MUC1 Antibody (SM3) - BSA Free

Mucin 1 (MUC1), also known as episialin, EMA (epithelial membrane antigen), PEM (polymorphic epithelial mucin), and CA-15-3 antigen, is a membrane-bound type I transmembrane glycoprotein (1,2). MUC1 is typically expressed in the luminal or glandular epithelial cells of the gastrointestinal tract, breast, lungs, and more, and is often overexpressed in epithelial cancers, but also serves a protective role against infection and helps regulate inflammatory response (2,3). Human MUC1 is 1255 amino acids (aa) in length with a theoretical molecular weight of 122 kDa; however, depending on the amount of glycosylation can weigh between 250 - 500 kDa (2,4). Structurally, MUC1 consists of a N-terminal domain which contains a signal peptide, a variable number tandem repeat region (VNTR), and a SEA domain, as well a C-terminal domain which has the extracellular domain (ECD), transmembrane domain (TMD), and cytoplasmic tail (CT) (2,3). The VNTR is comprised of between 25 - 125 repeats of a 20 aa conserved sequence (3). MUC1 is heavily O-glycosylated in the VNTR and has moderate N-glycosylation sites following the VNTR and in the ECD (2). Glycosylation contributes to MUC1's functional properties (2). The MUC1 gene contains seven exons, giving rise to several MUC1 isoforms as a result of alternative splicing (2).

Overexpression of mucins, including MUC1, is a feature of many epithelial cancers (1,3,5,6). The presence of truncated glycan structures called tumor-associated carbohydrate antigens (TACAs) on MUC1 play a role in cancer progression and a loss of apical-basal polarity (5). Carbohydrate-binding partners called lectins are the primary binding partners of TACAs that give rise to the pro-tumor microenvironment and metastasis (5). Given this unique feature, TACAs are a potential target for cancer immunotherapies (5). There are a number of vaccines, drugs, and antibodies targeting MUC1 for treatment of a variety of cancers including breast, lung, and prostate (6). In addition to a role in cancer progression, MUC1, and specifically the CT portion, has been shown to have a positive, anti-inflammatory role in a variety of lung and airway infections (7).

References

1. Khodabakhsh, F., Merikhian, P., Eisavand, M. R., & Farahmand, L. (2021). Crosstalk between MUC1 and VEGF in angiogenesis and metastasis: a review highlighting roles of the MUC1 with an emphasis on metastatic and angiogenic signaling. Cancer cell international. https://doi.org/10.1186/s12935-021-01899-8

2. Nath, S., & Mukherjee, P. (2014). MUC1: a multifaceted oncoprotein with a key role in cancer progression. Trends in molecular medicine. https://doi.org/10.1016/j.molmed.2014.02.007

3. Dhar, P., & McAuley, J. (2019). The Role of the Cell Surface Mucin MUC1 as a Barrier to Infection and Regulator of Inflammation. Frontiers in cellular and infection microbiology. https://doi.org/10.3389/fcimb.2019.00117

4. Uniprot (P15941)

5. Beckwith, D. M., & Cudic, M. (2020). Tumor-associated O-glycans of MUC1: Carriers of the glyco-code and targets for cancer vaccine design. Seminars in immunology. https://doi.org/10.1016/j.smim.2020.101389

6. Almasmoum H. (2021). The Roles of Transmembrane Mucins Located on Chromosome 7q22.1 in Colorectal Cancer. Cancer management and research. https://doi.org/10.2147/CMAR.S299089

7. Ballester, B., Milara, J., & Cortijo, J. (2021). The role of mucin 1 in respiratory diseases. European respiratory review : an official journal of the European Respiratory Society. https://doi.org/10.1183/16000617.0149-2020

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

We have publications tested in 2 confirmed species: Human, Mouse.

We have publications tested in 4 applications: ELISA, FLOW, IF/IHC, IHC.

Showing Publications 1 - 10 of 13. Show All 13 Publications. Collapse Publications.

