Recombinant Human CD44v6 Fc Chimera Avi-tag Protein, CF Summary
N-terminal Sequence |
Gln21, inferred from enzymatic pyroglutamate treatment revealing Ile22 |
Structure / Form |
Disulfide-linked Homodimer Biotinylated via Avitag |
Protein/Peptide Type |
Recombinant Proteins |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
60 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 |
105-120 kDa, under reducing conditions |
Packaging, Storage & Formulations
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. |
Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
Reconstitution Instructions |
Reconstitute at 500 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human CD44v6 Fc Chimera Avi-tag Protein, CF
Background
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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