Recombinant human GST-EML4-ALK protein (Active)
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Recombinant human GST-EML4-ALK protein (Active) is a Human Fragment protein, in the 1 to 534 aa range, expressed in Baculovirus infected Sf9 cells, with >70%, suitable for SDS-PAGE, FuncS.
View Alternative Names
CD246, ALK tyrosine kinase receptor, Anaplastic lymphoma kinase, ALK, C2orf2, EMAPL4, EML4, Echinoderm microtubule-associated protein-like 4, EMAP-4, Restrictedly overexpressed proliferation-associated protein, Ropp 120
- FuncS
Supplier Data
Functional Studies - Recombinant human GST-EML4-ALK protein (Active) (AB268523)
The specific activity of ab268523 was 4.2 nmol/min/mg in a peptide kinase assay using IGF1Rtide (KKKSPGEYVNIEFG) as substrate.
- SDS-PAGE
Project
SDS-PAGE - Recombinant human GST-EML4-ALK protein (Active) (AB268523)
SDS-PAGE analysis of ab268523.
Reactivity data
Product details
Sequence info
Properties and storage information
Form
Purification technique
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
The EML4-ALK fusion protein functions as an oncoprotein promoting uncontrolled cell proliferation and survival. It is not necessarily part of a complex but acts within signaling networks due to its kinase activity. By phosphorylating downstream substrates the EML4-ALK fusion disrupts normal cellular signaling enabling cancerous characteristics in affected cells. Its aberrant activation of signaling pathways can lead to sustained oncogenic signaling bypassing normal growth factor receptor regulation.
Pathways
ALK EML4 fusion interacts within key pathways like the PI3K/AKT and MAPK signaling cascades. These pathways are critical for cell growth survival and metabolism and the presence of EML4-ALK fusion causes constitutive activation promoting oncogenesis. The protein often impacts other signaling proteins such as mTOR and ERK which are downstream effectors within these pathways leading to enhanced cell proliferation and resistance to apoptosis.
General info
Function
Neuronal receptor tyrosine kinase that is essentially and transiently expressed in specific regions of the central and peripheral nervous systems and plays an important role in the genesis and differentiation of the nervous system (PubMed : 11121404, PubMed : 11387242, PubMed : 16317043, PubMed : 17274988, PubMed : 30061385, PubMed : 34646012, PubMed : 34819673). Also acts as a key thinness protein involved in the resistance to weight gain : in hypothalamic neurons, controls energy expenditure acting as a negative regulator of white adipose tissue lipolysis and sympathetic tone to fine-tune energy homeostasis (By similarity). Following activation by ALKAL2 ligand at the cell surface, transduces an extracellular signal into an intracellular response (PubMed : 30061385, PubMed : 33411331, PubMed : 34646012, PubMed : 34819673). In contrast, ALKAL1 is not a potent physiological ligand for ALK (PubMed : 34646012). Ligand-binding to the extracellular domain induces tyrosine kinase activation, leading to activation of the mitogen-activated protein kinase (MAPK) pathway (PubMed : 34819673). Phosphorylates almost exclusively at the first tyrosine of the Y-x-x-x-Y-Y motif (PubMed : 15226403, PubMed : 16878150). Induces tyrosine phosphorylation of CBL, FRS2, IRS1 and SHC1, as well as of the MAP kinases MAPK1/ERK2 and MAPK3/ERK1 (PubMed : 15226403, PubMed : 16878150). ALK activation may also be regulated by pleiotrophin (PTN) and midkine (MDK) (PubMed : 11278720, PubMed : 11809760, PubMed : 12107166, PubMed : 12122009). PTN-binding induces MAPK pathway activation, which is important for the anti-apoptotic signaling of PTN and regulation of cell proliferation (PubMed : 11278720, PubMed : 11809760, PubMed : 12107166). MDK-binding induces phosphorylation of the ALK target insulin receptor substrate (IRS1), activates mitogen-activated protein kinases (MAPKs) and PI3-kinase, resulting also in cell proliferation induction (PubMed : 12122009). Drives NF-kappa-B activation, probably through IRS1 and the activation of the AKT serine/threonine kinase (PubMed : 15226403, PubMed : 16878150). Recruitment of IRS1 to activated ALK and the activation of NF-kappa-B are essential for the autocrine growth and survival signaling of MDK (PubMed : 15226403, PubMed : 16878150). May function as regulator of gastric epithelial differentiation (By similarity).
Sequence similarities
Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily.
Post-translational modifications
Phosphorylated at tyrosine residues by autocatalysis, which activates kinase activity (PubMed:11121404, PubMed:15938644, PubMed:16878150, PubMed:34819673). In cells not stimulated by a ligand, receptor protein tyrosine phosphatase beta and zeta complex (PTPRB/PTPRZ1) dephosphorylates ALK at the sites in ALK that are undergoing autophosphorylation through autoactivation (PubMed:17681947). Phosphorylation at Tyr-1507 is critical for SHC1 association (PubMed:17274988).. N-glycosylated.
Target data
Additional targets
Product promise
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