Analytical Data
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Gene name
ALK
- Application
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Alternative Names
ALK; anaplastic lymphoma receptor tyrosine kinase; anaplastic lymphoma kinase (Ki 1); ALK tyrosine kinase receptor; CD246; CD246 antigen; mutant anaplastic lymphoma kinase; NBLST3;
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Species
Human
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Source
Baculovirus
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Tag
Avi
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9UM73
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Expression Region
V1058-P1620, L1196M
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Protein Length
Partial
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
The research on ALK (anaplastic lymphoma kinase) recombinant proteins has gained significant attention in recent years due to their critical role in various cancers, particularly in anaplastic large cell lymphoma and non-small cell lung cancer (NSCLC). ALK is a receptor tyrosine kinase that, when mutated or rearranged, contributes to oncogenesis via constitutive activation of signaling pathways that promote cell proliferation and survival. Advances in molecular biology have enabled the identification of ALK gene fusions with other genes, leading to the production of oncogenic fusion proteins that drive tumorigenesis. This has spurred the development of targeted therapies, such as ALK inhibitors, which have shown promise in clinical trials and transformed treatment paradigms for ALK-positive cancers. Research into ALK recombinant proteins not only aids in understanding the structure-function relationships of these proteins and their role in cancer biology but also provides insights into resistance mechanisms against ALK inhibitors. Such studies are crucial for optimizing therapeutic strategies and improving patient outcomes, emphasizing the need for continued exploration of ALK's biology and its implications in cancer treatment.
