IL-6R alpha Protein, Mouse (HEK293, His)
Based on 1 Customer Validation
IL-6R alpha is a subunit alpha of IL-6 receptors, also shared by other interleukin receptors. IL-6R alpha acts as IL-6 agonist and involves in JAK/STAT, MAPK, and Akt signaling pathway. IL-6R alpha, Mouse consists of 460 amino acids (M1-R460) with two fibronectin type-III-like domains contained in the N-terminal part (109-214 a.a, 215-313 a.a). Soluble IL-6R (sIL-6R) can be detected in the cerebrospinal fluid, conducts trans signaling by binding IL-6 and dimerized gp130, and exhibits a immune tissue expression property. IL-6R alpha Protein, Mouse (HEK293, His) is soluble form and produced in HEK293 cells with a C-Terminal His-tag.
- Species: Mouse
- Source: HEK293
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Storage: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.
Biological Activity
Description
IL-6R alpha is a subunit alpha of IL-6 receptors, also shared by other interleukin receptors. IL-6R alpha acts as IL-6 agonist and involves in JAK/STAT, MAPK, and Akt signaling pathway[1][2]. IL-6R alpha, Mouse consists of 460 amino acids (M1-R460) with two fibronectin type-III-like domains contained in the N-terminal part (109-214 a.a, 215-313 a.a). Soluble IL-6R (sIL-6R) can be detected in the cerebrospinal fluid, conducts trans signaling by binding IL-6 and dimerized gp130, and exhibits a immune tissue expression property. IL-6R alpha Protein, Mouse (HEK293, His) is soluble form and produced in HEK293 cells with a C-Terminal His-tag.
Background
IL-6 acts as both inflammatory factor and anti-inflammatory factor, fuels cancer progression through activating a series of downstream signalling cascade including gp130 (dimers), JAK/STAT, MAPK, and Akt[1][2].
IL-6R alpha (IL-6Rα) as a part of the receptor for interleukin 6, is a type I transmembrane glycoprotein, which forms a complex with the type I transmembrane signal transducer Glycoprotein 130 (CD130) and regulates the biological activity of IL-6 with a low affinity[3].
The sequence of amino acids in IL-6R alpha proteins of mouse is very different from human (54.07%), but shows high similarity with rat (89.3%).
IL-6R alpha has 2 isoform including mIL6R (the longer one) or sIL6R (the shorter one):
The mIL6R is membrane-bound interleukin-6 receptor, has the potential to drive naive CD4+ T cells to the Th17 lineage, through 'cluster signaling' by dendritic cells[4].
The sIL-6R is soluble interleukin-6 receptor subunit, cleaved from IL-6R alpha (IL-6Rα) in activated CD4+ T cells by proteolysis, and serves as IL-6 agonist. sIL-6R binds membrane-bound IL6R and subunit IL6ST to activate regenerative and anti-inflammatory signal via IL-6 trans signaling and promotes pro-inflammatory properties of IL-6. The hydrolysis of IL-6R alpha is also called ectodomain shedding[1].
IL-6R alpha involves in regulating cell growth and differentiation, and plays an important role in regulation of immune response, acute-phase reactions and hematopoiesis[5].
However, IL-6R alpha shows tissue expression specificity in liver and some cells of the immune system, thus results a limitation of IL6 signaling[6].
It's worth noting that IL-6R alpha dysregulation is implicated in the pathogenesis of many diseases, such as multiple myeloma, autoimmune diseases, and prostate cancer[7][8].
In Vitro
IL-6R (mSR323) (10 ng/mL; 60 min; room temperature) binds MR16-1, the IL-6R antibody, with the N-terminal half of the fibronectin domain II in COS-7 cells[1].
In Vivo
sIL-6R (mIL-6R α) achieves accelerated regeneration of the axotomized nerve in transgenic mice constitutively expressing both IL-6 and IL-6R, compared with nontransgenic controls[2].
IL-6 signal may play an important role in nerve regeneration after trauma in vivo[2].
sIL-6R (mIL-6R α), causes nodular regenerative hyperplasia and adenomas of the liver in over-expressing double IL-6/sIL-6R transgenic mice[3].
Verified Bioactivity
Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 for this effect is 3.014 ng/mL in the presence of 2 ng/mL recombinant mouse IL-6, corresponding to a specific activity is 3.32×105 units/mg.
