Recombinant Human MUC1 GST (N-Term) Protein Summary
Description |
A recombinant protein with a N-terminal GST tag corresponding to the amino acid sequence 315-420 of Human MUC-1 Source: Wheat Germ (in vitro) Amino Acid Sequence: NSSLEDPSTDYYQELQRDISEMFLQIYKQGGFLGLSNIKFRPGSVVVQLTLAFREGTINVHDMETQFNQYKTEAASRYNLTISDVSVSDVPFPFSAQSGAGVPGWG |
Preparation Method |
in vitro wheat germ expression system |
Details of Functionality |
This protein was produced in an in vitro wheat germ expression system that should preserve correct conformational folding that is necessary for biological function. While it is possible that this protein could display some level of activity, the functionality of this protein has not been explicitly measured or validated. |
Source |
Wheat germ |
Protein/Peptide Type |
Recombinant Protein |
Gene |
MUC1 |
Purity |
>80% by SDS-PAGE and Coomassie blue staining |
Applications/Dilutions
Dilutions |
- ELISA
- Immunoaffinity Purification
- Protein Array
- Western Blot
|
Theoretical MW |
37.4 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
Publications |
|
Packaging, Storage & Formulations
Storage |
Store at -80C. Avoid freeze-thaw cycles. |
Buffer |
50 mM Tris-HCI, 10 mM reduced Glutathione, pH 8.0 in the elution buffer. |
Preservative |
No Preservative |
Purity |
>80% by SDS-PAGE and Coomassie blue staining |
Notes
This product is produced by and distributed for Abnova, a company based in Taiwan.
Alternate Names for Recombinant Human MUC1 GST (N-Term) Protein
Background
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
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are
guaranteed for 3 months from date of receipt.
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Publications for MUC1 Partial Recombinant Protein (H00004582-Q01)(5)
Showing Publications 1 -
5 of 5.
Publications using H00004582-Q01 |
Applications |
Species |
Florea A, Taleat Z, Cristea C et al. Label free MUC1 aptasensors based on electrodeposition of gold nanoparticles on screen printed electrodes. Electrochemistry Communications. 2013-08-01 |
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Liu H, Zhang L, Xu Y et al. Sandwich immunoassay coupled with isothermal exponential amplification reaction: An ultrasensitive approach for determination of tumor marker MUC1. Talanta. 2019-06-04 [PMID: 31357289] |
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McDaniel JR, Pero SC, Voss WN et al. Identification of tumor-reactive B cells and systemic IgG in breast cancer based on clonal frequency in the sentinel lymph node. Cancer Immunol Immunother 2018-02-09 [PMID: 29427082] |
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Lu H, Ladd J, Feng Z et al. Evaluation of Known Oncoantibodies, HER2, p53, and Cyclin B1, in Prediagnostic Breast Cancer Sera. Cancer Prev Res (Phila). 2012-07-03 [PMID: 22715141] |
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Desmetz C, Bascoul-Mollevi C, Rochaix P et al. Identification of a New Panel of Serum Autoantibodies Associated with the Presence of In situ Carcinoma of the Breast in Younger Women. Clin Cancer Res 2009-07-15 [PMID: 19584157] |
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Reviews for MUC1 Partial Recombinant Protein (H00004582-Q01) (0)
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Product General Protocols
Find general support by application which include: protocols, troubleshooting, illustrated assays, videos and webinars.
Video Protocols
FAQs for MUC1 Partial Recombinant Protein (H00004582-Q01). (Showing 1 - 3 of 3 FAQs).
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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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I am interested in purchasing MUC1 protein from you and it would be a great help if you could answer a few of my questions. 1) How much of the glycoprotein is glycosylated? 2) Is it soluble in water? 3) It says on the website that the product is not active, what exactly do you mean by that?
- This protein is a recombinant protein. It does not undergo glycosylation. It may not be folded in the same way as the native protein therefore it may be not act in the same way. This should only be used for WB and as a positive control in ELISA. It is soluble in water.
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Could you recommend us a protocol for ELISA test in a sandwich format for MUC1 protein catalog # H00004582-Q01 using catalog # NB100-65647 as primary antibody and catalog # NBP1-61561 as secondary with a third labeled antibody? Regarding the request below with that pair of antibodies and that recombinant protein: could you help us with another primary monoclonal antibody to replace the NB100-65647 antibody with it, so we could use it in a sandwich assay with the protein H00004582-Q01 and the NBP1-61561. Thank you. Also do you know if this recombinant protein is tumoral MUC1 or normal MUC1, because they have different structures.
- Unfortunately, the antibody and protein combination you have chosen will not work. As is stated in our datasheet for NB100-65647 The dominant epitope recognized by this antibody is the 12-mer GVTSAPDTRPAP. Unfortunately, this epitope is not present in the partial recombinant protein H00004582-Q01. While NB100-65647 and NBP1-61561 are suitable pairs to use for ELISA, H00004582-Q01 is not a suitable standard for use with this pair, and unfortunately it does not look like we carry a suitable standard for you. I apologize for the inconvenience. Please see our ELISA protocol. H00004582-Q01 is produced by a Taiwanese company called Abnova and we distribute it for them. It is produced in their cell-free wheat germ expression system. I would recommend using one of Abnova's matched antibody pairs for use in ELISA if you are going to use H00004582-Q01 as a standard. I would recommend using the H00004582-AP41 antibody pair.