Rat Tyrosine-Protein Kinase Receptor UFO (AXL) Protein
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Description
AXL Receptor Tyrosine Kinase Protein is a recombinant Rat protein expressed in E. coli.
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Product specifications
| Category | Proteins and Peptides |
| Immunogen Target | Tyrosine-Protein Kinase Receptor UFO (AXL) |
| Host | E. coli |
| Origin | Rat |
| Conjugation | Unconjugated |
| Observed MW | Molecular Weight: Calculated MW: 23.5 kDa Concentration: Prior to lyophilization: 200 µg/ml Sequence Fragment: Lys21-His202 Tag: N-terminal His tag |
| Expression | Recombinant |
| Purity | > 90% |
| Size 1 | 10 µg |
| Size 2 | 50 µg |
| Size 3 | 100 µg |
| Size 4 | 200 µg |
| Size 5 | 500 µg |
| Form | Lyophilized To keep the original salt concentration, we recommend reconstituting to the original concentration prior to lyophilization (see Concentration) in ddH2O. If a lower concentration is required, dilute in PBS, pH 7.4. If a higher concentration is required, the product can be reconstituted directly in PBS, pH 7.4, though please note that this will change the overall salt concentration. The stock concentration should be between 0.1-1.0 mg/ml. Do not vortex. |
| Tested Applications | WB, SDS-PAGE |
| Buffer | Prior to lyophilization: PBS, pH 7.4, containing 0.01% Sarcosyl, 1 mM DTT, 5% Trehalose and Proclin-300. |
| Availability | Shipped within 5-7 working days. |
| Storage | Store at 2-8 °C for up to one month. Store at -80 °C for up to one year. Avoid repeated freeze/thaw cycles. |
| Dry Ice | No |
| Alias | ARK,UFO,AXL3,JTK11,Tyro7,AXL oncogene,Tyrosine-protein kinase receptor UFO |
| Background | Protein AXL |
| Status | RUO |
| Note | This product is for research use only. Not for human consumption, cosmetic, therapeutic or diagnostic use. |
Descripción
AXL receptor tyrosine kinase (AXL) is a member of the TAM (Tyro3, AXL, and MERTK) receptor tyrosine kinase family. This family of receptors is characterized by their roles in cell survival, proliferation, migration, and immune regulation. AXL was first identified as a transforming gene in chronic myeloid leukemia, and since then, it has been implicated in a variety of physiological and pathological processes, including cancer, fibrosis, and immune response modulation. AXL and its ligands are widely expressed in various tissues, including the cardiovascular, immune, and nervous systems. The primary ligand for AXL is growth arrest-specific 6 (Gas6), a vitamin K-dependent protein that mediates the receptor's activation. Binding of Gas6 to AXL triggers a cascade of downstream signaling events that influence cellular behaviors and fate decisions.
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anti- AXL antibody
Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding growth factor GAS6 and which is thus regulating many physiological processes including cell survival, cell proliferation, migration and differentiation. Ligand binding at the cell surface induces dimerization and autophosphorylation of AXL. Following activation by ligand, ALX binds and induces tyrosine phosphorylation of PI3-kinase subunits PIK3R1, PIK3R2 and PIK3R3; but also GRB2, PLCG1, LCK and PTPN11. Other downstream substrate candidates for AXL are CBL, NCK2, SOCS1 and TNS2. Recruitment of GRB2 and phosphatidylinositol 3 kinase regulatory subunits by AXL leads to the downstream activation of the AKT kinase. GAS6/AXL signaling plays a role in various processes such as endothelial cell survival during acidification by preventing apoptosis, optimal cytokine signaling during human natural killer cell development, hepatic regeneration, gonadotropin-releasing hormone neuron survival and migration, platelet activation, or regulation of thrombotic responses. Plays also an important role in inhibition of Toll-like receptors(TLRs)-mediated innate immune response. (Microbial infection) Acts as a receptor for lassa virus and lymphocytic choriomeningitis virus, possibly through GAS6 binding to phosphatidyl-serine at the surface of virion envelope(PubMed:22156524, PubMed:22673088, PubMed:25277499, PubMed:21501828). Acts as a receptor for ebolavirus, possibly through GAS6 binding to phosphatidyl-serine at the surface of virion envelope(PubMed:17005688).
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