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wizard mini-preparation kit
Wizard Mini Preparation Kit, supplied by Promega, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/wizard+mini-preparation+kit/wizard+mini+preparation+kit/pm27208884-46-7-10
Average 90 stars, based on 1 article reviews
Wizard Mini Preparation Kit, supplied by Promega, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/wizard+mini-preparation+kit/wizard+mini+preparation+kit/pm27208884-46-7-10
Average 90 stars, based on 1 article reviews
wizard mini-preparation kit - by Bioz Stars,
2026-10
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Plasmid Preparation:Article Title: Molecular characterization of a Niemann–Pick disease type C2 protein from the honeybee Apis cerana Article Snippet: Molecular characterization of a Niemann-Pick disease type C2 protein from the honeybee Apis cerana Kwang Sik Lee, Hee Geun Park, Deng Yijie, Bo Yeon Kim, Seung Su Kyung, Yong Soo Choi, Hyung Joo Yoon, Mingshun Li, Byung Rae Jin PII: S1226-8615(14)00065-X DOI: doi: 10.1016/j.aspen.2014.05.005 Reference: ASPEN 535 To appear in: Journal of Asia-Pacific Entomology Received date: 9 April 2014 Revised date: 7 May 2014 Accepted date: 14 May 2014 Please cite this article as: Lee, Kwang Sik, Park, Hee Geun, Yijie, Deng, Kim, Bo Yeon, Kyung, Seung Su, Choi, Yong Soo, Yoon, Hyung Joo, Li, Mingshun, Jin, Byung Rae, Molecular characterization of a Niemann-Pick disease type C2 protein from the honeybee Apis cerana, Journal of Asia-Pacific Entomology (2014), doi: 10.1016/j.aspen.2014.05.005 This is a PDF file of an unedited manuscript that has been accepted for publication.. As a service to our customers we are providing this early version of the manuscript.. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Article Title: Molecular characterization of a venom acid phosphatase from the Asiatic honeybee Apis cerana Article Snippet: Article history: Received 13 June 2016 Revised 20 July 2016 Accepted 24 July 2016 Available online 26 July 2016 Bee venom contains a variety of toxic components, including enzymes, peptides, and biogenic amines.. An acid phosphatase Acph-1-like protein has been identified from Asiatic honeybee (Apis cerana) venom.. However, no molecular information is currently available for acid phosphatases from A. cerana venom. Article Title: Apolipophorin III from honeybees (Apis cerana) exhibits antibacterial activity. Article Snippet: Article history: Received 20 August 2014 Received in revised form 28 November 2014 Accepted 29 November 2014 Available online 5 December 2014 Article Title: Dual function of a bee (Apis cerana) inhibitor cysteine knot peptide that acts as an antifungal peptide and insecticidal venom toxin. Article Snippet: Inhibitor cysteine knot (ICK) peptides exhibit ion channel blocking, insecticidal, and antimicrobial activities, but currently, no functional roles for bee-derived ICK peptides have been identified.. In this study, a bee (Apis cerana) ICK peptide (AcICK) that acts as an antifungal peptide and as an insecticidal venom toxin was identified.. AcICK contains an ICK fold that is expressed in the epidermis, fat body, or venom gland and is present as a 6.6-kDa peptide in bee venom. Article Title: A bumblebee (Bombus ignitus) venom serine protease inhibitor that acts as a microbial serine protease inhibitor. Article Snippet: Contents lists available at ScienceDirect Comparative Biochemistry and Physiology, Part B j ourna l homepage: www.e lsev ie r .com/ locate /cbpb A bumblebee (Bombus ignitus) venom serine protease inhibitor that acts as a microbial serine protease inhibitor Hu Wan a,1, Bo Yeon Kim a,1, Kwang