ACVR2A/Activin RIIA Protein, Mouse (HEK293, His)

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, Mouse (HEK293, His) is produced in HEK293 cells with a C-Terminal His-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].

Recombinant mouse ACVR2A (2.5 μg/.1 mL/mouse, i.v) significantly reduces the parasitemia levels in malarial mice^[2].

1.This product does not contain protein kinase domain.
2.Measured by its ability to neutralize Activin-mediated inhibition on MPC11 cell proliferation.The ED₅₀ for this effect is typically 0.4-3 μg/mL in the presence of 10 ng/mL Recombinant Human Activin A.

• 
  Measured by its ability to neutralize Activin-mediated inhibition on MPC11 cell proliferation.The ED₅₀ for this effect is 0.7681 μg/mL in the presence of 10 ng/mL Recombinant Human Activin A, corresponding to a specific activity is 1302 U/mg.

Mouse

HEK293

C-His

P27038 (A20-P134)

11480  [NCBI]

Extracellular Domain

AILGRSETQECLFFNANWERDRTNQTGVEPCYGDKDKRRHCFATWKNISGSIEIVKQGCWLDDINCYDRTDCIEKKDSPEVYFCCCEGNMCNEKFSYFPEMEVTQPTSNPVTPKP

Approximately 35 kDa

• 
  ≥ 95%, as determined by reducing SDS-PAGE.

Lyophilized powder.

Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Stored at -20°C for 2 years from date of receipt. 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]