Recombinant Human CRELD2 Protein, CF Summary
Ala21-Leu353, with a C-terminal 6-His tag
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.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 250 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
Cysteine-rich with EGF-like domain protein 2 (CRELD2) is an approximately 60 kDa glycoprotein that contains two EGF‑like domains and two FU domains (1). Mature human CRELD2 shares approximately 78% aa sequence identity with mouse and rat CRELD2. Alternative splicing of human CRELD2 generates additional isoforms with substitutions, deletions, and/or insertions in the C-terminal half of the molecule (2). The various isoforms are widely expressed in fetal and adult tissues (1‑3). CRELD2 localizes to the endoplasmic reticulum and Golgi and can also be secreted (3‑5). It is up‑regulated during the cellular stress‑induced unfolded protein response (UPR), cartilage and bone pathologies (MED and MCDS), and arsenic‑induced liver toxicity (4, 6‑8). CRELD2 interacts intracellularly with the alpha 4 and beta 2 subunits of the nicotinic acetylcholine receptor and inhibits cell surface expression of the receptor (3, 9). CRELD2 expression is up‑regulated in prostate cancer by dihydroxytestosterone and is down‑regulated following anti-androgen treatment (10).
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- Maslen, C.L. et al. (2006) Gene 382:111.
- Ortiz, J.A. et al. (2005) J. Neurochem. 95:1585.
- Oh-hashi, K. et al. (2009) Biochem. Biophys. Res. Commun. 387:504.
- Oh-hashi, K. et al. (2011) FEBS Lett. 585:2481.
- Cameron, T.L. et al. (2011) PLoS ONE 6:e24600.
- Nundlall, S. et al. (2010) Cell Stress Chaperones 15:835.
- Nohara, K. et al. (2012) Toxicol. Sci. epub.
- Hosur, V. et al. (2009) J. Neurochem. 111:848.
- Jariwala, U. et al. (2007) Mol. Cancer 6:39.
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