Sik Lee a, Hyung Joo Yoon b, Kyung Yong Lee b, Byung Rae Jin a,⁎ a College of Natural Resources and Life Science, Dong-A University, Busan 604-714, Republic of Korea b Department of Agricultural Biology, National Academy of Agricultural Science, Suwon, Republic of Korea ⁎ Corresponding author.. Tel./fax: +82 51 200 7594.. E-mail address: brjin@dau.ac.kr (B.R. Article Title: Secapin, a bee venom peptide, exhibits anti-fibrinolytic, anti-elastolytic, and anti-microbial activities. Article Snippet: Bee venom contains a variety of peptide constituents that have various biological, toxicological, and pharmacological actions.. However, the biological actions of secapin, a venom peptide in bee venom, remain largely unknown.. Here, we provide the evidence that Asiatic honeybee (Apis cerana) secapin (AcSecapin-1) exhibits anti-fibrinolytic, anti-elastolytic, and anti-microbial activities. Article Title: Peroxiredoxin 5 from common cutworm (Spodoptera litura) acts as a potent antioxidant enzyme. Article Snippet: Article history: Received 23 April 2014 Received in revised form 24 June 2014 Accepted 27 June 2014 Available online 4 July 2014 Sequencing:Article Title: Molecular characterization of a Niemann–Pick disease type C2 protein from the honeybee Apis cerana Article Snippet: Molecular characterization of a Niemann-Pick disease type C2 protein from the honeybee Apis cerana Kwang Sik Lee, Hee Geun Park, Deng Yijie, Bo Yeon Kim, Seung Su Kyung, Yong Soo Choi, Hyung Joo Yoon, Mingshun Li, Byung Rae Jin PII: S1226-8615(14)00065-X DOI: doi: 10.1016/j.aspen.2014.05.005 Reference: ASPEN 535 To appear in: Journal of Asia-Pacific Entomology Received date: 9 April 2014 Revised date: 7 May 2014 Accepted date: 14 May 2014 Please cite this article as: Lee, Kwang Sik, Park, Hee Geun, Yijie, Deng, Kim, Bo Yeon, Kyung, Seung Su, Choi, Yong Soo, Yoon, Hyung Joo, Li, Mingshun, Jin, Byung Rae, Molecular characterization of a Niemann-Pick disease type C2 protein from the honeybee Apis cerana, Journal of Asia-Pacific Entomology (2014), doi: 10.1016/j.aspen.2014.05.005 This is a PDF file of an unedited manuscript that has been accepted for publication.. As a service to our customers we are providing this early version of the manuscript.. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Article Title: Molecular characterization of a venom acid phosphatase from the Asiatic honeybee Apis cerana Article Snippet: Article history: Received 13 June 2016 Revised 20 July 2016 Accepted 24 July 2016 Available online 26 July 2016 Bee venom contains a variety of toxic components, including enzymes, peptides, and biogenic amines.. An acid phosphatase Acph-1-like protein has been identified from Asiatic honeybee (Apis cerana) venom.. However, no molecular information is currently available for acid phosphatases from A. cerana venom. Article Title: Apolipophorin III from honeybees (Apis cerana) exhibits antibacterial activity. Article Snippet: Article history: Received 20 August 2014 Received in revised form 28 November 2014 Accepted 29 November 2014 Available online 5 December 2014 Article Title: Dual function of a bee (Apis cerana) inhibitor cysteine knot peptide that acts as an antifungal peptide and insecticidal venom toxin. Article Snippet: Inhibitor cysteine knot (ICK) peptides exhibit ion channel blocking, insecticidal, and antimicrobial activities, but currently, no functional roles for bee-derived ICK peptides have been identified.. In this study, a bee (Apis cerana) ICK peptide (AcICK) that acts as an antifungal peptide and as an insecticidal venom toxin was identified.. AcICK contains an ICK fold that is expressed in the epidermis, fat body, or