MCE Validation Data
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Purity - SDS-PAGE
Purity - SDS-PAGE
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Bioactivity - Cell-Based Assay
Bioactivity - Cell-Based Assay
Technical Parameters
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Species Mouse
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Source HEK293
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Tag C-6*His
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Accession
P22272 (L20-P364)
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Protein Length
Extracellular Domain
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Synonyms
IL6R; IL-6R 1; Interleukin 6 Receptor; IL-6RA; Gp80; Interleukin 6 Receptor Subunit Alpha; Interleukin-6 Receptor Subunit Alpha; IL-6R Subunit Alpha; Membrane Glycoprotein 80; IL-6R-Alpha; IL-1Ra; IL-6R-1; IL6RA; IL6QTL; IL-6R; IL6RQ; CD126; HIES5; IL-6 R
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AA Sequence
LVLGSCRALEVANGTVTSLPGATVTLICPGKEAAGNVTIHWVYSGSQNREWTTTGNTLVLRDVQLSDTGDYLCSLNDHLVGTVPLLVDVPPEEPKLSCFRKNPLVNAICEWRPSSTPSPTTKAVLFAKKINTTNGKSDFQVPCQYSQQLKSFSCQVEILEGDKVYHIVSLCVANSVGSKSSHNEAFHSLKMVQPDPPANLVVSAIPGRPRWLKVSWQHPETWDPSYYLLQFQLRYRPVWSKEFTVLLLPVAQYQCVIHDALRGVKHVVQVRGKEELDLGQWSEWSPEVTGTPWIAEPRTTPAGILWNPTQVSVEDSANHEDQYESSTEATSVLAPVQESSSMSLP
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Molecular Weight
Approximately 50-65 kDa, based on SDS-PAGE under reducing conditions.
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Glycosylation
Yes
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Purity
≥ 95%, as determined by reducing SDS-PAGE.
Product Properties
Lyophilized powder.
1.Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4.
2.Lyophilized from a 0.22 μm filtered solution of 20 mM PB, 150 mM NaCl, pH 7.4.
Please refer to the lot-specific COA for specific buffer information.
<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.
Documentation
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Data Sheet (267 KB)
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SDS (252 KB)
- English - EN (252 KB)
- Français - FR (252 KB)
- Deutsch - DE (252 KB)
- Norwegian - NO (252 KB)
- Español - ES (252 KB)
- Swedish - SV (252 KB)
- Italian - IT (252 KB)
- Korean - KR (252 KB)
- Portuguese - PT (252 KB)
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Handling Instructions (2659 KB)
References
[1]. Garbers C, et al. Inhibition of classic signaling is a novel function of soluble glycoprotein 130 (sgp130), which is controlled by the ratio of interleukin 6 and soluble interleukin 6 receptor. J Biol Chem. 2011 Dec 16;286(50):42959-70. [Content Brief]
[3]. Larsen JV, et al. SorLA in Interleukin-6 Signaling and Turnover. Mol Cell Biol. 2017 May 16;37(11):e00641-16. [Content Brief]
[4]. Kang S, et al. Targeting Interleukin-6 Signaling in Clinic. Immunity. 2019 Apr 16;50(4):1007-1023. [Content Brief]
[5]. Giannitrapani L, et al. Circulating IL-6 and sIL-6R in patients with hepatocellular carcinoma. Ann N Y Acad Sci. 2002 Jun;963:46-52. [Content Brief]
[6]. Arnold P, et al. Joint Reconstituted Signaling of the IL-6 Receptor via Extracellular Vesicles. Cells. 2020 May 24;9(5):1307. [Content Brief]
[7]. Mishra AK, et al. Metformin inhibits IL-6 signaling by decreasing IL-6R expression on multiple myeloma cells. Leukemia. 2019 Nov;33(11):2695-2709. [Content Brief]
[8]. Gruber CN, et al. Mapping Systemic Inflammation and Antibody Responses in Multisystem Inflammatory Syndrome in Children (MIS-C). Cell. 2020 Nov 12;183(4):982-995.e14. [Content Brief]
[9]. Okazaki M, et al. Characterization of anti-mouse interleukin-6 receptor antibody. Immunol Lett. 2002 Dec 3;84(3):231-40. [Content Brief]
[10]. Hirota H, Kiyama H, Kishimoto T, Taga T. Accelerated Nerve Regeneration in Mice by upregulated expression of interleukin (IL) 6 and IL-6 receptor after trauma. J Exp Med. 1996 Jun 1;183(6):2627-34. [Content Brief]
[11]. Maione D, et al. Coexpression of IL-6 and soluble IL-6R causes nodular regenerative hyperplasia and adenomas of the liver. EMBO J. 1998 Oct 1;17(19):5588-97. [Content Brief]
Calculators
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)