Recombinant Human RECK His-tag Protein, CF Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinant Human RECK His-tag (Catalog # 10236-RE) is immobilized
at 2 µg/mL (100 µL/well), Biotinylated Recombinant Human TEM5/GPR124 His-tag binds
with an ED50 of 0.7-4.9 µg/mL. |
Source |
Chinese Hamster Ovary cell line, CHO-derived human RECK protein Gly27-Pro941, with a C-terminal 6-His tag |
Accession # |
|
N-terminal Sequence |
Gly27 |
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 |
103 - 122 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 Tris and NaCl. |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 250 μg/mL in water. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human RECK His-tag Protein, CF
Background
Reversion-inducing cysteine-rich protein with Kazal motifs (RECK), also known as Suppressor of tumorigenicity 15 protein (ST15), is a 971 amino acid highly conserved protein that serves as an important mediator of tissue remodeling (1). The multi-domain protein includes hydrophobic regions at the N- and C-termini that correspond to a signal domain and GPI anchoring site, respectively (2). Internally, there are three serine protease inhibitor-like (SPI) domains and two regions with EGF-like repeats (2). The N-terminal region also contains a cysteine-rich domain essential for MMP (3) and Wnt7 binding (4, 5). RECK is normally expressed in all human and mammalian cells (2, 6) while undetectable or downregulated in malignant and cancer cells (1, 2). There is a strong correlation with expression of RECK in several cancers including colorectal, breast, and pancreatic making it a prognostic marker of interest (1, 3, 7-9). Polymorphisms in RECK leads to increased cancer susceptibility (10). RECK's ability to bind several proteins confers complex functionality. RECK is known to bind and inhibit MMPs (1, 2, 11), interact with ADAMTS10 (12), modulate Notch signaling (13), promote p53 signaling (14) and act as a selective Wnt7 receptor through binding of Gpr124 (4). RECK acts as a tumor suppression gene by inhibiting angiogenesis, invasion, and metastasis through its role in the regulation and signaling within the extracellular matrix (1, 3, 6). Through its interaction with Wnt7, RECK promotes angiogenesis and regulates the blood-brain barrier in CNS by mediating canonical Wnt/beta-catenin signaling (4).
- Alexius-Lindgren, M. et al. (2014) Anticancer Res. 34:3867.
- Takahashi, C. et al. (1998) Proc. Natl. Acad. Sci. U.S.A. 95:13221.
- Clark, J.C.M. et al. (2007) Cancer Mestast. Rev. 26:675.
- Vallon, M. et al. (2018) Cell Reports. 25:339.
- Cho, C. et al. (2019) Elife. 8:e47300.
- Oh, J. et al. (2001) Cell. 107:789.
- Takeuchi, T. et al. (2004) Clin. Cancer Res. 10:5572.
- Zhang, G. et al. (2012) Cancer Sci. 103:1084.
- Masui, T. et al. (2003) Clin. Cancer Res. 9:1779.
- Chung, T.T. et al. (2012) PLoS ONE. 7:e33517.
- Miki, T. et al. (2007) J. Biol. Chem. 282:12341.
- Matsuzaki, T. et al. (2018) Biol. Open 7:bio033985.
- Muraguchi, T. et al. (2007) Nat. Neurosci. 10:838.
- Lui, Y. et al. (2018) J. Cell. Biochem. 119:3058.
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