venom gland and is present as a 6.6-kDa peptide in bee venom. Article Title: A bumblebee (Bombus ignitus) venom serine protease inhibitor that acts as a microbial serine protease inhibitor. Article Snippet: Contents lists available at ScienceDirect Comparative Biochemistry and Physiology, Part B j ourna l homepage: www.e lsev ie r .com/ locate /cbpb A bumblebee (Bombus ignitus) venom serine protease inhibitor that acts as a microbial serine protease inhibitor Hu Wan a,1, Bo Yeon Kim a,1, Kwang Sik Lee a, Hyung Joo Yoon b, Kyung Yong Lee b, Byung Rae Jin a,⁎ a College of Natural Resources and Life Science, Dong-A University, Busan 604-714, Republic of Korea b Department of Agricultural Biology, National Academy of Agricultural Science, Suwon, Republic of Korea ⁎ Corresponding author.. Tel./fax: +82 51 200 7594.. E-mail address: brjin@dau.ac.kr (B.R. Article Title: Secapin, a bee venom peptide, exhibits anti-fibrinolytic, anti-elastolytic, and anti-microbial activities. Article Snippet: Bee venom contains a variety of peptide constituents that have various biological, toxicological, and pharmacological actions.. However, the biological actions of secapin, a venom peptide in bee venom, remain largely unknown.. Here, we provide the evidence that Asiatic honeybee (Apis cerana) secapin (AcSecapin-1) exhibits anti-fibrinolytic, anti-elastolytic, and anti-microbial activities. Article Title: Peroxiredoxin 5 from common cutworm (Spodoptera litura) acts as a potent antioxidant enzyme. Article Snippet: Article history: Received 23 April 2014 Received in revised form 24 June 2014 Accepted 27 June 2014 Available online 4 July 2014 DNA Extraction:Article Title: Molecular characterization of a Niemann–Pick disease type C2 protein from the honeybee Apis cerana Article Snippet: Molecular characterization of a Niemann-Pick disease type C2 protein from the honeybee Apis cerana Kwang Sik Lee, Hee Geun Park, Deng Yijie, Bo Yeon Kim, Seung Su Kyung, Yong Soo Choi, Hyung Joo Yoon, Mingshun Li, Byung Rae Jin PII: S1226-8615(14)00065-X DOI: doi: 10.1016/j.aspen.2014.05.005 Reference: ASPEN 535 To appear in: Journal of Asia-Pacific Entomology Received date: 9 April 2014 Revised date: 7 May 2014 Accepted date: 14 May 2014 Please cite this article as: Lee, Kwang Sik, Park, Hee Geun, Yijie, Deng, Kim, Bo Yeon, Kyung, Seung Su, Choi, Yong Soo, Yoon, Hyung Joo, Li, Mingshun, Jin, Byung Rae, Molecular characterization of a Niemann-Pick disease type C2 protein from the honeybee Apis cerana, Journal of Asia-Pacific Entomology (2014), doi: 10.1016/j.aspen.2014.05.005 This is a PDF file of an unedited manuscript that has been accepted for publication.. As a service to our customers we are providing this early version of the manuscript.. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Article Title: Molecular characterization of a venom acid phosphatase from the Asiatic honeybee Apis cerana Article Snippet: Article history: Received 13 June 2016 Revised 20 July 2016 Accepted 24 July 2016 Available online 26 July 2016 Bee venom contains a variety of toxic components, including enzymes, peptides, and biogenic amines.. An acid phosphatase Acph-1-like protein has been identified from Asiatic honeybee (Apis cerana) venom.. However, no molecular information is currently available for acid phosphatases from A. cerana venom. Article Title: Apolipophorin III from honeybees (Apis cerana) exhibits antibacterial activity. Article Snippet: Article history: Received 20 August 2014 Received in revised form 28 November 2014 Accepted 29 November 2014 Available online 5 December 2014 Article Title: Dual function of a bee (Apis cerana) inhibitor cysteine