Recombinant Human Activin E Protein, CF

Measured by its ability to activate ALK7-dependent SEAP reporter activity in HEK293 human embryonic kidney cells. The ED50 for this effect is 1.00-10.0 ng/mL.

2 μg/lane of Recombinant Human Activin E Protein (Catalog # 11779-AE) was resolved with SDS-PAGE under reducing (R) condition and visualized by Coomassie® Blue staining, showing bands at 12-15 kDa.

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human Activin E Protein, CF Summary

• Details of Functionality: Measured by its ability to activate CAGA-SEAP reporter in HEK293 human embryonic kidney cells transfected with human ALK7. The ED50 for this effect is 1.00-10.0 ng/mL.
• Source: E. coli-derived human INHBE protein
  Thr237-Ser350
• Accession #: P58166.1
• N-terminal Sequence: Met-Thr237
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 13 kDa.
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
• SDS-PAGE: 12-15 kDa, under reducing conditions.

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in HCl with Trehalose.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining
• Reconstitution Instructions: Reconstitute at 250 μg/mL in water.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Activin E Protein, CF

• activin beta E
• Activin beta-E chain
• activin
• INHBE
• inhibin beta E chain
• Inhibin Beta E
• inhibin, beta E
• MGC4638

Background

Activin E, encoded by the INHBE gene, is a liver-enriched member of the transforming growth factor-beta (TGF-beta ) superfamily and functions as a hepatokine involved in systemic energy homeostasis. Structurally, it is a disulfide-linked homodimer of mature inhibin beta E subunits, sharing the conserved cystine-knot motif characteristic of TGF-beta ligands, which facilitates receptor binding and downstream signaling activation (1). Activin E signals through the type I receptor ALK7 (ACVR1C), activating the SMAD2/3 pathway and repressing PPARG target genes in adipose tissue (2). This signaling cascade suppresses beta -adrenergic-induced lipolysis, thereby promoting lipid retention in white adipose tissue and preventing excessive hepatic lipid influx during metabolic stress such as fasting (2, 3). In murine models, mRNA knocked down results in increased fat oxidation, reduced adiposity, and improved metabolic profiles under high-fat diet conditions (3). Conversely, hepatic overexpression of INHBE leads to visceral fat accumulation and adipocyte hypertrophy, indicating a maladaptive role in obesity (4). Rare loss-of-function variants in human INHBE are associated with favorable fat distribution and reduced risk of type 2 diabetes, highlighting its clinical relevance (4). Expression of INHBE is upregulated by ATF4 during endoplasmic reticulum stress, linking it to nutrient sensing and adaptive metabolic responses (5). These findings underscore the potential of recombinant Activin E as a therapeutic target for metabolic disorders such as nonalcoholic fatty liver disease (NAFLD) and obesity (5).

1. Morita, M. Hashimoto, O. (2019) Molecular Biology Reports 46:1603. 
2.  Adam, R.C. et al. (2023) Proc Natl Acad Sci U S A 120:e2309967120 
3.  Sugiyama, M. et al. (2018) Plos one 13:e0194798.
4.  Deaton, A.M. et. al. (2022) Nat Commun. 13: 4319. 
5. Park, S.Y. et al. (2025) Exp Mol Med 57:466.

Bioinformatics

• Uniprot:
  • P58166.1()