ACVR2A/Activin RIIA Protein, Human (HEK293, Fc)

ACVR2A, also known as Activin RIIA, is an activin type II receptor. On ligand binding, ACVR2A can forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. ACVR2A is a receptor for Activin A, Activin B and Inhibin A^[1][2]. ACVR2A/Activin RIIA Protein, Human (HEK293, Fc) is produced in HEK293 cells with a C-Terminal Fc-tag. It consists of 134 amino acids (M1-P134).

ACVR2A is a type II member of the TGF-β family of receptor Serine/Threonine kinases. ACVR2A is a receptor for Activin A, Activin B and Inhibin A^[1][2].
The sequence of amino acids in ACVR2A proteins from different species is very stable, which leads to the conclusion that in the process of evolution, ACVR2A has been only slightly altered, and that both in humans and in animals, its function is similar.
Signaling by activins and BMPs is highly promiscuous, since apart from signaling through ALK4/7, the activin type II receptors (ACVR2A and 2B) can interact also with several type I BMP receptors (ALK1/2/3/6), which can also form complexes with the type II BMP receptor, BMPRII. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. ACVR2A can form complexes with different type I receptors that signal either to Smad2/3 (ALK4) or to Smad1/5/8 (ALK2, ALK3, ALK6). The different type I receptors compete for binding to ACVR2A and that this competition provides a mechanism that balances signaling between Activin A-mediated, ALK4-dependent Smad2/3 signaling, and BMP-mediated ALK2 or ALK3-dependent signaling to Smad1/5/8. In myeloma cells, BMP-6- and BMP-9-induced activation of SMAD1/5/8 through ACVR2A/ACVR2B/ALK2 is inhibited by activin A treatment^[1][3].

Recombinant human ACVR2A (5 μg/mL) inhibits the effects of BMP-9 on INA-6 and IH-1 cells^[1].
Recombinant human ACVR2A (1 μg/mL; 96 hours) blocks the β-cell-proliferative effect of adenoviruses containing mouse Pdx-1 (AdCMV-mPdx-1) treatment^[4].

1.Immobilized Human Activin A, No Tag at 1μg/ml (100μl/well) on the plate. Dose response curve for Human Activin RIIA, hFc Tag with the EC₅₀ of 1.6ng/ml determined by ELISA.
2.Measured by its ability to neutralize Activin-mediated inhibition on MPC-11 cell proliferation. The ED₅₀ for this effect is typically 54.24 ng/mL in the presence of 10 ng/ml Recombinant Human Activin A, corresponding to a specific activity is 1.84×10⁴ units/mg.

Human

HEK293

C-hFc

P27037-1 (A20-P135)

92  [NCBI]

AILGRSETQECLFFNANWEKDRTNQTGVEPCYGDKDKRRHCFATWKNISGSIEIVKQGCWLDDINCYDRTDCVEKKDSPEVYFCCCEGNMCNEKFSYFPEMEVTQPTSNPVTPKPP

Approximately 55-70kDa due to the glycosylation.

Greater than 95% as determined by reducing SDS-PAGE

Lyophilized powder

Lyophilized from 0.22 μm filtered solution in PBS (pH 7.4). Normally 8% trehalose is added as protectant before lyophilization.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.

• [1]. Oddrun Elise Olsen, et al. Activin A inhibits BMP-signaling by binding ACVR2A and ACVR2B. Cell Commun Signal. 2015 Jun 6;13:27.  [Content Brief]

  [2]. V K Chin, et al. Inhibition of Activin A suppressed tumor necrosis factor-α secretion and improved histopathological conditions in malarial mice. Trop Biomed. 2021 Mar 1;38(1):187-204.  [Content Brief]

  [3]. Szabina Szófia Szilágyi, et al. Competition between type I activin and BMP receptors for binding to ACVR2A regulates signaling to distinct Smad pathways. BMC Biol. 2022 Feb 18;20(1):50.  [Content Brief]

  [4]. Heather L Hayes, et al. A Pdx-1-Regulated Soluble Factor Activates Rat and Human Islet Cell Proliferation. Mol Cell Biol. 2016 Nov 14;36(23):2918-2930.  [Content Brief]