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Recombinant Human Interleukin-11 (IL11)
(Cat. No.: C006)
Background:
IL-11 is a thrombopoietic growth factor that directly stimulates the proliferation of hematopoietic stem cells and megakaryocyte progenitor cells and induces megakaryocyte maturation resulting in increased platelet production. IL-11 is a member of a family of human growth factors which includes human growth hormone, granulocyte colony-stimulating factor and other growth factors.
Description:
The protein is produced in P. Pichia by recombinant DNA technology. The protein has a molecular mass of approximately 19,000 Daltons and is non-glycosylated. The protein is 177 amino acids in length and differs from the 178 amino acid length of native IL-11 only in lacking the amino-terminal praline residue.
Quality Control:
Biological activity: The ED50 as determined by the dose-dependant stimulation of the proliferation of murine 7TD1 was found to be less then 0.2ng/ml, corresponding to a Specific Activity of 8.0 x 106 IU/ mg.
Purity: Greater than 95% as determined by
(a) Analysis by SEC-HPLC.
(b) Analysis by reducing and non-reducing SDS-PAGE Silver Stained gel.
Molecular weight: 19.2KD+/-10% determined by reduced SDS-PAGE.
Isoelectric Point: More than 11
UV scan: the maximal absorption wave is 278+/-3nm.
Amino-Acid Sequence: The sequence of the first fifteen N-terminal amino acids was determined and was found to be Gly-Pro-Pro-Pro-Gly-Pro-Pro-Arg-Val-Ser-Pro-Asp-Pro- Arg-Ala.
Residual DNA: less than 2ng/mg analysis by solid phase blot.
Residual host cell protein: less than 0.1% analysis by ELISA.
Endotoxin: Less than 2ng/mg (2IEU/mg) determined by LAL test.
Formulation: The protein was lyophilized from a concentrated (1mg/ml) solution with no additives.
Storage: Lyophilized rHuIL-11 although stable at room temperature for 3 weeks, should be stored desiccated below -18oC. Upon reconstitution rHuIL-11 should be stored at 4oC between 2-7 days and for future use below -18oC. For long-term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please avoid freeze-thaw cycles.
Reconstitution: It is recommended to reconstitute the lyophilized rHuIL-11 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Latest Publications:
1: Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi 2009
Jan;Vol 25(1)
[Jak/STAT signaling pathway of IL-11 in the protection of intestinal epithelial cells from neutron radiation.]
[Abstract] AIM: To explore the effect of IL-11 on the activation of Jak/STAT pathway and the expressions of Bax and Bcl-2 in the intestinal epithelial cells exposed to neutron radiation. METHODS: The BALB/c mice and IEC-6, irradiated by 4 Gy neutron with or without IL-11 treatment, served as in vivo and in vitro model seperately. The changes of the intestines, activity of Jak1 and STAT3 and expressions of Bax and Bcl-2 were observed by HE staining, Western blot, EMSA, immunohistochemistry and image analysis. RESULTS: (1)Mice exposed to neutron radiation showed severe intestinal damages and no obvious regeneration was seen. IL-11-treated mice had a larger number of cryptal epithelial cells and crypts. (2)Neutron radiation decreased the activities of Jak1 and STAT3, while
IL-11 increased their activities. (3) Neutron radiation decreased the expression of Bax and didn't change the level of Bcl-2 in the murine intestine. IL-11 administration decreased the expression of Bax and increased that of Bcl-2. CONCLUSION: The mechanism of the intestinal protection of IL-11 in neutron irradiation might be that IL-11 stimulation triggered activation of Jak/STAT pathway, downregulated the expression of Bax and upregulated the expression of Bcl-2.
2: Oral Dis 2009 Jan;Vol 15(1)
The impact of the IL-11:IL-17 ratio on the chronic periodontitis pathogenesis: a preliminary report.
[Abstract] OBJECTIVE: An imbalance in the pro- and anti-inflammatory cytokines may be responsible for periodontal breakdown through immune responses. This study aimed to determine the total amount, concentration and ratio of interleukin (IL)-11 and IL-17 in gingival crevicular fluid (GCF) of chronic periodontitis (CP) patients. MATERIALS AND METHODS: Forty CP patients and 20 healthy controls (C) were included. The CP group was divided into two subgroups in line with the probing depth (PD) in GCF-sampling sites (CPa: PD >or= 5 mm, CPb: PD <or= 4 mm). For each patient, gingival index, plaque index, gingival bleeding time index, PD, and clinical attachment level values were recorded. IL-11 and IL-17 in GCF were evaluated by enzyme-linked immunosorbent assays. RESULTS: The
total amount and concentration of IL-11 and IL-17 were significantly lower in the CPa group (P < 0.05). The C group has the highest IL-11:IL-17 ratio, followed by CPb and CPa groups respectively. The ratio was significantly lower in CPa group than the CPb and C groups (P < 0.01). CONCLUSION: Our data confirm that the decreased ratio of IL-11:IL-17 may be a factor, which has shown this imbalance between the cytokines' activities in deeper pockets in our study.
