Analytical Data
-
Gene name
FLI1
- Application
-
Alternative Names
FLI1；Friend leukemia integration 1 transcription factor
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q01543
-
Expression Region
1-452aa
-
AA Sequence
MDGTIKEALSVVSDGQSLFDSAYGAAAHLPKADMAASGSPDYGQPHKINP LPPQQEWISQPVRVNVKREYDHMNGSRESPVDCSVSKCSKLVGGGESNPM NYNSYMDEKNGPPPPNMTTNERRVIVPADPTLWTQEHVRQWLEWAIKEYS LMEIDTSFFQNMDGKELCKMNKEDFLRATTLYNTEVLLSHLSYLRESSLL AYNTTSHTDQSSRLSVKEDPSYDSVRRGAWGNNMNSGLNKSPPLGGAQTI SKNTEQRPQPDPYQILGPTSSRLANPGSGQIQLWQFLLELLSDSANASCI TWEGTNGEFKMTDPDEVARRWGERISKPNMNYDKLSRALRYYYDKNIMTK VHGKRYAYKFDFHGIAQALQPHPTESSMYKYPSDISYMPSYHAHQQKVNF VPPHPSSMPVTSSSFFGAASQYWTSPTGGIYPNPNVPRHPNTHVPSHLGS YY
-
Molecular Weight
75 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
FLI1 (Fused in Sarcoma, Friend Leukemia Integration 1) is a transcription factor that plays a critical role in various biological processes, including embryonic development, hematopoiesis, and the regulation of cell differentiation. Its significance is highlighted by its involvement in certain oncogenic processes, particularly in hematological malignancies such as acute myeloid leukemia (AML) and lymphoma, where FLI1 can contribute to tumorigenesis through aberrant gene expression. Research has shown that FLI1 interacts with various signaling pathways and transcriptional networks, making it a pivotal component in both normal cellular functions and disease states. The recombinant expression of FLI1 protein is essential for elucidating its structure-function relationships, discovering its protein-protein interactions, and exploring its role in transcriptional regulation. Advanced techniques such as X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy can provide insights into FLI1's three-dimensional structure, potentially leading to the identification of new therapeutic targets. Moreover, studying recombinant FLI1 protein offers opportunities for developing novel strategies in cancer treatment, especially in targeting FLI1-mediated signaling pathways. This research is crucial for understanding the molecular mechanisms underlying FLI1 function, ultimately paving the way for innovative diagnostics and targeted therapies in cancers associated with FLI1 dysregulation.
