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14-555-M

Sigma-Aldrich

Alk Protein, active, 10 µg

Active, N-terminal His6-tagged, recombinant human ALK, residues 1058-end, for use in Kinase Assays.

Synonym(s):

Anaplastic lymphoma kinase

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About This Item

UNSPSC Code:
12352202
eCl@ss:
32160405
NACRES:
NA.32

biological source

human

Quality Level

recombinant

expressed in baculovirus infected Sf21 cells

mol wt

Mw 63.8 kDa

manufacturer/tradename

Upstate®

technique(s)

activity assay: suitable (kinase)

NCBI accession no.

UniProt accession no.

General description

Research area: CELL SIGNALING

Product Source: expressed by baculovirus in Sf21 cells

The anaplastic lymphoma kinase (ALK) is a member of the insulin receptor superfamily of receptor tyrosine kinases. The ALK gene is located on human chromosome 2p23 and shares a high similarity with the leukocyte tyrosine kinase (Ltk). ALK is composed of three domains: an extracellular domain responsible for ligand binding, a transmembrane domain that spans the cell membrane, and a cytoplasmic domain housing the tyrosine kinase activity. The cytoplasmic tyrosine kinase domain of ALK plays a significant role in disease pathologies associated with the gene. Within the structure, there are two short conserved β-strands (β7-β8) housing majority of the catalytic residues. Full-length ALK is specifically expressed in the developing central and peripheral nervous systems during embryogenesis and is associated with the balance of cell proliferation and differentiation.

Application

Research Category

Inflammation & Immunology

Biochem/physiol Actions

Protein Target: ALK

Target Sub-Family: TK Anaplastic lymphoma kinase (ALK) plays a crucial role in the development of neurons. Binding of ligand to its extracellular domain triggers the activation of the tyrosine kinase that in turn activates the mitogen-activated protein kinase (MAPK) pathway. ALK fusion proteins induce the activation of diverse pathways including Phospholipase C gamma (PLC-γ) and Ras/Extracellular Signal-Regulated Kinase 1/2 (Ras/ERK1/2), which contribute to cell proliferation, while the Janus Kinase/signal transducer and activator of transcription (JAK/STAT) pathway and Phosphoinositide 3-kinase/Protein Kinase B (PI3K/Akt) pathways facilitate cell survival. Notably, ALK has been found to be overexpressed in various human tumors and cell lines such as lymphomas, neuroblastoma, and non-small-cell lung cancer.

Quality

routinely evaluated by phosphorylation of IGF-1Rtide

Physical form

Ni2+/NTA-agarose

Storage and Stability

6 months at -70°C from date of shipment

Other Notes

For Specific Activity data, refer to the Certificate of Analysis for individual lots of this enzyme.

Legal Information

UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Mechanistic insight into ALK receptor tyrosine kinase in human cancer biology
Hallberg B and Palmer RH
Nature Reviews. Cancer, 13(10), 685-700 (2013)
Mechanism for the activation of the anaplastic lymphoma kinase receptor
Reshetnyak AV, et al.
Nature, 600(7887), 153-157 (2021)
ALK a novel lymphoma-associated tumor antigen for vaccination strategies.
Passoni, Lorena and Gambacorti-Passerini, Carlo
Leukemia & Lymphoma, 44, 1675-1681 (2003)
Anaplastic lymphoma kinase (ALK): structure, oncogenic activation, and pharmacological inhibition
Roskoski R Jr
Pharmacological Research, 68(1), 68-94 (2013)
Anaplastic lymphoma kinase proteins in growth control and cancer.
Pulford, K, et al.
Journal of Cellular Physiology, 199, 330-358 (2004)

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