of signal sequences to identify putative proteins encoded by expressed sequence tags (ESTs) from human cDNA libraries. A third approach surveyed ESTs for protein sequence similarity to a set of known receptors and their ligands with the BLAST algorithm. Finally, both signal-sequence prediction algorithms and BLAST were used to identify single exons of potential genes from within human genomic sequence. The isolation of full-length cDNA clones for each of these candidate genes resulted in the identification of >1000 novel proteins. A total of 256 of these cDNAs are still novel, including variants and novel genes, per the most recent GenBank release version. The success of this large-scale effort was assessed by a bioinformatics analysis of the proteins through predictions of protein domains, subcellular localizations, and possible functional roles. The SPDI collection should facilitate efforts to better understand intercellular communication, may lead to new understandings of human diseases, and provides potential opportunities for the development of therapeutics.

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製品内容

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リパーゼ Candida rugosa由来, Type VII, ≥700 unit/mg solid
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リパーゼ ブタ膵臓由来, Type II, ≥125 units/mg protein (using olive oil (30 min incubation)), 30-90 units/mg protein (using triacetin)
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酸性ホスファターゼ コムギ胚芽由来, ≥0.4 unit/mg solid
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リパーゼ・アクリル樹脂 from Candida antarctica, ≥5,000 U/g, recombinant, expressed in Aspergillus niger
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酸性ホスファターゼ ジャガイモ由来, lyophilized powder, ≥0.5 unit/mg solid
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リパーゼ ブタ膵臓由来, Type VI-S, ≥20,000 units/mg protein, lyophilized powder
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リパーゼB, Candida antarctica由来, 組換え体 from Aspergillus oryzae, powder, beige, ~9 U/mg
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ホスホリパーゼA2 from honey bee venom (Apis mellifera), salt-free, lyophilized powder, 600-2400 units/mg protein
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リパーゼ from Aspergillus niger, powder (fine), ~200 U/g
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リパーゼ Candida rugosa由来, lyophilized powder, ≥40,000 units/mg protein
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Lipase immobilized from Candida antarctica, beads, slightly brown, >2 U/mg
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ホスホリパーゼA2 ウシ膵臓由来, lyophilized powder, ≥20 units/mg protein
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ホスホリパーゼA2 ブタ膵臓由来, ammonium sulfate suspension, ≥600 units/mg protein
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酸性ホスファターゼ ジャガイモ由来, lyophilized powder, ≥3.0 units/mg solid
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リパーゼ Candida sp.(カンジダ属)由来, recombinant, expressed in Aspergillus niger
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リパーゼ from Rhizomucor miehei, ≥20,000 U/g
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ホスホリパーゼD from Streptomyces chromofuscus, ≥50,000 units/mL, buffered aqueous glycerol solution
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β-ヒドロキシ酪酸デヒドロゲナーゼ Pseudomonas lemoignei由来, lyophilized powder, ≥200 units/mg protein
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酸性ホスファターゼ from sweet potato, ammonium sulfate suspension, ≥10.0 units/mg protein (modified Warburg-Christian)
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ホスホリパーゼD 放線菌由来, Type VII, lyophilized powder, ≥150 units/mg solid
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ホスホリパーゼD キャベツ由来, Type IV, lyophilized powder, ≥100 units/mg solid
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リパーゼ Pseudomonas cepacia由来, powder, light beige, ≥30 U/mg
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スフィンゴミエリナーゼ Bacillus cereus由来, lyophilized powder, ≥100 units/mg protein
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リパーゼ コムギ胚芽由来, Type I, lyophilized powder, 5-15 units/mg solid
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スフィンゴミエリナーゼ Bacillus cereus由来, buffered aqueous glycerol solution, ≥100 units/mg protein (Lowry)
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L-アミノ酸オキシダーゼ from Crotalus adamanteus, Type I (dried venom)
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リパーゼ from Rhizopus oryzae, powder (fine), ~10 U/mg
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スフィンゴミエリナーゼ Staphylococcus aureus由来, buffered aqueous glycerol solution, 100-300 units/mg protein (Lowry)
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リパーゼ from Aspergillus oryzae, lyophilized, powder, white, ~50 U/mg
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リパーゼ Pseudomonassp. (シュードモナス)由来, Type XIII, lyophilized powder, ≥15 units/mg solid