knot peptide that acts as an antifungal peptide and insecticidal venom toxin. Article Snippet: Inhibitor cysteine knot (ICK) peptides exhibit ion channel blocking, insecticidal, and antimicrobial activities, but currently, no functional roles for bee-derived ICK peptides have been identified.. In this study, a bee (Apis cerana) ICK peptide (AcICK) that acts as an antifungal peptide and as an insecticidal venom toxin was identified.. AcICK contains an ICK fold that is expressed in the epidermis, fat body, or venom gland and is present as a 6.6-kDa peptide in bee venom. Article Title: A bumblebee (Bombus ignitus) venom serine protease inhibitor that acts as a microbial serine protease inhibitor. Article Snippet: Contents lists available at ScienceDirect Comparative Biochemistry and Physiology, Part B j ourna l homepage: www.e lsev ie r .com/ locate /cbpb A bumblebee (Bombus ignitus) venom serine protease inhibitor that acts as a microbial serine protease inhibitor Hu Wan a,1, Bo Yeon Kim a,1, Kwang Sik Lee a, Hyung Joo Yoon b, Kyung Yong Lee b, Byung Rae Jin a,⁎ a College of Natural Resources and Life Science, Dong-A University, Busan 604-714, Republic of Korea b Department of Agricultural Biology, National Academy of Agricultural Science, Suwon, Republic of Korea ⁎ Corresponding author.. Tel./fax: +82 51 200 7594.. E-mail address: brjin@dau.ac.kr (B.R. Article Title: Secapin, a bee venom peptide, exhibits anti-fibrinolytic, anti-elastolytic, and anti-microbial activities. Article Snippet: Bee venom contains a variety of peptide constituents that have various biological, toxicological, and pharmacological actions.. However, the biological actions of secapin, a venom peptide in bee venom, remain largely unknown.. Here, we provide the evidence that Asiatic honeybee (Apis cerana) secapin (AcSecapin-1) exhibits anti-fibrinolytic, anti-elastolytic, and anti-microbial activities. Article Title: Peroxiredoxin 5 from common cutworm (Spodoptera litura) acts as a potent antioxidant enzyme. Article Snippet: Article history: Received 23 April 2014 Received in revised form 24 June 2014 Accepted 27 June 2014 Available online 4 July 2014 Isolation:Article Title: Molecular characterization of a Niemann–Pick disease type C2 protein from the honeybee Apis cerana Article Snippet: Molecular characterization of a Niemann-Pick disease type C2 protein from the honeybee Apis cerana Kwang Sik Lee, Hee Geun Park, Deng Yijie, Bo Yeon Kim, Seung Su Kyung, Yong Soo Choi, Hyung Joo Yoon, Mingshun Li, Byung Rae Jin PII: S1226-8615(14)00065-X DOI: doi: 10.1016/j.aspen.2014.05.005 Reference: ASPEN 535 To appear in: Journal of Asia-Pacific Entomology Received date: 9 April 2014 Revised date: 7 May 2014 Accepted date: 14 May 2014 Please cite this article as: Lee, Kwang Sik, Park, Hee Geun, Yijie, Deng, Kim, Bo Yeon, Kyung, Seung Su, Choi, Yong Soo, Yoon, Hyung Joo, Li, Mingshun, Jin, Byung Rae, Molecular characterization of a Niemann-Pick disease type C2 protein from the honeybee Apis cerana, Journal of Asia-Pacific Entomology (2014), doi: 10.1016/j.aspen.2014.05.005 This is a PDF file of an unedited manuscript that has been accepted for publication.. As a service to our customers we are providing this early version of the manuscript.. