IL-4R alpha/CD124 Protein, Rat (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^[1]. IL-4R alpha/CD124, Rat consists of 801 amino acids (M1-S801), exerts IL-4 binding function and results the phosphorylation of C-terminal tyrosine residues. IL-4R alpha/CD124, Rat has an immunoreceptor tyrosine inhibitor motif (ITIM) (698-703 a.a), which can bind to the SH2 domain of some phosphatases by phosphorylating ITIM. IL-4R alpha/CD124, Rat has a soluble form (1-229 a.a) and a transmembrane domain (233-256 a.a). The soluble IL-4R (sIL4R) inhibits IL4-induced spleen cell proliferation. IL-4R alpha/CD124 Protein, Rat (M1-R232) is produced in HEK293 cells, including a Fibronectin typr III domain (125-223 a.a) and 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 rat shows low homology with human (52.82%) and mouse (79.53%).
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 shows a high R/S value in extracellular domain that indicates selective pressure for amino acid exchanges, and shows a low R/S value for the intracellular part^[1].
IL-4 R alpha can be cleaved into a soluble interleukin-4 receptor, as sIL-4R, is expressed in kidney cells and antagonistically functional on IL-4-induced proliferation of spleen cells^[2].
sIL-4R is found not only in rats spleen cells but also in their glomerular epithelial cells (GEC)^[2].

IL-4 R alpha shows a high R/S value in extracellular domain that indicates selective pressure for amino acid exchanges, and shows a low R/S value for the intracellular part^[6].
IL-4 R alpha can be cleaved into a soluble interleukin-4 receptor, as sIL-4R, is expressed in kidney cells and antagonistically functional on IL-4-induced proliferation of spleen cells^[7].
sIL-4R is found not only in rats spleen cells but also in their glomerular epithelial cells (GEC)^[7].

Measured by its ability to bind mouse IL4-His in a functional ELISA.

Rat

HEK293

C-His

Q63257 (M1-R232)

25084  [NCBI]

Approximately 25.3 kDa

Greater than 95% as determined by reducing SDS-PAGE

Lyophilized powder.

Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween 80 are added as protectants 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]. 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]. Richter G, et al. The rat interleukin 4 receptor: coevolution of ligand and receptor. Cytokine. 1995 Apr;7(3):237-41.  [Content Brief]

  [7]. Guangping, et al. Identification of soluble interleukin-4 receptor in rat glomerular epithelial cells[J]. Biochimica Et Biophysica Acta Molecular Cell Research, 1999.