Recombinant Human CD44v6 Fc Chimera Avi-tag Protein, CF Summary
Product Specifications
Analysis
Product Datasheets
AVI11175
Carrier Free
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.
AVI11175
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
| Reconstitution | Reconstitute at 500 μg/mL in PBS. |
| Stability & Storage: | Store the unopened product at -20 to -70 °C. Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Do not use past expiration date. |
Scientific Data
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Measured by its binding ability in a functional ELISA. Biotinylated Recombinant Human CD44v6 Fc Chimera Avi-tag Protein (Catalog # AVI11175) binds to Recombinant Human LSECtin/CLEC4G Protein (2947-CL) with an ED50 of 40.0-400 ng/mL.
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2 μg/lane of Biotinylated Recombinant Human CD44v6 Fc Chimera Avi-tag Protein (Catalog # AVI11175) was resolved with SDS-PAGE under reducing (R) condition and visualized by Coomassie® Blue staining, showing bands at 105-120 kDa.
Background: CD44
CD44 is a ubiquitously expressed protein that is the major receptor for hyaluronan and exerts control over cell growth and migration (1-3). Human CD44 has a 20 amino acid (aa) signal sequence, an extracellular domain (ECD) with a 100 aa hyaluronan-binding disulfide-stabilized link region and a 325-530 aa stem region, a 21 aa transmembrane domain, and a 72 aa cytoplasmic domain. CD44 transcripts undergo complex alternative splicing, and, within the stem, ten variably spliced exons (v1‑10 corresponding to exons 6-15; although human CD44 lacks v1/exon 6) produce multiple protein isoforms (1-4). The standard or hematopoietic form, CD44H, does not include the variable segments (1-4). Cancer aggressiveness and T cell activation have been correlated with expression of specific isoforms (1, 4, 5). Human CD44v6 contains exon 11 (v6) and is involved in many biological processes including cell growth, apoptosis, and metastasis (6-7). With variable N- and O‑glycosylation and splicing within the stalk, CD44 can range from 80 to 200 kDa (1). Within the N-terminal invariant portion of the ECD (aa 21-222), human CD44 shares 76%, 76%, 86%, 83% and 79% identity with corresponding mouse, rat, equine, canine and bovine CD44, respectively. The many reported functions of CD44 fall within three categories (1). First, CD44 binds hyaluronan and other ligands within the extracellular matrix and can function as a "platform" for growth factors and metalloproteinases. Second, CD44 can function as a co-receptor that modifies activity of receptors including MET and the ERBB family of tyrosine kinases. Third, the CD44 intracellular domain links the plasma membrane to the actin cytoskeleton via the ERM proteins, ezrin, radixin and moesin. CD44 can be synthesized in a soluble form (8) or may be cleaved at multiple sites by either membrane-type matrix metalloproteinases, or ADAM proteases to produce soluble ectodomains (9-10). The cellular portion may then undergo gamma secretase-dependent intramembrane cleavage to form an A beta-like transmembrane portion and a cytoplasmic signaling portion that affects gene expression (11‑12). These cleavage events are thought to promote metastasis by enhancing tumor cell motility and growth (1, 8). CD44v6 plays an important role in colorectal cancer progression involving in cell colonization, invasion, and metastasis and is considered a functional cancer biomarker (7). Our Avi-tag Biotinylated human CD44v6 Fc Chimera 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.
- Ponta, H. et al. (2003) Nat. Rev. Mol. Cell Biol. 4:33.
- Screaton, G.R. et al. (1992) Proc. Natl. Acad. Sci. USA 89:12160.
- Screaton, G.R. et al. (1993) J. Biol. Chem. 268:12235.
- Lynch, K.W. (2004) Nat. Rev. Immunol. 4:931.
- Todaro, M. et al. (2014) Cell stem cell 14:342.
- Vizoso, F.J. et al. (2004) J. Cancer Res. Clin. Oncol. 130:679.
- Ma, L. et al. (2019) Cell Death Dis. 10:30.
- Yu, Q. and B.P. Toole (1996) J. Biol. Chem. 271:20603.
- Nagano, O. and H. Saya (2004) Cancer Sci. 95:930.
- Nakamura, H. et al. (2004) Cancer Res. 64:876.
- Murakami, D. et al. (2003) Oncogene 22:1511.
- Lammich, S. et al. (2002) J. Biol. Chem. 277:44754.
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