Recombinant Human FAS, His & GST tagged

• Cat.No.: FAS-281H
• Product Overview: Recombinant Human FAS extracellular domain (Met 1-Glu 173) (NP_000034.1), fused with the Fc region of human IgG1 at the C-terminus, was produced in Human Cell.

Specification

• Source: Human Cells
• Species: Human
• Tag: His&GST
• Form: Lyophilized from sterile PBS, pH 7.4
• Molecular Mass: The recombinant human Fas/Fc chimera is a disulfide-linked homodimeric protein generated after removal of the signal peptide. The reduced monomer consists of 386 amino acids and has a predicted molecular mass of 43.4 kDa. In SDS-PAGE under reducing conditions, the monomer migrates as an approximately 55-60 kDa protein due to glycosylation.
• Endotoxin: < 1.0 eu per μg of the protein as determined by the LAL method.
• Stability: Samples are stable for up to twelve months from date of receipt at -70oC.
• Storage: Store it under sterile conditions at -20oC~-70oC. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
• Reconstitution: It is recommended that sterile water be added to the vial to prepare a stock solution. Centrifuge the vial at 4℃ before opening to recover the entire contents.
• Protein length: Met1-Glu173

Gene Information

• Gene Name: FAS Fas (TNF receptor superfamily, member 6) [ Homo sapiens ]
• Official Symbol: FAS
• Gene ID: 355
• mRNA Refseq: NM_000043
• Protein Refseq: NP_000034
• MIM: 134637
• UniProt ID: P25445

Citation

Soluble Fas affects erythropoiesis in vitro and acts as a potential predictor of erythropoiesis-stimulating agent therapy in patients with chronic kidney disease

Journal: American Journal of Physiology - Renal Physiology    PubMed ID: 32003597    Data: 2021/4/1

Authors: Daniela Mendes Chiloff, Danilo Candido de Almeida, Miguel Angelo Goes

Article Snippet:Isolated CD34 + cells were seeded into Nunc four-well dishes (ThermoFisher Scientific) at a density of 1.0 × 10 5 cells/mL in 2 mL (per well) of methylcellulose-based Iscove’s modified DMEM containing FBS, BSA, human transferrin (iron-saturated), 2-mercaptoethanol, supplements, and the following recombinant human growth factors/cytokines: insulin, stem cell factor, IL-3, granulocyte-macrophage colony-stimulating factor, and Epo (MethoCult GF 4434 Classic, STEMCELL Technologies).dishes (ThermoFisher Scientific) at a density of 1.0 × 10 5 cells/mL in 2 mL (per well) of methylcellulose-based Iscove’s modified DMEM containing FBS, BSA, human transferrin (iron-saturated), 2-mercaptoethanol, supplements, and the following recombinant human growth factors/cytokines: insulin, stem cell factor, IL-3, granulocyte-macrophage colony-stimulating factor, and Epo (MethoCult GF 4434 Classic, STEMCELL Technologies). ... Cells were divided into 18 wells in 6 plates for CD34 + cells and incubated for 14 days ( 13 , 30 ) in the absence or presence of various levels of human recombinant sFas (FAS-FAS-281H, Creative BioMart).. We tested the effects of both 1 ) high levels (sFas-Hc group: 2, 4, and 8 ng/mL) and 2 ) low levels (sFas-Lc group: 0, 0.5, and 1 ng/mL) of sFas on CD34 + HSCs.We tested the effects of both 1 ) high levels (sFas-Hc group: 2, 4, and 8 ng/mL) and 2 ) low levels (sFas-Lc group: 0, 0.5, and 1 ng/mL) of sFas on CD34 + HSCs.

Global correlations between the variables analyzed. Correlations were performed using our data collection comprising 77 patients with nondialysis chronic kidney disease patients with anemia and not submitted to erythropoiesis-stimulating agent (ESA) therapy at baseline. We observed a positive correlation between serum erythropoietin (EPO) versus soluble Fas (sFas), hemoglobin (Hgb) versus estimated glomerular filtration rate (eGFR) and Hgb versus transferrin. In contrast, we detected a negative correlation among Hgb versus sFas, eGFR versus sFas, and EPO versus transferrin. P < 0.05.

Direct comparison of soluble Fas (sFas), hemoglobin (Hgb), and estimated glomerular filtration rate (eGFR) levels in patients with erythropoiesis-stimulating agent (ESA) and non-ESA therapy. sFas, Hgb, and eGFR were compared between patients that needed ESA therapy and those who did not need ESA therapy at their baseline. The violin-plot chart shows clearly that patients who further needed ESA therapy in our followup presented higher levels of sFas and a lower index of Hgb and eGFR at baseline than patients who did not submitted to ESA therapy. After 6 yr of followup, we verified that eGFR and Hgb index remained decreased in patients who needed ESA treatment. P < 0.05.

Analyze of the human recombinant soluble Fas (sFas) influence on in vitro erythropoiesis. The concentration of sFas protein negatively correlated with the number of erythroid progenitor colonies (BFU-e/CFU-e). Also, it was observed that higher concentrations of recombinant human sFas protein presented smaller number of global erythroid colonies. BFU-e, burst forming unit-erythroid; CFU-e, colony forming unit-erythroid; Lc-sFas group, low concentrations of recombinant human sFas protein (0, 0.5, and 1 ng/mL); Hc-sFas group, high concentrations of recombinant human sFas protein (2, 4, and 8 ng/mL). P < 0.05.

Publication :

Soluble Fas affects erythropoiesis in vitro and acts as a potential predictor of erythropoiesis-stimulating agent therapy in patients with chronic kidney disease (2020)

Reviews

09/07/2022

When experimenting with FAS, the results are very reproducible.

07/29/2022

The stability of FAS products allows them to cope with different experimental conditions and modes of operation.

09/20/2021

FAS has high specific activity and can exert strong biological effect at low concentration.

Q&As

Does FAS protein play a role in cell signaling?

FAS protein plays an important role in cell signaling, it can activate downstream signaling pathways, such as death signaling pathway and survival signaling pathway, by binding to its ligand and transmitting signals.

Why apply knowledge of FAS proteins to clinical practice?

It can provide a reference for clinical practice and guide the diagnosis, treatment and prevention of diseases by detecting the expression level of FAS protein and understanding its mechanism of action.

How can diseases associated with FAS protein be prevented and treated?

FAS protein-related diseases can be prevented and treated by regulating the expression level of FAS protein and inhibiting its signaling pathway.

How can gene knockout or knockdown techniques be used to study the function of FAS proteins?

Gene knockout or knockdown techniques can be used to study the function and mechanism of action of FAS proteins. By knocking out or knocking down the FAS gene, changes in processes such as apoptosis and immune response can be observed to further understand its function and mechanism of action.

What is the role of FAS protein in apoptosis?

FAS protein can bind to its ligand, activate the death signaling pathway, and induce apoptosis.

How can FAS protein be used to predict disease prognosis?

The expression level and activity of FAS protein can be measured to predict the prognosis and development trend of certain diseases.