Recombinant Human LRRC24 His-tag Protein, CF Summary
Cys23-Ser365, with a C-terminal 6-His tag
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 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.
2 μg/lane of Recombinant Human LRRC24 His-tag (Catalog # 10512-LR) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 45-55 kDa.
Leucine-rich repeat-containing protein 24 (LRRC24) is type I transmembrane protein found within the large LRR superfamily. The LRR family is known to have diverse functions, including roles in innate immunity and nervous system development (1). The extracellular domain (ECD) of LRRC24 contains several LRR repeats along with an Ig-like C2-type region. The mature ECD of human LRRC24 shares 86% and 80% amino acid sequence identity with mouse and rat LRRC24, respectively. LRRC24 has been shown to interact with Robo2, which is important for axon guidance and cell migration (2). LRRC24 has been suggested to be a novel negative regulator of the ErbB family and suppress ErbB-driven tumor cell proliferation and motility (3).
- Ng, A.C.Y. et al. (2011) PNAS 108:4631.
- Söllner, C. and Wright, G.J. (2009) Genome Biol. 10:R99.
- Andrews, A. et al. (2017) DOI:10.21767/2254-6081-C1-003.
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