Recombinant Mouse LRIG1 Protein, CF Summary
Product Specifications
Ala37-Thr794, 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.
3688-LR
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
| Reconstitution | Reconstitute at 100 μg/mL in sterile PBS. |
| Shipping | The product is shipped with polar packs. 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: LRIG1
LRIG1 is a 145 kDa leucine-rich repeat (LRR) and Ig-like domain-containing single-pass transmembrane glycoprotein. It has been shown to suppress tumor growth, regulate tissue homeostasis, and maintain stem cell quiescence (1-5). Mouse LRIG1 is synthesized with a 34 amino acid (aa) signal sequence, a 761 aa extracellular domain (ECD), a 21 aa transmembrane sequence, and a 275 aa cytoplasmic region. The LRIG1 ECD contains three C-type Ig-like domains as well as fifteen LRRs that are flanked by cysteine-rich regions (6, 7). The ECD of mouse LRIG1 shares 90% and 95% aa identity with the ECD of human and rat LRIG1, respectively. LRIG1 shares 45-50% aa identity with its mammalian paralogs, LRIG2 and LRIG3. LIRG1 is expressed widely throughout mouse and human tissues, including the liver, brain, stomach, small intestine, skeletal muscle, cornea, and hair follicle (3, 6, 8). LRIG1 functions as a tumor suppressor by controlling cell proliferation through the negative regulation of the EGF family of receptor tyrosine kinases. Specifically, the ECD of LRIG1 binds to EGF R, ErbB2, ErbB3, and ErbB4, inducing receptor ubiquitination and degradation (9, 10). LRIG1 expression, which is often dysregulated in human cancers, is a prognostic indicator of cancer development and relapse; decreased LRIG1 is associated with an increase in recurrence and mortality for a variety of cancers including breast, uterine, head-and-neck, glioma, prostate, and squamous cell (2, 11-13). Tissue homeostasis and stem cell dormancy is also thought to be modulated by the actions of LRIG1 on cell proliferation (14).
- Chang, L. et al. (2013) J. Exp. Clin. Cancer Res. 32:101.
- Lindquist, D. et al. (2014) Acta Oncol. 53:1135.
- Nakamura, T. et al. (2014) J. Clin. Invest. 124:385.
- Wang, Y. et al. (2013) Br. J. Cancer 108:1765.
- Jensen, K.B. and F.M. Watt (2006) Proc. Natl. Acad. Sci. U S A 103:11958.
- Guo, D. et al. (2004) Genomics 84:157.
- Jensen, K.B. et al. (2009) Cell Stem Cell 4:427.
- Suzuki, H. et al. (1996) J. Biol. Chem. 271:18981.
- Gur, G. et al. (2004) EMBO J. 23:3270.
- Laederich, M.B. et al. (2004) J. Biol. Chem. 279:47050.
- Johansson, M. et al. (2013) Neuro. Oncol. 15:1200.
- Thomasson, M. et al. (2003) Br. J. Cancer 89:1285.
- Thompson, P.A. et al. (2014) Cancer Res. 74:2928.
- Ordonez-Moran, P. and J. Huelsken (2012) EMBO J. 31:2064.
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