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biological source
mouse
Quality Level
100
500
conjugate
unconjugated
antibody form
culture supernatant
antibody product type
primary antibodies
clone
MRQ-18, monoclonal
description
For In Vitro Diagnostic Use in Select Regions (See Chart)
form
buffered aqueous solution
species reactivity
human
packaging
vial of 0.1 mL concentrate (291M-14)
vial of 0.5 mL concentrate (291M-15)
bottle of 1.0 mL predilute (291M-17)
vial of 1.0 mL concentrate (291M-16)
bottle of 7.0 mL predilute (291M-18)
manufacturer/tradename
Cell Marque™
technique(s)
immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:50-1:200
isotype
IgG1κ
control
colon
shipped in
wet ice
storage temp.
2-8°C
visualization
cytoplasmic
Gene Information
human ... MUC2(4583)
Related Categories
General description
Mucins are a diverse group of complex, highly glycosylated extracellular proteins. Mucin 2 (MUC2) protects the gastric and intestinal epithelium from chemical and mechanical injury. Anti-MUC2 reactivity is normally seen in goblet cells of the small intestine and colon and is associated with mucinous carcinomas, including those of the gastrointestinal tract and ovary. MUC2 immunohistochemistry is useful for identifying colonic, gastric, and esophageal carcinomas.
Mucins are high molecular weight glycoproteins which constitute the major component of the mucus layer that protects the gastric epithelium from chemical and mechanical aggressions. In humans, at least 14 mucin genes have been identified that code for the mucin proteins. They are designated as MUC1, MUC2, MUC3, MUC4, MUC5AC, MUC5B , MUC6 , MUC7, MUC8, MUC9, MUC11, MUC12, MUC13 and MUC16. Mucins share a common feature of a tandem-repeat domain rich in serine and threonine residues. These amino acid residues are potential O-glycosylation sites for attachment of the O-glycan chains that constitute up to 80% of the molecular weight of the final mucin glycoprotein.
The heterogeneous pattern of mucin expression, including the expression of the intestinal mucin MUC2, may provide new insights into the differentiation pathways of gastric carcinoma. The pattern of mucin expression may also be used as a clue to bring new insights into the biological behaviour of distinct clinicopathological entities related to the localisation of gastric carcinoma, namely proximal and distal gastric carcinomas. Pinto-de-Sousa et al. have shown in a comprehensive study of gastric carcinomas evaluated for expression of several mucins (MUC1, MUC2, MUC5AC and MUC6) that: (1) mucin expression is associated with tumour type (MUC5AC with diffuse and infiltrative carcinomas and MUC2 with mucinous carcinomas) but not with the clinico-biological behaviour of the tumours; and (2) mucin expression is associated with tumour location (MUC5AC with antrum carcinomas and MUC2 with cardia carcinomas), indirectly reflecting differences in tumour differentiation according to tumour location.
The following generalities apply to the patterns of Mucin expression:
MUC1 expression: apical surfaces of most epithelial cells in breast, GI, respiratory, and GU tracts.
MUC2 expression: specifically expressed in goblet cells of the small intestine & colon.
Colonic CAs – 65%, Gastric CAs – 42%, Esophageal CAs – 17%
Rare outside of GI tract – with exception of; mucinous ca of breast, clear cell-type CAs of the ovary.
The heterogeneous pattern of mucin expression, including the expression of the intestinal mucin MUC2, may provide new insights into the differentiation pathways of gastric carcinoma. The pattern of mucin expression may also be used as a clue to bring new insights into the biological behaviour of distinct clinicopathological entities related to the localisation of gastric carcinoma, namely proximal and distal gastric carcinomas. Pinto-de-Sousa et al. have shown in a comprehensive study of gastric carcinomas evaluated for expression of several mucins (MUC1, MUC2, MUC5AC and MUC6) that: (1) mucin expression is associated with tumour type (MUC5AC with diffuse and infiltrative carcinomas and MUC2 with mucinous carcinomas) but not with the clinico-biological behaviour of the tumours; and (2) mucin expression is associated with tumour location (MUC5AC with antrum carcinomas and MUC2 with cardia carcinomas), indirectly reflecting differences in tumour differentiation according to tumour location.
The following generalities apply to the patterns of Mucin expression:
MUC1 expression: apical surfaces of most epithelial cells in breast, GI, respiratory, and GU tracts.
MUC2 expression: specifically expressed in goblet cells of the small intestine & colon.
Colonic CAs – 65%, Gastric CAs – 42%, Esophageal CAs – 17%
Rare outside of GI tract – with exception of; mucinous ca of breast, clear cell-type CAs of the ovary.
Quality
 IVD |  IVD |  IVD |  RUO |
Linkage
MUC2 Positive Control Slides, Product No. 291S, are available for immunohistochemistry (formalin-fixed, paraffin-embedded sections).
Physical form
Solution in Tris Buffer, pH 7.3-7.7, with 1% BSA and <0.1% Sodium Azide
Preparation Note
Download the IFU specific to your product lot and formatNote: This requires a keycode which can be found on your packaging or product label.
Other Notes
For Technical Service please contact: 800-665-7284 or email: service@cellmarque.com
Legal Information
Cell Marque is a trademark of Merck KGaA, Darmstadt, Germany
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Emad A Rakha et al.
Modern pathology : an official journal of the United States and Canadian Academy of Pathology, Inc, 18(10), 1295-1304 (2005-06-25)
Mucins are a large family of glycoproteins expressed by many epithelial cells and their malignant counterparts. Much interest has been focused on expression of its members in breast cancer because of their potential role as prognostic indicators and their involvement
T Mizoshita et al.
Histology and histopathology, 22(3), 251-260 (2006-12-14)
We have previously demonstrated links between clinicopathological findings and phenotypes using several gastric and intestinal phenotypic markers in stomach and pancreatic cancers. However, the clinicopathological significance of the phenotype and Cdx2 expression has hitherto remained unclear in colorectal carcinogenesis. We
Seog-Yun Park et al.
Archives of pathology & laboratory medicine, 131(10), 1561-1567 (2007-10-10)
Although identification of the primary tumor in patients with metastatic adenocarcinoma has a profound clinical impact, diagnosing the organ of origin is frequently difficult. Because none of the individual immunohistochemical markers used for tissue identification are both site specific and
Fionnuala P O'Connell et al.
Archives of pathology & laboratory medicine, 129(3), 338-347 (2005-03-02)
Breast carcinoma often metastasizes to the gastrointestinal tract, especially the stomach, where it is frequently difficult to distinguish from a primary gastric carcinoma. To evaluate the utility of immunohistochemical stains in differentiating primary gastric carcinomas from metastatic breast carcinomas. Mucosal
P Chaves et al.
Diseases of the esophagus : official journal of the International Society for Diseases of the Esophagus, 18(6), 383-387 (2005-12-13)
Intestinal metaplasia is a prerequisite criterion for the diagnosis of Barrett's metaplasia and the sole columnar esophageal lining associated with malignancy. It is recognized by the presence of goblet cells, but columnar non-goblet elements, producing gastric or intestinal proteins, are
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