Recombinant Human MUC-1 Fc Chimera Avi-tag Protein, CF Summary
Additional Information |
Biotinylated |
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Biotinylated
Recombinant Human MUC-1 Fc Chimera Avi-tag (Catalog # AVI10332) is immobilized
at 1 µg/mL (100 µL/well), Recombinant Human Siglec-9 Fc Chimera
(Catalog #
1139-SL)
binds with an ED 50 of 0.25-2 µg/mL. |
Source |
Human embryonic kidney cell, HEK293-derived human MUC-1 protein Human MUC-1 (Ser24-Ser380) Accession # P15941.3 | IEGRMD | Human IgG1 (Pro100-Lys330) | Avi-tag | N-terminus | | | C-terminus | |
|
Accession # |
|
Structure / Form |
Disulfide-linked homodimer, biotinylated via Avi-tag |
Protein/Peptide Type |
Recombinant Proteins |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
62 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. |
SDS-PAGE |
168-195 kDa, under reducing conditions |
Packaging, Storage & Formulations
Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.- 6 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after opening.
- 3 months, -20 to -70 °C under sterile conditions after opening.
|
Buffer |
Supplied as a 0.2 μm filtered solution in PBS with Trehalose. |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human MUC-1 Fc Chimera Avi-tag Protein, CF
Background
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 amino acid (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). Our Avi-tag Biotinylated human
MUC-1 features biotinylation at a single site contained within the Avi-tag, a
unique 15 amino acid peptide. Protein orientation will be uniform when bound to
streptavidin-coated surface due to the precise control of biotinylation and the
rest of the protein is unchanged so there is no interference in the protein's
bioactivity.
- 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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