3: Am J Respir Cell Mol Biol 2008
Dec;Vol 39(6)
Endogenous IL-11 signaling is essential in Th2- and IL-13-induced inflammation and mucus production.
[Abstract] IL-11 and IL-11 receptor (R)alpha are induced by Th2 cytokines. However, the role(s) of endogenous IL-11 in antigen-induced Th2 inflammation has not been fully defined. We hypothesized that IL-11, signaling via IL-11Ralpha, plays an important role in aeroallergen-induced Th2 inflammation and mucus metaplasia. To test this hypothesis, we compared the responses induced by the aeroallergen ovalbumin (OVA) in wild-type (WT) and IL-11Ralpha-null mutant mice. We also generated and defined the effects of an antagonistic IL-11 mutein on pulmonary Th2 responses. Increased levels of IgE, eosinophilic tissue and bronchoalveolar lavage (BAL) inflammation, IL-13 production, and increased mucus production and secretion were noted in OVA-sensitized and -challenged WT mice.
These responses were at least partially IL-11 dependent because each was decreased in mice with null mutations of IL-11Ralpha. Importantly, the administration of the IL-11 mutein to OVA-sensitized mice before aerosol antigen challenge also caused a significant decrease in OVA-induced inflammation, mucus responses, and IL-13 production. Intraperitoneal administration of the mutein to lung-specific IL-13-overexpressing transgenic mice also reduced BAL inflammation and airway mucus elaboration. These studies demonstrate that endogenous IL-11R signaling plays an important role in antigen-induced sensitization, eosinophilic inflammation, and airway mucus production. They also demonstrate that Th2 and IL-13 responses can be regulated by interventions that manipulate IL-11 signaling in the murine
lung.
4: J Clin Invest 2008
May;Vol 118(5)
STAT3 and STAT1 mediate IL-11-dependent and inflammation-associated gastric tumorigenesis in gp130 receptor mutant mice.
[Abstract] Deregulated activation of STAT3 is frequently associated with many human hematological and epithelial malignancies, including gastric cancer. While exaggerated STAT3 signaling facilitates an antiapoptotic, proangiogenic, and proproliferative environment for neoplastic cells, the molecular mechanisms leading to STAT3 hyperactivation remain poorly understood. Using the gp130(Y757F/Y757F) mouse model of gastric cancer, which carries a mutated gp130 cytokine receptor signaling subunit that cannot bind the negative regulator of cytokine signaling SOCS3 and is characterized by hyperactivation of the signaling molecules STAT1 and STAT3, we have provided genetic evidence that IL-11 promotes chronic gastric inflammation and associated tumorigenesis. Expression of IL-11
was increased in gastric tumors in gp130(Y757F/Y757F) mice, when compared with unaffected gastric tissue in wild-type mice, while gp130(Y757F/Y757F) mice lacking the IL-11 ligand-binding receptor subunit (IL-11Ralpha) showed normal gastric STAT3 activation and IL-11 expression and failed to develop gastric tumors. Furthermore, reducing STAT3 activity in gp130(Y757F/Y757F) mice, either genetically or by therapeutic administration of STAT3 antisense oligonucleotides, normalized gastric IL-11 expression and alleviated gastric tumor burden. Surprisingly, the genetic reduction of STAT1 expression also reduced gastric tumorigenesis in gp130(Y757F/Y757F) mice and coincided with reduced gastric inflammation and IL-11 expression. Collectively, our data have identified IL-11 as a crucial cytokine
promoting chronic gastric inflammation and associated tumorigenesis mediated by excessive activation of STAT3 and STAT1.
Domain Info
GeneBank Entry:
NM_000641
Protein Accession No.:
NP_000632
Protein Sequence:
GPPPG PPRVS PDPRA ELDST VLLTR SLLAD TRQLA AQLRD KFPAD GDHNL DSLPT LAMSA GALGA LQLPG VLTRL RADLL SYLRH VQWLR RAGGS SLKTL EPELG TLQAR LDRLL RRLQL LMSRL ALPQP PPDPP APPLA PPSSA WGGIR AAHAI LGGLH LTLDW AVRGL LLLKT RL
Transcript Info
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*NOTE: ALL PRODUCTS ARE FOR RESEARCH USE ONLY |
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