Recombinant Human LRIG2 Fc Chimera Protein, CF Summary
Accession # O94898
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 500 μg/mL in 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.
When Recombinant Human LRIG2 Fc Chimera (Catalog # 1941-LR) is coated at 4 μg/mL, 100 μL/well, Recombinant Human PDGF R beta Fc Chimera (Catalog # 385-PR) binds with an ED50 of 1.5-9 μg/mL.
2 μg/lane of Recombinant Human LRIG2 Fc Chimera was resolved with SDS-PAGE underreducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Bluestaining, showing bands at 125-145 kDa and 250-290 kDa, respectively.
LRIG2 (leucine-rich repeats and Ig-like domains-2), also known as LIG-2, is a type I transmembrane glycoprotein member of the mammalian LRIG glycoprotein family (1). This family contains three members who share 45-50% amino acid (aa) identity (1). Human LRIG2 is synthesized as large precursor molecule, containing a signal sequence, a 767 amino acid (aa) extracellular domain (ECD), a single transmembrane sequence, and a 237 aa intracellular region. In the ECD, all LRIG family members contain at least fifteen LRRs, accompanied by two flanking cysteine-rich regions, and three C2-type Ig-like domains in their extracellular domains (ECD) (1-3). The ECD of human LRIG2 shares 94% and 93% aa sequence identity with mouse and rat, respectively. LRIG2 might have a function different from that of LRIG1, and possibly contribute to the etiology of oligodendroglioma (4). It was previously demonstrated that LRIG2 positively regulates epidermal growth factor receptor (EGFR) signaling, the most common aberrant receptor tyrosine kinase (RTK) signaling in glioblastoma multiforme (GBM), which promotes GBM growth. LRIG2 has the ability to physically interact with PDGFR beta, promoting the total expression and the activation of PDGF R beta, and enhancing its downstream signaling pathways of Akt and STAT3 and the effectors of key regulators of cell cycle progression, resulting in increased GBM cell proliferation (5).
- Guo, D. et al. (2004) Genomics 84:157.
- Holmlund, C. et al. (2004) Gene 332:35.
- Wang, B. et al. (2009) Cancer Biol Ther. 8:1018.
- Holmlund C et al. (2009) Neuropathology. 29:242.
- Qungen Xiao et al. (2018) Int J Oncol. 53:1069.
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