MUC1 Antibody (SM3) - BSA Free Summary
Hydrogen fluoride deglycosylated milk mucin.
Cell Membrane and Cytoplasmic
Reacts very little with normal tissue. Found to react with breast, colon and ovarian carcinomas and adinocarcinoma. SM3 recognises the under-glycosylated form of MUC1 and is therefore tumour specific.
Protein G purified
Test in a species/application not listed above to receive a full credit towards a future purchase.
- Flow Cytometry
- Immunocytochemistry/Immunofluorescence 10 ug/ml
- Immunohistochemistry 1:10-1:500
- Immunohistochemistry-Frozen 1:10-1:500
- Immunohistochemistry-Paraffin 1:10-1:500
IHC-Fr and IHC-P: Use at an assay dependent dilution. Use in ELISA, and FLOW reported in various pieces of scientific literature.
|Read Publications using
NB120-22711 in the following applications:
Human. Mouse reactivity reported in scientific literature (PMID: 1372533) Not record of testing in other species.
Packaging, Storage & Formulations
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.
0.02% Sodium Azide
Protein G purified
Alternate Names for MUC1 Antibody (SM3) - BSA Free
- Breast carcinoma-associated antigen DF3
- Carcinoma-associated mucin
- CD227 antigen
- DF3 antigen
- H23 antigen
- mucin 1, cell surface associated
- mucin 1, transmembrane
- Peanut-reactive urinary mucin
- Polymorphic epithelial mucin
- tumor associated epithelial mucin
- Tumor-associated epithelial membrane antigen
- Tumor-associated mucin
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).
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.
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FAQs for MUC1 Antibody (NB120-22711). (Showing 1 - 1 of 1 FAQs).
I would like to perform a sandwich assay for the determination of MUC1 protein. May you suggest me some antibodies that can be used together? In particular, if possible, I should need antibodies product in mouse or rabbit.
- Unfortunately we are not aware of a pair of antibodies that have been used in sandwich ELISA in particular. If you are interested in trying two you may find our Innovators Reward Program to be helpful.
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