Analytical Data
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Gene name
LYN
- Application
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Alternative Names
LYN;JTK8;Tyrosine-Protein kinase Lyn
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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
P07948
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Expression Region
2-512aa
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AA Sequence
GCIKSKGKDSLSDDGVDLKTQPVRNTERTIYVRDPTSNKQQRPVPESQLLPGQRFQTKDPEEQGDIVVALYPYDGIHPDDLSFKKGEKMKVLEEHGEWWKAKSLLTKKEGFIPSNYVAKLNTLETEEWFFKDITRKDAERQLLAPGNSAGAFLIRESETLKGSFSLSVRDFDPVHGDVIKHYKIRSLDNGGYYISPRITFPCISDMIKHYQKQADGLCRRLEKACISPKPQKPWDKDAWEIPRESIKLVKRLGAGQFGEVWMGYYNNSTKVAVKTLKPGTMSVQAFLEEANLMKTLQHDKLVRLYAVVTREEPIYIITEYMAKGSLLDFLKSDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIEDNEYTAREGAKFPIKWTAPEAINFGCFTIKSDVWSFGILLYEIVTYGKIPYPGRTNADVMTALSQGYRMPRVENCPDELYDIMKMCWKEKAEERPTFDYLQSVLDDFYTATEGQYQQQP
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Molecular Weight
64.4 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
LYN is a member of the Src family of tyrosine kinases, playing a crucial role in cellular signaling pathways that regulate various biological processes, including cell growth, differentiation, and immune responses. Research on LYN has gained significant attention due to its involvement in hematological malignancies, particularly in the context of B-cell receptor (BCR) signaling in diseases such as chronic lymphocytic leukemia (CLL) and diffuse large B-cell lymphoma (DLBCL). Aberrant LYN activity is often associated with poor prognosis and resistance to therapies, making it a potential therapeutic target. Studies have investigated the molecular mechanisms by which LYN contributes to oncogenesis, revealing its interactions with various substrates and regulatory proteins that modulate signaling cascades. The ongoing exploration of LYN's structural and functional properties aims to better understand its role in tumor biology and to develop strategies for targeted therapies that may enhance treatment efficacy in patients with cancer. This growing body of research highlights the need for innovative approaches to inhibit LYN function, offering hope for novel interventions that could improve patient outcomes in malignancies driven by dysregulated signaling pathways.