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Article Title: Molecular characterization of a venom acid phosphatase from the Asiatic honeybee Apis cerana Article Snippet: Article history: Received 13 June 2016 Revised 20 July 2016 Accepted 24 July 2016 Available online 26 July 2016 Bee venom contains a variety of toxic components, including enzymes, peptides, and biogenic amines.. An acid phosphatase Acph-1-like protein has been identified from Asiatic honeybee (Apis cerana) venom.. However, no molecular information is currently available for acid phosphatases from A. cerana venom. Article Title: Apolipophorin III from honeybees (Apis cerana) exhibits antibacterial activity. Article Snippet: Article history: Received 20 August 2014 Received in revised form 28 November 2014 Accepted 29 November 2014 Available online 5 December 2014 Article Title: Dual function of a bee (Apis cerana) inhibitor cysteine knot peptide that acts as an antifungal peptide and insecticidal venom toxin. Article Snippet: Inhibitor cysteine knot (ICK) peptides exhibit ion channel blocking, insecticidal, and antimicrobial activities, but currently, no functional roles for bee-derived ICK peptides have been identified.. In this study, a bee (Apis cerana) ICK peptide (AcICK) that acts as an antifungal peptide and as an insecticidal venom toxin was identified.. AcICK contains an ICK fold that is expressed in the epidermis, fat body, or venom gland and is present as a 6.6-kDa peptide in bee venom. Article Title: A bumblebee (Bombus ignitus) venom serine protease inhibitor that acts as a microbial serine protease inhibitor. Article Snippet: Contents lists available at ScienceDirect Comparative Biochemistry and Physiology, Part B j ourna l homepage: www.e lsev ie r .com/ locate /cbpb A bumblebee (Bombus ignitus) venom serine protease inhibitor that acts as a microbial serine protease inhibitor Hu Wan a,1, Bo Yeon Kim a,1, Kwang Sik Lee a, Hyung Joo Yoon b, Kyung Yong Lee b, Byung Rae Jin a,⁎ a College of Natural Resources and Life Science, Dong-A University, Busan 604-714, Republic of Korea b Department of Agricultural Biology, National Academy of Agricultural Science, Suwon, Republic of Korea ⁎ Corresponding author.. Tel./fax: +82 51 200 7594.. E-mail address: brjin@dau.ac.kr (B.R. Article Title: Secapin, a bee venom peptide, exhibits anti-fibrinolytic, anti-elastolytic, and anti-microbial activities. Article Snippet: Bee venom contains a variety of peptide constituents that have various biological, toxicological, and pharmacological actions.. However, the biological actions of secapin, a venom peptide in bee venom, remain largely unknown.. Here, we provide the evidence that Asiatic honeybee (Apis cerana) secapin (AcSecapin-1) exhibits anti-fibrinolytic, anti-elastolytic, and anti-microbial activities. Article Title: Peroxiredoxin 5 from common cutworm (Spodoptera litura) acts as a potent antioxidant enzyme. Article Snippet: Article history: Received 23 April 2014 Received in revised form 24 June 2014 Accepted 27 June 2014 Available online 4 July 2014 Generated:Article Title: Molecular characterization of a Niemann–Pick disease type C2 protein from the honeybee Apis cerana Article Snippet: Molecular characterization of a Niemann-Pick disease type C2 protein from the honeybee Apis cerana Kwang Sik Lee, Hee Geun Park, Deng Yijie, Bo Yeon Kim, Seung Su Kyung, Yong Soo Choi, Hyung Joo Yoon, Mingshun Li, Byung Rae Jin PII: S1226-8615(14)00065-X DOI: doi: 10.1016/j.aspen.2014.05.005 Reference: ASPEN 535 To appear in: Journal of Asia-Pacific Entomology Received date: 9 April 2014 Revised date: 7 May 2014 Accepted date: 14 May 2014 Please cite this article as: Lee, Kwang Sik, Park, Hee Geun, Yijie, Deng, Kim, Bo Yeon, Kyung, Seung Su, Choi, Yong Soo, Yoon, Hyung Joo, Li, Mingshun, Jin, Byung Rae, Molecular characterization of a Niemann-Pick disease type C2 protein from the honeybee Apis cerana, Journal of Asia-Pacific Entomology (2014), doi: 10.1016/j.aspen.2014.05.005 This is a PDF file of an unedited manuscript that has been accepted for publication.. As a service to our customers we are providing this early version of the manuscript.. