Batch dependent - please inquire should you have specific requirements.
Preservative
None
Storage
Refrigerate at +2-8°C for 12 months or store at -20°C for at least 3 years
Antigen Description
CA 15-3, for Carcinoma Antigen 15-3, is a tumor marker for many types of cancer, most notably breast cancer. It is derived from MUC1. CA 15-3 and associated CA 27-29 are different epitopes on the same protein antigen product of the breast cancer-associated MUC1 gene. Elevated CA15-3, in conjunction with alkaline phosphatase (ALP), was found to be associated with an increased chance of early recurrence in breast cancer. Both CA 15-3 and CA 27-29 may be elevated in patients with benign ovarian cysts, benign breast disease, and benign liver disease. Elevations may also be seen in cirrhosis, sarcoidosis and lupus.
Keywords
CA 15-3; MUC1; breast cancer
Citations
Publication ()
Have you cited DAGF-212 in a publication? Let us know and earn a reward for your research.
Background
CA 15-3 was initially identified as a tumor antigen recognized by two monoclonal antibodies (DF3 and 115D8). The antibody DF3 interacts with mucin 1 core protein (MUC1 or CD227) while 115D8 attaches to specific glycan chains present on MUC1. The highly glycosylated transmembrane protein appears on epithelial cells' mucosal surfaces within the lungs, breasts, stomach, gallbladder, lymph nodes, colon, rectum, and pancreas. During breast cancer transformation CA 15-3 blood levels rise because increased protease and sialidase activity breaks down cytoskeletal structures and cell membrane components are released. Studies report elevated serum CA 15-3 levels in 30%-50% of breast cancer patients and 80% of metastatic cases, with concentration changes closely correlating to therapeutic outcomes. Clinically, CA 15-3 is currently considered the preferred clinical indicator for early diagnosis, disease monitoring, postoperative recurrence assessment, and treatment efficacy evaluation in breast cancer patients.
MUC1 functions as a Type I transmembrane protein that forms a heterodimer and possesses a glycosylated extracellular domain measuring 200 to 500 nm through 20-amino-acid unit tandem repeats. The primary difference between healthy and cancerous cells is reflected in the length and structure of O-glycan chains on this heavily glycosylated protein which contains many serine and threonine residues that support O-glycan attachment. Healthy epithelial MUC1 carries linear polylactosamine chains that may be fucosylated, while breast cancer cells express shortened O-glycans called dense Thomsen–Friedenreich (T/TF) antigens or sialylated TF-antigens, with GalNAc-Gal typically forming the terminal two monomers of these chains.
Figure 1. Structure of MUC1 in normal tissues and diseased tissues (Source: Chen W, et al. 2021)
Current methods for measuring serum CA 15-3 levels include ELISA as the most common technique, though it requires prolonged incubation and multiple washing steps with relatively low sensitivity. To address these limitations, researchers developed a magnetic bead-labeled electrochemical biosensor showing improved sensitivity and reliability. Recent advancements focus on detecting MUC1 abnormal glycosylation, a hallmark of cancer progression. In pancreatic cancer, CA 15-3 exhibits altered glycan structures characterized by truncated O-glycans (e.g., dense T/TF antigens). Novel antibody-lectin sandwich assays targeting CA 15-3 glycosylation patterns demonstrate superior performance over ELISA in distinguishing breast cancer stages (I, IIA, IIB, III), potentially enhancing clinical staging accuracy.
Alternative Names
Human milk derived MUC1 antigen Human milk derived CA15-3 antigen Human milk derived carbohydrate antigen15-3 antigen
References
1. Li X, et al. Serum CA153 as biomarker for cancer and noncancer diseases. Prog Mol Biol Transl Sci. 2019;162:265-276.
2. Chen W, et al. MUC1: Structure, Function, and Clinic Application in Epithelial Cancers. Int J Mol Sci. 2021 Jun 18;22(12):6567.
