Recombinant Mouse PTK7/CCK4 Fc Chimera Protein, CF Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. Recombinant Mouse PTK7/CCK4 Fc Chimera (Catalog # 10333-TK) binds
Biotinylated Recombinant Mouse Wnt-3a
(Catalog #
BT1324). The ED 50 for this
effect is 8-48 μg/mL. |
Source |
Mouse myeloma cell line, NS0-derived mouse PTK7/CCK4 protein Mouse PTK7/CCK4 (Ala23-Thr696) Accession # Q8BKG3 | IEGRMDP | Mouse IgG2A (Glu98-Lys330) | N-terminus | | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
Ala23 |
Structure / Form |
Disulfide-linked homodimer |
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 |
102 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 |
110-130 kDa, under reducing conditions |
Packaging, Storage & Formulations
Storage |
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 with Trehalose. |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
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 Mouse PTK7/CCK4 Fc Chimera Protein, CF
Background
Protein
tyrosine kinase 7 (PTK7), also known as colon carcinoma kinase 4 (CCK4), is a
member of the receptor tyrosine kinase superfamily (1, 2). PTK7 is a type I
transmembrane receptor with a large extracellular domain (ECD) containing 7
Ig-like C2 type loops, a transmembrane domain, and a cytoplasmic tyrosine
kinase homology domain. However, due to the lack of the DFG triplet motif
required for catalytic activity in the kinase domain, PTK7 is considered a
pseudokinase (1, 3). The mature ECD of
mouse PTK7 shares 92% amino acid sequence identity with human PTK7. PTK7 is
expressed in a wide array of tissue types ranging from lung and liver to kidney
and placenta and has been linked to a broad range of functions (5). While
originally identified as being over-expressed in colon carcinomas, PTK7 has
been shown to play a role in embryogenesis, epithelial tissue organization,
angiogenesis, cell motility, and survival (1, 6, 7). PTK7 has been shown to be
an important regulator of the Wnt signaling pathways, both canonical and
non-canonical, and is linked to the regulation of the planar cell polarity
pathway (3, 6). Proteolysis of full-length PTK7 by MMPs (matrix metalloproteinases),
ADAMs (a disintegrin domain and metalloproteinases), and gamma-secretases results
in a soluble N-terminal fragment and several C-terminal, membrane-associated or
intracellular proteolytic fragments (3, 6). The soluble form is a co-receptor
for the Semaphorin/Plexin and VEGF signaling pathways (8). Deregulation of PTK7
signaling has now been observed in numerous cancers including colon, gastric,
lung, and acute myeloid leukemia (1, 3). Recent studies have shown that PTK7
expression promoted increased migration and resistance to apoptosis in leukemic
cells and acute myeloid leukemia (AML) blasts, while knock-down of PTK7 induced
apoptosis in colorectal carcinoma cells (2, 7). Further, other studies have
suggested that the ratio of full-length vs. cleaved protein, not just
expression, contributes to PTK7's metastatic effects in cancer (6).
- Shin, W. et al. (2008) Biochem. Bioph. Res. Co. 371:793.
- Meng, L. et al. (2010) PLoS ONE 5:e14018.
- Golubkov, V. et al. (2010) J. Biol. Chem. 285:35740.
- Berger, H. et al. (2017) Front. Cell Dev. Biol. 5:31.
- Park, S. et al. (1996) J. Biochem. 119:235.
- Golubkov, V. et al. (2014) J. Biol. Chem. 289:24238.
- Prebet, T. et al. (2010) Blood. 116:2315.
- Peradziryi, H. et al. (2012) Arch. Biochem. Biophys. 524:71.
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