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Avicenna Journal of Medical Biochemistry، جلد ۳، شماره ۲، صفحات ۰-۰
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| عنوان فارسی |
Production and Characterization of Monoclonal Antibodies Against the Dimerization Domain of Human HER۲ |
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| چکیده فارسی مقاله |
Results Isotype of 1F1 clone was determined to be IgG1, which reacted with native protein in the western blot experiment and stained 20% of the membrane of neoplastic cells overexpressing HER2 with 3+ grade. However, 3L5 clone showed a low reaction (10%) with native HER2 in immunohistochemistry. Conclusions The results of both western blotting and Immunohistochemistry showed that native HER2 can be detected with 1F1 monoclonal antibody. Objectives In this study we aimed to produce murine Monoclonal Antibodies (MAbs) with the ability of specific recognition of the HER2 dimerization arm. Materials and Methods Primarily, BALB/c mice were immunized with a 30-aminoacid peptide as a part of the human HER2 subdomain II. Splenocytes from hyperimmunized mice were fused with myeloma cells (SP2/0), selected in hypoxanthine-aminopterin-thymidine (HAT) medium, and screened by indirect Enzyme-Linked Immunosorbent Assay (ELISA). Secreted MAbs were characterized according to isotypes, reactions with the native HER2 in SKBR3 cells by western blotting, and in tissue sections from HER2 positive breast cancer specimens by Immunohistochemistry (IHC). Background Human Epidermal Growth factor Receptor 2 (HER2), also known as ErbB2 is a 185 kDa protein belonging to the Human Epidermal Receptor (HER) family of tyrosine kinase receptors overexpressed in 20% - 30% of patients with breast cancer. Similar to other members of the HER family, HER2 glycoprotein comprises of multiple domains including an extracellular ligand-binding domain, a single transmembrane domain and a cytoplasmic domain with tyrosine kinase activity. The extracellular domain of HER2 with 632 amino acids is composed of four subdomains (I - IV); subdomains I and III form a ligand binding site, and cysteine-rich subdomains II and IV play an important role in dimerization of the receptor. |
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| کلیدواژه‌های فارسی مقاله |
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| عنوان انگلیسی |
Production and Characterization of Monoclonal Antibodies Against the Dimerization Domain of Human HER2 |
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| چکیده انگلیسی مقاله |
Results Isotype of 1F1 clone was determined to be IgG1, which reacted with native protein in the western blot experiment and stained 20% of the membrane of neoplastic cells overexpressing HER2 with 3+ grade. However, 3L5 clone showed a low reaction (10%) with native HER2 in immunohistochemistry. Conclusions The results of both western blotting and Immunohistochemistry showed that native HER2 can be detected with 1F1 monoclonal antibody. Objectives In this study we aimed to produce murine Monoclonal Antibodies (MAbs) with the ability of specific recognition of the HER2 dimerization arm. Materials and Methods Primarily, BALB/c mice were immunized with a 30-aminoacid peptide as a part of the human HER2 subdomain II. Splenocytes from hyperimmunized mice were fused with myeloma cells (SP2/0), selected in hypoxanthine-aminopterin-thymidine (HAT) medium, and screened by indirect Enzyme-Linked Immunosorbent Assay (ELISA). Secreted MAbs were characterized according to isotypes, reactions with the native HER2 in SKBR3 cells by western blotting, and in tissue sections from HER2 positive breast cancer specimens by Immunohistochemistry (IHC). Background Human Epidermal Growth factor Receptor 2 (HER2), also known as ErbB2 is a 185 kDa protein belonging to the Human Epidermal Receptor (HER) family of tyrosine kinase receptors overexpressed in 20% - 30% of patients with breast cancer. Similar to other members of the HER family, HER2 glycoprotein comprises of multiple domains including an extracellular ligand-binding domain, a single transmembrane domain and a cytoplasmic domain with tyrosine kinase activity. The extracellular domain of HER2 with 632 amino acids is composed of four subdomains (I - IV); subdomains I and III form a ligand binding site, and cysteine-rich subdomains II and IV play an important role in dimerization of the receptor. |
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| کلیدواژه‌های انگلیسی مقاله |
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| نویسندگان مقاله |
محمد ندری | mohammad nadri
department of biochemistry, school of medicine, mashhad university of medical sciences, mashhad, ir iran
سازمان اصلی تایید شده: دانشگاه علوم پزشکی مشهد (Mashhad university of medical sciences)
محمد سوختانلو | mohammad soukhtanloo
department of biochemistry, school of medicine, mashhad university of medical sciences, mashhad, ir iran; cancer molecular pathology research center, ghaem hospital, school of medicine, mashhad university of medical sciences, mashhad, ir iran
سازمان اصلی تایید شده: دانشگاه علوم پزشکی مشهد (Mashhad university of medical sciences)
امیرحسین جعفریان | amir hosein jafarian
cancer molecular pathology research center, ghaem hospital, school of medicine, mashhad university of medical sciences, mashhad, ir iran
سازمان اصلی تایید شده: دانشگاه علوم پزشکی مشهد (Mashhad university of medical sciences)
محبوبه علمداری | mahboobeh alamdari
department of biochemistry, school of medicine, mashhad university of medical sciences, mashhad, ir iran
سازمان اصلی تایید شده: دانشگاه علوم پزشکی مشهد (Mashhad university of medical sciences)
محسن سی سختی | mohsen sisakhti
department of biochemistry, school of medicine, mashhad university of medical sciences, mashhad, ir iran
سازمان اصلی تایید شده: دانشگاه علوم پزشکی مشهد (Mashhad university of medical sciences)
طیبه کیانوش | tayebeh kianoush
department of biochemistry, school of medicine, mashhad university of medical sciences, mashhad, ir iran
سازمان اصلی تایید شده: دانشگاه علوم پزشکی مشهد (Mashhad university of medical sciences)
فرناز زاهدی اول | farnaz zahedi avval
department of biochemistry, school of medicine, mashhad university of medical sciences, mashhad, ir iran; biochemistry amp;amp; nutrition research center, mashhad university of medical sciences, mashhad, ir iran; department of biochemistry, school of medicine, mashhad university of medical sciences, p. o. box 917794-8564, mashhad, ir iran. tel 98-5138002365, fax 98-5138828574
سازمان اصلی تایید شده: دانشگاه علوم پزشکی مشهد (Mashhad university of medical sciences)
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| نشانی اینترنتی |
http://www.avicennajb.com/index.php?page=article&article_id=29918 |
| فایل مقاله |
فایلی برای مقاله ذخیره نشده است |
| کد مقاله (doi) |
10.17795/ajmb-29918 |
| زبان مقاله منتشر شده |
fa |
| موضوعات مقاله منتشر شده |
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| نوع مقاله منتشر شده |
research-article |
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