Follistatin/FST 蛋白, Mouse (HEK293, His)

Follistatin (FST) is a regulator of TGFβ family signaling and acts by selectively binding to TGFβ family ligands and preventing ligand binding to the receptor complex. Follistatin has the ability to suppress the follicle stimulating hormone (FSH)^[1][2]. Follistatin/FST Protein, Mouse (HEK293, His) is produced in HEK293 cells with a C-Terminal His-tag. It consists of 344 amino acids (M1-W344).

卵泡抑素首先被描述为存在于卵巢卵泡液中的卵泡刺激激素抑制物质。卵泡抑素以低纳摩尔 (nM) 亲和力结合激活素 A 和肌生长抑制素，完全包围配体，封闭所有受体结合位点并与配体结合^[1][2] .
成熟的人卵泡抑素与小鼠和大鼠卵泡抑素具有 97% 的氨基酸序列同一性。
卵泡抑素是一种 32-35-kDa 的糖蛋白，由四个结构域组成，包括一个 N 端结构域 (ND)，后跟三个结构域卵泡抑素结构域（FSD1、FSD2 和 FSD3）。卵泡抑素的 C 端剪接可产生各种同工型，包括 FS288 和 FS315。卵泡抑素通过围绕配体形成几乎不可逆的非信号复合物并防止与 TGFβ 受体相互作用，从而中和 TGFβ 配体、肌生长抑制素和激活素 A。在人类中，编码卵泡抑素的基因位于染色体 5q11.2 上。卵泡抑素蛋白含有 TGF-β 结合位点，其中激活素、骨形态生成蛋白 (BMP) 和生长分化因子 (GDF) 以高亲和力结合，从而被中和。卵泡抑素的配体结合位点与这些配体的 I 型和 II 型受体结合位点重叠。卵泡抑素还含有肝素结合位点，细胞外基质中的蛋白聚糖可以结合该位点，因此卵泡抑素被认为结合细胞外基质。卵泡抑素有两种主要亚型：FST288（通过与硫酸肝素蛋白聚糖相互作用固定在细胞表面）和 FST315（循环中的主要形式）。这两种异构体由选择性剪接产生。315 同种型包括 27 个氨基酸的酸性 C 末端尾部，而 Follistatin 288 则没有。Follistatin 315 上的酸性尾部中和肝素结合位点，从而抑制 Follistatin 315 与细胞外基质的结合^[1][2][3].
卵泡抑素作为一种肝源性蛋白质，受胰高血糖素与胰岛素比例的调节，表明与能量代谢有关。在人类中，FST 和激活素的异常表达与不孕症有关。卵泡抑素是性腺、垂体、妊娠膜、脉管系统和肝脏中的有效组织调节剂^[1][3]。

Recombinant mouse Follistatin (.2 μg/mL; 1-48 hours) significantly inhibits P21 mRNA expression, and increases Pcna and Cyclin D2 mRNA expression in CD49f positive cells (CD49f⁺ cells) isolated from male murine salivary glands^[4].

Recombinant mouse Follistatin (.5-1 μg; four does) is administered intranasally (5 μL) 1 h before each challenge in ovalbumin-sensitized BALB/c mice. Follistatin inhibits the allergen-specific Th2 immune response in mediastinal lymph nodes and mucus production in the lung^[5].

1. Measured by its ability to neutralize Activin-mediated inhibition on MPC11 cell proliferation and the ED₅₀ is 0.01-0.08 μg/mL in the presence of 10 ng/mL Human Activin A.
2. Measured in a cell proliferation assay using MPC-11 cells. The ED₅₀ this effect is 0.177 μg/mL, corresponding to a specific activity is 5.65×10³ units/mg.

• 
  Measured in a cell proliferation assay using MPC-11 cells. The ED₅₀ this effect is 0.177 μg/ml, corresponding to a specific activity is 5.65×10³ units/mg.

Mouse

HEK293

C-His

P47931-1 (G30-W344)

14313  [NCBI]

GNCWLRQAKNGRCQVLYKTELSKEECCSTGRLSTSWTEEDVNDNTLFKWMIFNGGAPNCIPCKETCENVDCGPGKKCRMNKKNKPRCVCAPDCSNITWKGPVCGLDGKTYRNECALLKARCKEQPELEVQYQGKCKKTCRDVFCPGSSTCVVDQTNNAYCVTCNRICPEPSSSEQYLCGNDGVTYSSACHLRKATCLLGRSIGLAYEGKCIKAKSCEDIQCGGGKKCLWDSKVGRGRCSLCDELCPDSKSDEPVCASDNATYASECAMKEAACSSGVLLEVKHSGSCNSISEETEEEEEEEDQDYSFPISSILEW

Approximately 47.42 kDa

• 
  Greater than 95% as determined by reducing SDS-PAGE

无菌粉末.

Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4 or 20 mM PB, 150 mM NaCl, 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. 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]. Jakob Schiøler Hansen, et al. Circulating follistatin in relation to energy metabolism. Mol Cell Endocrinol. 2016 Sep 15;433:87-93.  [Content Brief]

  [2]. Ryan G Walker, et al. Heparin-mediated dimerization of follistatin. Exp Biol Med (Maywood). 2021 Feb;246(4):467-482.  [Content Brief]

  [3]. D J Phillips, et al. Follistatin: a multifunctional regulatory protein. Front Neuroendocrinol. 1998 Oct;19(4):287-322.  [Content Brief]

  [4]. A Ikeda, et al. Follistatin expressed in mechanically-damaged salivary glands of male mice induces proliferation of CD49f+ cells. Sci Rep. 2020 Nov 17;10(1):19959.  [Content Brief]

  [5]. C L Hardy, et al. Follistatin is a candidate endogenous negative regulator of activin A in experimental allergic asthma. Clin Exp Allergy. 2006 Jul;36(7):941-50.  [Content Brief]