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.
Availability June 30, 2025
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Species : Human
Source : Human Cells
Tag : GST&His
Protein Length : 1-173 a.a.
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.
Publications :
Soluble Fas affects erythropoiesis in vitro and acts as a potential predictor of erythropoiesis-stimulating agent therapy in patients with chronic kidney disease (2020)
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

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.

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.

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.

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.

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