|Detection of Mouse LRIG1 by Western Blot. Western blot shows lysates of bEnd.3 mouse endothelioma cell line untreated (-), treated (+) or mock treated (m) with 30 pmol mouse LRIG1 or mouse ERK1 siRNA. PVDF membrane was probed with 2 µg/mL of Goat Anti-Mouse LRIG1 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3688) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF109). Specific bands were detected for LRIG1 at approximately 140 kDa and 70 kDa (as indicated, upper panel). For additional reference ERK1 was detected using Rabbit Anti-Human/Mouse/Rat ERK1 Antigen Affinity-purified Polyclonal Antibody (lower panel, Catalog # AF1575) This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
|Detection of LRIG1 in bEnd.3 Mouse Cell Line by Flow Cytometry. bEnd.3 mouse endothelioma cell line was stained with Goat Anti-Mouse LRIG1 Antigen Affinity‑purified Polyclonal Antibody (Catalog # AF3688, filled histogram) or control antibody (Catalog # AB-108-C, open histogram), followed by Phycoerythrin-conjugated Anti-Goat IgG Secondary Antibody (Catalog # F0107).|
|LRIG1 in bEnd.3 Mouse Cell Line. LRIG1 was detected in immersion fixed bEnd.3 mouse endothelioma cell line using Goat Anti-Mouse LRIG1 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3688) at 10 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Anti-Goat IgG Secondary Antibody (red, upper panel; Catalog # NL001) and counterstained with DAPI (blue, lower panel). Specific staining was localized to cytoplasm. View our protocol for Fluorescent ICC Staining of Cells on Coverslips.|
LRIG-1 (leucine-rich repeats and Ig-like domains-1; also LIG-1) is an approximately 130-145 kDa glycoprotein that belongs to the LRIG gene family. It is widely expressed, and appears on the surface of prostatic epithelium, endothelial cells, vascular and visceral smooth muscle, mammary epithelium, cardiac muscle, keratinocytes and neurons. LRIG-1 is believed to negatively regulate the ErbB family of receptors. In particular, and in a ligand-independent manner, LRIG-1 complexes with all four ErbBs, promoting their ubiquitination and decreasing their number. Alternatively, LRIG-1 is suggested to bind to the ErbBs, preventing their dimerization and signal transduction. Mature mouse LRIG-1 is a 1057 amino acid (aa) type I transmembrane protein (SwissProt #:P70193). It contains a large 762 amino acid (aa) extracellular domain (ECD) (aa 35-795) plus a 274 aa cytoplasmic region. The ECD contains 17 LRRs (aa’s 35-491) and three C2-type Ig-like domains (aa’s 497-781). These two domain types are each sufficient for EGFR binding. There one potential alternative splice form that a deletion of aa 875-923. The LRIG-1 ECD undergoes proteolysis, generating 90-105 and 60-70 kDa soluble fragments. Over aa 37-794, human LRIG-1 shares 97% and 90% aa sequence identity with rat and human LRIG-1, respectively.
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