IL-4R alpha/CD124 Protein, Mouse (HEK293, His)

IL-4R alpha is a subunit alpha shared by IL-4 and IL-13 receptors, found in leukocytes originally. IL-4R alpha couples to the JAK1/2/3-STAT6 pathway and involves in promoting Th2 differentiation. IL-4R alpha/CD124, Mouse exerts IL-4 binding function and results the phosphorylation of C-terminal tyrosine residues. IL-4R alpha/CD124, Mouse has an immunoreceptor tyrosine inhibitor motif (ITIM), which can bind to the SH2 domain of some phosphatases by phosphorylating ITIM. IL-4R alpha/CD124, Mouse has a transmembrane domain. IL-4R alpha/CD124 Protein, Mouse is produced in HEK293 cells, including a Fibronectin typr III domainand a C-terminal His-tag.

Interleukin-4R alpha (IL-4Rα), also known as CD124 and B cell stimulatory factor (BSF) receptor, is one of the anti-inflammatory cytokines, and highly expressed in activated T-cells^[1].
IL-4R alpha participates in forming two interleukin receptors in different cell types. For the type I receptor, depends on IL-4R alpha binding IL-4 to recruit IL-2R gamma chain in immune cells. IL-2R gamma is the common subunit for a variety of interleukin receptors, involved in the stimulation of neutrophil phagocytosis by IL-15. For the type II receptor, depends on IL-4R alpha binding IL-4 to recruit IL-13R alpha 1 chain. IL-13R alpha 1 is an alternat accessory protein to the common cytokine receptor gamma chain in non-immune cells^[2][3].
The sequence of amino acids in IL-4R alpha proteins in mouse shows low homology with human (52.82%) and rat (53.35%).
需要补上 IL-4 R alpha generates a soluble form by alternate splicing or proteolysis, maintaining ligand binding properties and inhibiting IL-4 bioactivity. IL-4 R alpha soluble isoform 1 can be produced by proteolytic cleavage at the cell surface (shedding) by a metalloproteinase^[4].
IL-4 R alpha plays an important role in Th2-biased immune responses, alternative macrophage activation, mucosal immunity, allergic inflammation, tumor progression, and atherogenesis^[5].

IL-4 R alpha plays a key role in the control of RSV-induced lung injury by alternatively activated macrophages, and induces AA-Mφ differentiation^[6].
IL-4 R alpha deficiency, in IL-4R alpha^-/- RSV infected mice model, leads to strong inflammation in the lungs compared with control^[6].

IL-4 R alpha is regulated by IFN-beta in response to RSV (severe respiratory syncytial virus), exhibits sustained proinflammatory cytokine production^[6].

Measured by its ability to inhibit the IL-4-dependent proliferation of HT-2 mouse T cells. The ED₅₀ for this effect is 0.17 μg/ml in the presence 3 ng/mL of Recombinant Mouse IL‑4, corresponding to a specific activity is 5.88×10^3 units/mg.

• 
  Measured by its ability to inhibit the IL-4-dependent proliferation of HT-2 mouse T cells. The ED₅₀ for this effect is 0.17 μg/mL in the presence 3 ng/mL of Recombinant Mouse IL‑4, corresponding to a specific activity is 5.88×10^3 units/mg.

Mouse

HEK293

C-6*His

P16382-1 (I26-R233)

16190  [NCBI]

Extracellular Domain

IKVLGEPTCFSDYIRTSTCEWFLDSAVDCSSQLCLHYRLMFFEFSENLTCIPRNSASTVCVCHMEMNRPVQSDRYQMELWAEHRQLWQGSFSPSGNVKPLAPDNLTLHTNVSDEWLLTWNNLYPSNNLLYKDLISMVNISREDNPAEFIVYNVTYKEPRLSFPINILMSGVYYTARVRVRSQILTGTWSEWSPSITWYNHFQLPLIQR

28-50 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]. Keegan AD,et al. An IL-4 receptor region containing an insulin receptor motif is important for IL-4-mediated IRS-1 phosphorylation and cell growth. Cell. 1994 Mar 11;76(5):811-20.  [Content Brief]

  [2]. Zurawski SM, et al. The primary binding subunit of the human interleukin-4 receptor is also a component of the interleukin-13 receptor. J Biol Chem. 1995 Jun 9;270(23):13869-78.  [Content Brief]

  [3]. Rolling C, et al. IL4 and IL13 receptors share the gamma c chain and activate STAT6, STAT3 and STAT5 proteins in normal human B cells. FEBS Lett. 1996 Sep 9;393(1):53-6.  [Content Brief]

  [4]. Jung T, et al. Soluble human interleukin-4 receptor is produced by activated T cells under the control of metalloproteinases. Int Arch Allergy Immunol. 1999 May;119(1):23-30.  [Content Brief]

  [5]. HageT,etal.Crystalstructureoftheinterleukin-4/receptoralphachaincomplexrevealsamosaicbindinginterface.Cell.1999Apr16;97(2):271-81.  [Content Brief]

  [6]. Shirey KA, Pletneva LM, Puche AC, Keegan AD, Prince GA, Blanco JC, Vogel SN. Control of RSV-induced lung injury by alternatively activated macrophages is IL-4R alpha-, TLR4-, and IFN-beta-dependent. Mucosal Immunol. 2010 May;3(3):291-300.  [Content Brief]

  [7]. Myburgh E, et al. Murine IL-4 is able to signal via chimeric human IL-4Ralpha/mouse gamma-chain receptor. Mol Immunol. 2008 Mar;45(5):1327-36.  [Content Brief]