Recombinant Human MUC-1 Fc Chimera Protein, CF Summary
|Human MUC-1 |
Accession # P15941-1
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 400 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
When Recombinant Human MUC-1 Fc Chimera (Catalog # 10332-MU) is immobilized at 1 µg/mL (100 µL/well), Recombinant Human Siglec-9 Fc Chimera (Catalog # 1139-SL) binds with an ED50of 0.2-1.4 µg/mL.
2 μg/lane of Recombinant Human MUC-1 Fc Chimera (Catalog # 10332-MU) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 157-192 kDa and 310-380 kDa, respectively.
MUC-1 (Mucin-1) is a type 1 transmembrane glycoprotein that is normally expressed on the apical surface of most epithelial cells (1-2). It is known to be overexpressed by various human carcinomas and is shed into circulation (2). The extracellular domain is made up of tandem repeats (TRs) of 20 aa each, with each TR containing five potential O-glycosylation sites (3). The number of TRs vary between 25-100, depending on the allele (3). Within the mature region including 16 TRs (residues 24-380), human MUC-1 shares 30% aa sequence identity with mouse and rat MUC-1. It has been reported that high expression level of MUC-1 generally correlates with increased mortality rates (4). In addition, MUC-1 is aberrantly underglycosylated on cancer cells with short and sialylated O-linked glycans in contrast to the long, branched chain seen in normal epithelial cells (4-7). It has been demonstrated that MUC-1 can interact with E-selectin and ICAM-1 to mediate firm adhesion of circulating tumor cells and subsequent extravasation in the metastatic adhesion cascade (4). Furthermore, MUC-1 can modulate the tumor immunological microenvironment through engagement of Siglec-9 by inducing the recruitment of beta-catenin to the cytoplasmic tail of MUC-1, increasing the expression of PD-L1 by macrophages, and activating the MEK-ERK pathway (5,6). MUC-1 can also interact with Galectin-3 to promote EGFR activation thus regulating EGFR-associated tumorigenesis and cancer progression (7).
- Rughetti, A. et al. (2005) J. Immunol. 174:7764.
- Engelstaedter, V. et al. (2012) BMC Cancer 12:600.
- Taylor-Papadimitriou, J. et al. (1999) Biochim. Biophys. Acta 1455:301.
- Geng, Y. et al. (2012) Front Oncol. 2:76.
- Tanida, S. et al. (2013) J Biol Chem. 288:31842.
- Beatson, R. et al. (2016) Nat Immunol. 17:1273.
- Piyush, T. et al. (2017) Cell Death Differ. 24:1937.
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