Reactivity | MuSpecies Glossary |
Applications | Binding Activity |
Format | Carrier-Free |
Details of Functionality | Measured by its ability to bind ErbB4 in a functional ELISA. Laederich, M.B. et al. (2004) J. Biol. Chem. 279:47050. Immobilized Recombinant Mouse LRIG1 at 2.5 µg/mL (100 µL/well) can bind recombinant human ErbB4 with a linear range of 8-500 ng/mL. |
Source | Mouse myeloma cell line, NS0-derived mouse LRIG1 protein Ala37-Thr794, with a C-terminal 6-His tag |
Accession # | |
N-terminal Sequence | Ala37 |
Protein/Peptide Type | Recombinant Proteins |
Gene | Lrig1 |
Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 84.3 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 | 100-105 kDa, reducing conditions |
Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Buffer | Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Reconstitution Instructions | Reconstitute at 100 μg/mL in sterile PBS. |
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).
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