My Review for Human milk derived MUC1 (CA15-3) antigen
Creative Diagnostics products are for RESEARCH USE ONLY, please make sure your review is research based.
Required fields are marked with *
Terms and conditions:
We will select high-quality review customers and offer a $30 coupon for your next purchase.
All product reviews must be submitted in the English language.
Creative Diagnostics will not share any personal information of applicants, and all information will be treated with strict confidentiality and will not be sold or disclosed to a third party.
References
Multigene methylation in serum of sporadic Chinese female breast cancer patients as a prognostic biomarker
Objective: DNA methylation is a common molecular alteration in human neoplasia and can be detected easily in the bloodstream of patients. Here, we investigated whether DNA methylation in sera is of prognostic significance in breast cancer patients. Methods: Methylation status of BRCA1, p16 and 14-3-3 sigma was examined by methylation-specific PCR assay in the sera of sporadic breast cancer patients and healthy serum controls. Results: The panel gene methylation frequencies were 29% of sporadic breast cancers for p16, 32% for BRCA1 and 82% for 14-3-3 sigma; all were significantly associated with grades and estrogen receptor status. Only p16 methylation was associated with histological type. p16 and BRCA1 methylation were associated with progesterone receptor status, while 14-3-3 sigma was significantly associated with lymph node metastases. Seventy percent of patients with p16 methylation showed elevated serum CEA levels; of the breast cancer patients with BRCA1 methylation, 75.8% showed elevated serum CEA levels and 69.7% showed elevated serum CA15.3 levels. When analyzing all investigated patients, multivariate analysis showed methylated BRCA1 and/or p16 serum DNA to be independently associated with poor outcome, with a relative risk of death of 6.0. Conclusions: Epigenetic markers in sera, especially BRCA1/p16, may be more promising targets for the diagnosis of sporadic breast cancer than previous prognostic markers. Copyright (C) 2008 S. Karger AG, Basel.
A self-enhanced electrochemiluminescence immunosensor based on L-Lys-Ru(dcbpy)(3)(2+) functionalized porous six arrises column nanorods for detection of CA15-3
In this work, a new manganese ions doped zinc oxide porous six arrises column nanorods was rapidly synthesized with L-Lys as the precipitating and capping agent (L-Lys/Mn-ZnONRs). The as-synthesized L-Lys/Mn-ZnONRs exhibited large specific surface area and high ferromagnetism, which could serve as excellent nanocarrier. Meanwhile, due to the outstanding conductivity and biocompatibility, platinum nanoparticles (PtNPs) were decorated on the surface of L-Lys/Mn-ZnONRs by Pt-N bond to form PtNPs/L-Lys/Mn-ZnONRs complexes. After that the obtained complexes were used to immobilize abundant tris (4,4'-dicarboxylicacid-2,2'-bipyridyl) ruthenium(II) dichloride (Ru(dcbpy)(3)(2+)) and detection antibody for construction of sandwiched electrochemiluminescence (ECL) immunosensor. Coincidentally, L-Lys not only acted as the precipitating and capping agent to control shape and size of L-Lys/Mn-ZnONRs, but also acted as a co-reactant of Ru(dcbpy)(3)(2+) to efficiently amplify the ECL signal. Importantly, L-Lys had free amino group which could link with Ru(dcbpy) via amide bond to form a self-enhanced ECL complex. Through this way, the electron transfer path between luminophore and co-reactant reagent was shortened and the energy loss of luminophore was lessened. Consequently, the prepared ECL immunosensor showed excellent performance for the detection of carbohydrate antigen 15-3 in the range from 0.05 U/mL to 120 U/mL with a detection limit of 0.014 U/mL (S/N=3) and a correlation coefficient of R=0.9977. Moreover, the prepared ECL immunosensor had good stability, excellent selectivity and satisfactory reproducibility. (C) 2015 Elsevier B.V. All rights reserved.
COA
Publication 
Figure 1. Structure of MUC1 in normal tissues and diseased tissues
Loading ......
