Analytical Data
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Gene name
FASL
- Application
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Alternative Names
FASL；APT1LG1；CD95L；FASL；Tumor necrosis factor ligand superfamily member 6
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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
P48023
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Expression Region
103-281aa
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AA Sequence
QIGHPSPPPEKKELRKVAHLTGKSNSRSMPLEWEDTYGIVLLSGVKYKKG GLVINETGLYFVYSKVYFRGQSCNNLPLSHKVYMRNSKYPQDLVMMEGKM MSYCTTGQMWARSSYLGAVFNLTSADHLYVNVSELSLVNFEESQTFFGLY KL
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Molecular Weight
32 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
Related Products
Protein Description
FASL (Fas ligand) is a crucial component of the immune system, primarily involved in regulating apoptosis, or programmed cell death, through its interaction with the Fas receptor. Understanding the mechanisms by which FASL exerts its effects has significant implications for cancer therapy, autoimmune diseases, and transplantation. Recombinant FASL proteins have been developed to study these mechanisms in vitro and in vivo, providing insights into its role in immune regulation and potential therapeutic applications. Researchers have focused on various aspects of FASL, including its structure, signaling pathways, and interactions with other immune cells. The study of FASL-recombinant proteins allows for the examination of their functional properties, such as binding affinities and the ability to induce apoptosis in target cells. As scientists explore the therapeutic potential of FASL, including its role in enhancing antitumor immunity or blocking unwanted immune responses, the continued investigation of recombinant FASL proteins remains a significant area of research in immunology and cancer biology. This understanding paves the way for novel treatments aimed at manipulating the immune response to improve patient outcomes in various diseases.
