Recombinant Mouse CRELD2 Protein, CF Summary
Product Specifications
Ser23-Leu350, with a C-terminal 6-His tag
Analysis
Product Datasheets
Carrier Free
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.
3686-CR
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.
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Reconstitution Calculator
Background: CRELD2
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 mouse CRELD2 shares approximately 77% and 92% aa sequence identity with human and rat CRELD2, respectively. It is widely expressed in fetal and adult tissues (1, 2). CRELD2 localizes to the endoplasmic reticulum and Golgi and can also be secreted (2‑4). 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 (3, 5‑7). CRELD2 interacts intracellularly with the alpha 4 and beta 2 subunits of the nicotinic acetylcholine receptor and inhibits cell surface expression of the receptor (2, 8). CRELD2 expression is up‑regulated in prostate cancer by dihydroxytestosterone and is down‑regulated following anti‑androgen treatment (9).
- Rupp, P.A. et al. (2002) Gene 293:47.
- 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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