Publications using NB120-22711	Applications	Species
Lucarelli G, Netti GS, Rutigliano M et al. MUC1 Expression Affects the Immunoflogosis in Renal Cell Carcinoma Microenvironment through Complement System Activation and Immune Infiltrate Modulation International journal of molecular sciences 2023-03-02 [PMID: 36902242] (IHC, Human)	IHC	Human
Nalawade SA, Shafer P, Bajgain P Et al. Selectively targeting myeloid-derived suppressor cells through TRAIL receptor 2 to enhance the efficacy of CAR T cell therapy for treatment of breast cancer J Immunother Cancer 2021-11-24 [PMID: 34815355] Details: Citation using the Alexa Fluor 700 version of this antibody.
Sorensen AL, Reis CA, Tarp MA et al. Chemoenzymatically synthesized multimeric Tn/STn MUC1 glycopeptides elicit cancer-specific anti-MUC1 antibody responses and override tolerance. Glycobiology. 2006-02-16 [PMID: 16207894] (ELISA, Human)	ELISA	Human
Dalziel M, Whitehouse C, McFarlane I et al. The relative activities of the C2GnT1 and ST3Gal-I glycosyltransferases determine O-glycan structure and expression of a tumor-associated epitope on MUC1. J Biol Chem 2001-04-06 [PMID: 11118434] (FLOW, Human)	FLOW	Human
Mommers EC, Leonhart AM, von Mensdorff-Pouilly S et al. Aberrant expression of MUC1 mucin in ductal hyperplasia and ductal carcinoma In situ of the breast. Int J Cancer. 1999-10-22 [PMID: 10502721] (IF/IHC, Human)	IF/IHC	Human
Henderikx P, Kandiloqiannaki M, Petrarca C et a.l. Human single-chain Fv antibodies to MUC1 core peptide selected from phage display libraries recognize unique epitopes and predominantly bind adenocarcinoma. Cancer Res. 1998-10-01 [PMID: 9766660] (FLOW, Human)	FLOW	Human
Karsten U, Diotel c, Klich g et al. Enhanced binding of antibodies to the DTR motif of MUC1 tandem repeat peptide is mediated by site-specific glycosylation. Cancer Res. 1998-06-15 [PMID: 9635576] (ELISA, Human)	ELISA	Human
Bohm CM, Mulder MC, Zennadi R et al. Carbohydrate recognition on MUC1-expressing targets enhances cytotoxicity of a T cell subpopulation. Scnd J Immunol. 1997-07-01 [PMID: 9246205] (FLOW, Human)	FLOW	Human
Hanisch FG, Stadie TR, Deutzmann F et al. MUC1 glycoforms in breast cancer--cell line T47D as a model for carcinoma-associated alterations of 0-glycosylation. Eur J Biochem. 1996-02-15 [PMID: 8617281] (ELISA, Human)	ELISA	Human
Ho Jj, Siddiki B, Kim YS et al. Association of sialyl-Lewis(a) and sialyl-Lewis(x) with MUC-1 apomucin ina pancreatic cancer cell line. Cancer Res. 1995-08-15 [PMID: 7627976] (ELISA, Human)	ELISA	Human
Brockhausen I, Yang JM Burchell J et al. Mechanisms underlying aberrant glycosylation of MUC1 mucin in breast cancer cells Eur J Biochem. 1995-10-15 [PMID: 7588808] (FLOW, Human)	FLOW	Human
Kotera Y, Fontenot JD, Pecher G et al. Humoral immunity against a tandem repeat epitope of human mucin MUC-1 in sera from breast, pancreatic, and colon cancer patients. Cancer Res. 1994-06-01 [PMID: 7514493] (IF/IHC, Human)	IF/IHC	Human
Peat N, Gendler SJ, Lalani N et al. Tissue-specific expression of a human polymorphic epithelial mucin (MUC1) in transgenic mice. Cancer Res. 1992-04-01 [PMID: 1372533] (IF/IHC, Mouse, Human)	IF/IHC	Mouse, Human
Show All 13 Publications. Collapse Publications.

Array NB120-22711

• MUC1 Antibodies
• MUC1 Antibody Pair
• MUC1 ELISA Kits
• MUC1 Lysates
• MUC1 Proteins
• MUC1 Proteins and Enzymes