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Article Title: Molecular characterization of a venom acid phosphatase from the Asiatic honeybee Apis cerana Article Snippet: Article history: Received 13 June 2016 Revised 20 July 2016 Accepted 24 July 2016 Available online 26 July 2016 Bee venom contains a variety of toxic components, including enzymes, peptides, and biogenic amines.. An acid phosphatase Acph-1-like protein has been identified from Asiatic honeybee (Apis cerana) venom.. However, no molecular information is currently available for acid phosphatases from A. cerana venom. Article Title: Apolipophorin III from honeybees (Apis cerana) exhibits antibacterial activity. Article Snippet: Article history: Received 20 August 2014 Received in revised form 28 November 2014 Accepted 29 November 2014 Available online 5 December 2014 Article Title: Dual function of a bee (Apis cerana) inhibitor cysteine knot peptide that acts as an antifungal peptide and insecticidal venom toxin. Article Snippet: Inhibitor cysteine knot (ICK) peptides exhibit ion channel blocking, insecticidal, and antimicrobial activities, but currently, no functional roles for bee-derived ICK peptides have been identified.. In this study, a bee (Apis cerana) ICK peptide (AcICK) that acts as an antifungal peptide and as an insecticidal venom toxin was identified.. AcICK contains an ICK fold that is expressed in the epidermis, fat body, or venom gland and is present as a 6.6-kDa peptide in bee venom. Article Title: A bumblebee (Bombus ignitus) venom serine protease inhibitor that acts as a microbial serine protease inhibitor. Article Snippet: Contents lists available at ScienceDirect Comparative Biochemistry and Physiology, Part B j ourna l homepage: www.e lsev ie r .com/ locate /cbpb A bumblebee (Bombus ignitus) venom serine protease inhibitor that acts as a microbial serine protease inhibitor Hu Wan a,1, Bo Yeon Kim a,1, Kwang Sik Lee a, Hyung Joo Yoon b, Kyung Yong Lee b, Byung Rae Jin a,⁎ a College of Natural Resources and Life Science, Dong-A University, Busan 604-714, Republic of Korea b Department of Agricultural Biology, National Academy of Agricultural Science, Suwon, Republic of Korea ⁎ Corresponding author.. Tel./fax: +82 51 200 7594.. E-mail address: brjin@dau.ac.kr (B.R. Article Title: Secapin, a bee venom peptide, exhibits anti-fibrinolytic, anti-elastolytic, and anti-microbial activities. Article Snippet: Bee venom contains a variety of peptide constituents that have various biological, toxicological, and pharmacological actions.. However, the biological actions of secapin, a venom peptide in bee venom, remain largely unknown.. Here, we provide the evidence that Asiatic honeybee (Apis cerana) secapin (AcSecapin-1) exhibits anti-fibrinolytic, anti-elastolytic, and anti-microbial activities. Article Title: Peroxiredoxin 5 from common cutworm (Spodoptera litura) acts as a potent antioxidant enzyme. Article Snippet: Article history: Received 23 April 2014 Received in revised form 24 June 2014 Accepted 27 June 2014 Available online 4 July 2014 cDNA Library Assay:Article Title: Molecular characterization of a Niemann–Pick disease type C2 protein from the honeybee Apis cerana Article Snippet: Molecular characterization of a Niemann-Pick disease type C2 protein from the honeybee Apis cerana Kwang Sik Lee, Hee Geun Park, Deng Yijie, Bo Yeon Kim, Seung Su Kyung, Yong Soo Choi, Hyung Joo Yoon, Mingshun Li, Byung Rae Jin PII: S1226-8615(14)00065-X DOI: doi: 10.1016/j.aspen.2014.05.005 Reference: ASPEN 535 To appear in: Journal of Asia-Pacific Entomology