Analytical Data
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Gene name
ILK
- Application
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Alternative Names
ILK；ILK1；ILK2；Integrin-linked Protein kinase
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q13418
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Expression Region
1-452aa
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AA Sequence
MDDIFTQCREGNAVAVRLWLDNTENDLNQGDDHGFSPLHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLLQYKADINAVNEHGNVPLHYACFWGQDQVAEDLVANGALVSICNKYGEMPVDKAKAPLRELLRERAEKMGQNLNRIPYKDTFWKGTTRTRPRNGTLNKHSGIDFKQLNFLTKLNENHSGELWKGRWQGNDIVVKVLKVRDWSTRKSRDFNEECPRLRIFSHPNVLPVLGACQSPPAPHPTLITHWMPYGSLYNVLHEGTNFVVDQSQAVKFALDMARGMAFLHTLEPLIPRHALNSRSVMIDEDMTARISMADVKFSFQCPGRMYAPAWVAPEALQKKPEDTNRRSADMWSFAVLLWELVTREVPFADLSNMEIGMKVALEGLRPTIPPGISPHVCKLMKICMNEDPAKRPKFDMIVPILEKMQDK
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Molecular Weight
54.8 kDa
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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
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Protein Description
ILK (Integrin-Linked Kinase) is a crucial protein that plays a significant role in various cellular processes, including cell adhesion, migration, survival, and proliferation. Its involvement in the signaling pathways associated with integrin receptors links the extracellular matrix to the cytoskeleton, thereby influencing cellular responses to the environment. Research on ILK has gained momentum due to its implications in various diseases, particularly cancer, where aberrant ILK expression and activity have been associated with tumor progression and metastasis. The study of recombinant ILK proteins has become an important avenue for understanding its structure, function, and interactions with other signaling molecules. By producing ILK in a recombinant system, researchers can effectively analyze its biochemical properties and elucidate the mechanisms through which it contributes to cellular processes in health and disease. This includes studies on its kinase activity, its role in regulating cell survival pathways, and its interactions with integrin and other signaling components. Additionally, recombinant ILK proteins provide a valuable tool for therapeutic targeting, as inhibiting ILK activity could serve as a potential strategy for treating cancers and other diseases characterized by dysregulated cell signaling. Overall, the investigation of ILK through recombinant approaches holds promise for advancing our understanding of its biological roles and developing novel therapeutic interventions.
