Recombinant Human Axl Fc Chimera Avi-tag Protein, CF Summary
Learn more about Avi-tag Biotinylated ProteinsProduct Specifications
| Human Axl (Ala26 - Trp450) Accession # P30530.4 | IEGRMD | Human IgG1 Fc (Pro100 - Lys330) | Avi-tag |
| N-terminus | C-terminus | ||
Analysis
Product Datasheets
AVI11011
Carrier Free
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.
AVI11011
| 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.
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Scientific Data
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When recombinant human Gas6 (885-GSB) is immobilized at 2.00 µg/mL (100 µL/well), Biotinylated Recombinant Human Axl Fc Chimera Avitag Protein (Catalog # AVI11011) binds with an ED50 of 2.50-15.0 ng/mL.
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2 μg/lane of Biotinylated Recombinant Human Axl Fc Chimera Avi-tag Protein (Catalog # AVI11011) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 89-115 kDa and 180-230 kDa, respectively.
Background: Axl
Axl, also known as Ufo and Ark, is a widely expressed 140 kDa glycoprotein in the TAM receptor tyrosine kinase family. TAM family receptors (Dtk/Tyro3, Axl, and Mer) are involved in regulation of the inflammatory response, cell survival and migration, and tumorigenesis (1). Mature human Axl consists of a 426 aa extracellular domain (ECD) that contains two Ig-like domains and two fibronectin type III domains, a 21 aa transmembrane segment, and a 422 aa cytoplasmic domain that includes the tyrosine kinase domain (2). Within the ECD, human Axl shares approximately 82% aa sequence identity with mouse and rat Axl. A short alternately spliced form of human Axl has a 9 aa deletion in the extracellular juxtamembrane region (2). Axl binds the vitamin K-dependent protein Gas6 which triggers tyrosine autophosphorylation of the Axl cytoplasmic domain (3). Activation of Axl induces a broad range of activities including platelet aggregation and thrombus formation (4), macrophage and dendritic cell phagocytosis of apoptotic cells (5), NK cell development from hematopoietic progenitor cells (6), and in vivo angiogenesis (7). Axl is highly expressed in solid cancers and promotes in vivo tumorigenesis and tumor cell invasiveness (7, 8). It contributes to vascular remodeling and inflammatory cell infiltration in response to hypertension and restricted blood flow (9). It also functions as a cellular entry receptor for Gas6-opsonized lentiviruses (10). A 70-80 kDa soluble portion of the Axl ECD can be shed by proteolytic cleavage, and this fragment retains the ability to bind Gas6 (11, 12). Our Avi-tag Biotinylated Axl Fc Chimera 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.
- Linger, R.M.A. et al. (2011) Adv. Cancer Res. 100:35.
- O’Bryan, J.P. et al. (1991) Mol. Cell. Biol. 11:5016.
- Nagata, K. et al. (1996) J. Biol. Chem. 22:30022.
- Cosemans, J.M.E.M. et al. (2010) J. Thromb. Haemost. 8:1797.
- Seitz, H.M. et al. (2007) J. Immunol. 178:5635.
- Park, I.-K. et al. (2009) Blood 113:2470.
- Holland, S. et al. (2005) Cancer Res. 65:9294.
- Rankin, E.B. et al. (2010) Cancer Res. 70:7570.
- Korshunov, V.A. et al. (2006) Circ. Res. 98:1446.
- Morizono, K. et al. (2011) Cell Host Microbe 9:286.
- O’Bryan, J.P. et al. (1995) J. Biol. Chem. 270:551.
- Ekman, C. et al. (2010) J. Thromb. Haemost. 8:838.
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