Received date: 9 April 2014 Revised date: 7 May 2014 Accepted date: 14 May 2014 Please cite this article as: Lee, Kwang Sik, Park, Hee Geun, Yijie, Deng, Kim, Bo Yeon, Kyung, Seung Su, Choi, Yong Soo, Yoon, Hyung Joo, Li, Mingshun, Jin, Byung Rae, Molecular characterization of a Niemann-Pick disease type C2 protein from the honeybee Apis cerana, Journal of Asia-Pacific Entomology (2014), doi: 10.1016/j.aspen.2014.05.005 This is a PDF file of an unedited manuscript that has been accepted for publication.. As a service to our customers we are providing this early version of the manuscript.. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Article Title: Molecular characterization of a venom acid phosphatase from the Asiatic honeybee Apis cerana Article Snippet: Article history: Received 13 June 2016 Revised 20 July 2016 Accepted 24 July 2016 Available online 26 July 2016 Bee venom contains a variety of toxic components, including enzymes, peptides, and biogenic amines.. An acid phosphatase Acph-1-like protein has been identified from Asiatic honeybee (Apis cerana) venom.. However, no molecular information is currently available for acid phosphatases from A. cerana venom. Article Title: Apolipophorin III from honeybees (Apis cerana) exhibits antibacterial activity. Article Snippet: Article history: Received 20 August 2014 Received in revised form 28 November 2014 Accepted 29 November 2014 Available online 5 December 2014 Article Title: Dual function of a bee (Apis cerana) inhibitor cysteine knot peptide that acts as an antifungal peptide and insecticidal venom toxin. Article Snippet: Inhibitor cysteine knot (ICK) peptides exhibit ion channel blocking, insecticidal, and antimicrobial activities, but currently, no functional roles for bee-derived ICK peptides have been identified.. In this study, a bee (Apis cerana) ICK peptide (AcICK) that acts as an antifungal peptide and as an insecticidal venom toxin was identified.. AcICK contains an ICK fold that is expressed in the epidermis, fat body, or venom gland and is present as a 6.6-kDa peptide in bee venom. Article Title: A bumblebee (Bombus ignitus) venom serine protease inhibitor that acts as a microbial serine protease inhibitor. Article Snippet: Contents lists available at ScienceDirect Comparative Biochemistry and Physiology, Part B j ourna l homepage: www.e lsev ie r .com/ locate /cbpb A bumblebee (Bombus ignitus) venom serine protease inhibitor that acts as a microbial serine protease inhibitor Hu Wan a,1, Bo Yeon Kim a,1, Kwang Sik Lee a, Hyung Joo Yoon b, Kyung Yong Lee b, Byung Rae Jin a,⁎ a College of Natural Resources and Life Science, Dong-A University, Busan 604-714, Republic of Korea b Department of Agricultural Biology, National Academy of Agricultural Science, Suwon, Republic of Korea ⁎ Corresponding author.. Tel./fax: +82 51 200 7594.. E-mail address: brjin@dau.ac.kr (B.R. Article Title: Secapin, a bee venom peptide, exhibits anti-fibrinolytic, anti-elastolytic, and anti-microbial activities. Article Snippet: Bee venom contains a variety of peptide constituents that have various biological, toxicological, and pharmacological actions.. However, the biological actions of secapin, a venom peptide in bee venom, remain largely unknown.. Here, we provide the evidence that Asiatic honeybee (Apis cerana) secapin (AcSecapin-1) exhibits anti-fibrinolytic, anti-elastolytic, and anti-microbial activities. Article Title: Peroxiredoxin 5 from common cutworm (Spodoptera litura) acts as a potent antioxidant enzyme. Article Snippet: Article history: Received 23 April 2014 Received in revised form 24 June 2014 Accepted 27 June 2014 Available online 4 July 2014 |