Recombinant Human Mer His-tag Avi-tag Protein, CF Summary
Accession # Q12866.2
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 with Trehalose.|
|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.
Measured by its binding ability in a functional ELISA. When Biotinylated Recombinant Human Mer His-tag Avi-tag Protein (Catalog # AVI10515) is captured on EvenCoat Streptavidin Coated Plates (CP004) at 2.00 µg/mL (100 µL/well), Recombinant Human Gas6 Protein (885-GSB) binds with an ED50 of 80.0-800 ng/mL.
2 μg/lane of Recombinant Human Mer His-tag Avi-tag Protein (Catalog # AVI10515) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 108-121 kDa.
Tyrosine-protein Kinase Mer, also known as c-Mer and MerTK, is a member of the receptor tyrosine kinase subfamily TAM (Tyro3, Axl, and Mer). Mature human Mer consists of 485 aa extracellular domain, 21 aa transmembrane domain, and 473 aa cytoplasmic domain. Within the extracellular domain, human Mer shares 77.2% and 76.6% homology with mouse and rat Mer, respectively. Similar to Axl and Tyro3, the extracelluar domain of Mer contains two Ig-like motifs and two fibronectin type III motifs. Mer is not expressed in normal B- and T-cells but expressed in neoplastic B- and T-cell lines (1-2). It is also show higher expression in immunosuppressive M2‑like macrophages (3). Mer is known to bind Gas6, Protein S, Tubby, Tubby-like protein 1 (Tulp1), and Galectin-3 (4-7). Upon binding ligands via the Ig-like motif, Mer is dimerized to trans-autophosphorylate the kinase domain to induce downstream signaling. It has been shown that Mer signaling in macrophages induces M2 polarization, which promote tumor growth, metastasis and evasion of anti-tumor immunity in tumor microenviroment (8). Inhibition of Mer, especially on leukocytes and macrophages, is an effective anti-cancer therapy (9). Our Avi-tag Biotinylated Mer His-tag features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.
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- Kim, S.Y. et al. (2016) Sci. Rep. 6:29673.
- Cummings, C.T. et al. (2013) Clin. Cancer Res. 19:5275.
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