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MUC2: ELISA Kits

MUC2, also called mucin 2, is a member of the mucin protein family which are heavily glycosylated, high molecular weight proteins that are produced by goblet cells in epithelial tissues including the intestinal and respiratory tract (1). Mucins can form gels and function in lubrication of mucosal surfaces which serve as a protective barrier of the epithelial lining and an innate host defense (1). Mucins are divided into two groups based on whether they are membrane-bound or secreted, where MUC2 belongs to the secretory group (1,2). Secreted mucins have a distinctive composition characterized by a large central exon "mucin domain" containing O-glycosylated tandem repeat regions rich in proline, threonine, and serine residues, non-repetitive domains, and cysteine-rich domains (1,2). The mucin domain is flanked by 5' and 3' D domains, a B-like domain, a C-like domain, and a Ck-domain (1,2). MUC2 was the first secretory mucin identified in humans (3,4). Full-length MUC2 protein is synthesized as 5179 amino acids (aa) in length with a theoretical molecular weight of ~540 kDa (5).

Changes or perturbations to MUC2 expression has been associated with a number of disease pathologies (1-4, 6). Specifically, altered MUC2 composition has been indicated in colorectal cancer, inflammatory bowel diseases (IBD) including ulcerative colitis and Chron's disease, and chronic obstructive pulmonary disease (COPD) (1-4, 6). In general, decreased or reduced MUC2 expression is associated with colorectal cancer disease progression and development of IBD (1-4, 6). Additionally, studies have found that upon intestinal infection due to parasites or bacteria MUC2 expression is increased, as is overall mucus secretion (3, 6).

References

1. Pothuraju, R., Krishn, S. R., Gautam, S. K., Pai, P., Ganguly, K., Chaudhary, S., Rachagani, S., Kaur, S., & Batra, S. K. (2020). Mechanistic and Functional Shades of Mucins and Associated Glycans in Colon Cancer. Cancers. https://doi.org/10.3390/cancers12030649

2. Ballester, B., Milara, J., & Cortijo, J. (2019). Mucins as a New Frontier in Pulmonary Fibrosis. Journal of Clinical Medicine. https://doi.org/10.3390/jcm8091447

3. Liu, Y., Yu, X., Zhao, J., Zhang, H., Zhai, Q., & Chen, W. (2020). The role of MUC2 mucin in intestinal homeostasis and the impact of dietary components on MUC2 expression. International Journal of Biological Macromolecules. https://doi.org/10.1016/j.ijbiomac.2020.07.191

4. Allen, A., Hutton, D. A., & Pearson, J. P. (1998). The MUC2 gene product: a human intestinal mucin. The International Journal of Biochemistry & Cell Biology. https://doi.org/10.1016/s1357-2725(98)00028-4

5. Uniprot (Q02817)

6. Kim, Y. S., & Ho, S. B. (2010). Intestinal goblet cells and mucins in health and disease: recent insights and progress. Current Gastroenterology Reports. https://doi.org/10.1007/s11894-010-0131-2
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2 results for "MUC2 ELISA Kits" in Products

MUC2: ELISA Kits

MUC2, also called mucin 2, is a member of the mucin protein family which are heavily glycosylated, high molecular weight proteins that are produced by goblet cells in epithelial tissues including the intestinal and respiratory tract (1). Mucins can form gels and function in lubrication of mucosal surfaces which serve as a protective barrier of the epithelial lining and an innate host defense (1). Mucins are divided into two groups based on whether they are membrane-bound or secreted, where MUC2 belongs to the secretory group (1,2). Secreted mucins have a distinctive composition characterized by a large central exon "mucin domain" containing O-glycosylated tandem repeat regions rich in proline, threonine, and serine residues, non-repetitive domains, and cysteine-rich domains (1,2). The mucin domain is flanked by 5' and 3' D domains, a B-like domain, a C-like domain, and a Ck-domain (1,2). MUC2 was the first secretory mucin identified in humans (3,4). Full-length MUC2 protein is synthesized as 5179 amino acids (aa) in length with a theoretical molecular weight of ~540 kDa (5).

Changes or perturbations to MUC2 expression has been associated with a number of disease pathologies (1-4, 6). Specifically, altered MUC2 composition has been indicated in colorectal cancer, inflammatory bowel diseases (IBD) including ulcerative colitis and Chron's disease, and chronic obstructive pulmonary disease (COPD) (1-4, 6). In general, decreased or reduced MUC2 expression is associated with colorectal cancer disease progression and development of IBD (1-4, 6). Additionally, studies have found that upon intestinal infection due to parasites or bacteria MUC2 expression is increased, as is overall mucus secretion (3, 6).

References

1. Pothuraju, R., Krishn, S. R., Gautam, S. K., Pai, P., Ganguly, K., Chaudhary, S., Rachagani, S., Kaur, S., & Batra, S. K. (2020). Mechanistic and Functional Shades of Mucins and Associated Glycans in Colon Cancer. Cancers. https://doi.org/10.3390/cancers12030649

2. Ballester, B., Milara, J., & Cortijo, J. (2019). Mucins as a New Frontier in Pulmonary Fibrosis. Journal of Clinical Medicine. https://doi.org/10.3390/jcm8091447

3. Liu, Y., Yu, X., Zhao, J., Zhang, H., Zhai, Q., & Chen, W. (2020). The role of MUC2 mucin in intestinal homeostasis and the impact of dietary components on MUC2 expression. International Journal of Biological Macromolecules. https://doi.org/10.1016/j.ijbiomac.2020.07.191

4. Allen, A., Hutton, D. A., & Pearson, J. P. (1998). The MUC2 gene product: a human intestinal mucin. The International Journal of Biochemistry & Cell Biology. https://doi.org/10.1016/s1357-2725(98)00028-4

5. Uniprot (Q02817)

6. Kim, Y. S., & Ho, S. B. (2010). Intestinal goblet cells and mucins in health and disease: recent insights and progress. Current Gastroenterology Reports. https://doi.org/10.1007/s11894-010-0131-2
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