>90%, 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
Binding Activity
Theoretical MW
48.6 kDa (monomer). 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
72-86 kDa, reducing conditions
Publications
Read Publications using 3660-CD in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human CD44 Fc Chimera Protein, CF
CD44 antigen
CD44 molecule (Indian blood group)
CD44
CD44R
CDw44
cell surface glycoprotein CD44
chondroitin sulfate proteoglycan 8
CSPG8
ECMR-III
epican
Extracellular matrix receptor III
GP90 lymphocyte homing/adhesion receptor
HCAM
HCELL
hematopoietic cell E- and L-selectin ligand
Heparan sulfate proteoglycan
Hermes antigen
homing function and Indian blood group system
HUTCH-I
Hyaluronate receptor
IN
LHR
MC56
MDU2
MDU2CD44 antigen (homing function and Indian blood group system)
MDU3
MDU3CDW44
MIC4
MIC4MGC10468
MUTCH-I
Pgp1
PGP-1
PGP-I
Phagocytic glycoprotein 1
Phagocytic glycoprotein I
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. Within the stem, ten variably spliced exons (v1-10, exons 6-15) produce multiple protein isoforms (1-3). The standard or hematopoietic form, CD44H, does not include the variable segments (1-3). Cancer aggressiveness and T cell activation have been correlated with expression of specific isoforms (1, 3). 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 21-220), 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 (4) or may be cleaved at multiple sites by either membrane-type matrix metalloproteinases, or ADAM proteases to produce soluble ectodomains (5, 6). 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 (7, 8). These cleavage events are thought to promote metastasis by enhancing tumor cell motility and growth (1, 5).
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.
Lynch, K.W. (2004) Nat. Rev. Immunol. 4:931.
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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