Recombinant Mouse Interleukin-13 (IL13) Protein (His), Active

Name: Recombinant Mouse Interleukin-13 (IL13) Protein (His), Active
Brand: Beta LifeScience
SKU: BLC-05425P
Availability: InStock

Greater than 95% as determined by SDS-PAGE.

Collections: Antibody / cell therapy targets, Antibody therapeutic / adc target proteins, Buy cytokines, chemokines, and growth factors for research online, High-purity interleukins & receptors for research, High-quality cytokines for advanced research, High-quality recombinant proteins

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Product Overview

Description	Recombinant Mouse Interleukin-13 (IL13) Protein (His), Active is produced by our Mammalian cell expression system. This is a protein fragment.
Purity	Greater than 95% as determined by SDS-PAGE.
Endotoxin	Less than 1.0 EU/μg as determined by LAL method.
Activity	The ED50 as determined in a cell proliferation assay using TF-1 human erythroleukemic cells is less than 5 ng/ml.
Uniprotkb	P20109
Target Symbol	IL13
Synonyms	Il13; Il-13; Interleukin-13; IL-13; T-cell activation protein P600
Species	Mus musculus (Mouse)
Expression System	Mammalian cell
Tag	C-6His
Complete Sequence	SVSLPLTLKELIEELSNITQDQTPLCNGSMVWSVDLAAGGFCVALDSLTNISNCNAIYRTQRILHGLCNRKAPTTVSSLPDTKIEVAHFITKLLSYTKQLFRHGPF
Expression Range	26-131aa
Protein Length	Partial
Mol. Weight	12.7 kDa
Research Area	Immunology
Form	Lyophilized powder
Buffer	Lyophilized from a 0.2 μm filtered 1xPBS, pH 7.4
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Cytokine. Inhibits inflammatory cytokine production. Synergizes with IL2 in regulating interferon-gamma synthesis. May be critical in regulating inflammatory and immune responses. Positively regulates IL31RA expression in macrophages.
Subcellular Location	Secreted.
Protein Families	IL-4/IL-13 family
Database References	KEGG: mmu:16163 STRING: 10090.ENSMUSP00000020650 UniGene: PMID: 29782549 Combined blockade of the IL-13 and IL-33 pathways leads to a greater inhibition of type 2 inflammation over inhibition of either pathway alone. PMID: 27697499 Both pre- and post-transcriptional processes may be involved in the AR modulation of ILC2 IL-5 and IL-13 production. PMID: 28982732 the endothelial barrier was preserved in respiratory epithelium isolated from MCU-/- mice after exposure to IL-13. In the ovalbumin-model of allergic airway disease, MCU deficiency resulted in decreased apoptosis within the large airway epithelial cells. Concordantly, expression of the tight junction protein ZO-1 was preserved, indicative of maintenance of epithelial barrier function PMID: 29225050 controls the rate of epithelial cell movement through the epidermis and acts as a molecular bridge between intraepithelial lymphocytes and epithelial cells PMID: 27357235 results demonstrate that IL-13 is a major regulator of radiation-induced lung injury and demonstrates that strategies focusing on IL-13 may be useful in screening for timely delivery of anti-IL-13 therapeutics. PMID: 28004808 Using a mouse model of Th2-mediated inflammation induced by OVA-allergen, this study observed elevated lung amounts of IL-13 and IL-4 accompanied by increased autophagosome levels, determined by LC3BII protein levels and immunostaining. PMID: 28982074 Metaplasia induction and macrophage polarisation after parietal cell loss is coordinated through a cytokine signalling network of IL-33 and IL-13, linking a combined response to injury by both intrinsic mucosal mechanisms and infiltrating M2 macrophages. PMID: 28196875 IL-13 is able to signal independent of the IL-4Ra chain in AD (atopic dermatitis), which may lead to the identification of molecular pathways downstream of IL-13 signaling that could be targeted in future therapies for AD. PMID: 26896776 the presence of interleukin-13 (IL-13), which can convert inflammatory into Ym1+ alternatively activated macrophages, at (acinar-to-ductal metaplasia [ADM]), which then gives rise to pancreatic intraepithelial neoplasia lesions, is reported. PMID: 28514653 Data indicate that interleukin-33 (IL-33)-induced Interleukin-13 (IL-13) production by type-2 helper T cells (Th2 cells) Is dependent on epidermal growth factor receptor (EGFR) expression. PMID: 29045902 this study shows that environmental IL-13 plays a role in conditioning early thymic progenitors lineage choice, which would impact T cell development PMID: 28893952 IL-4 and IL-13 are required to effectively polarize macrophages/dendritic cells to an M2a phenotype and to promote recovery from acute kidney injury. PMID: 27745702 this study shows that ST2 regulates early IL-13 production in fungus-induced allergic airway inflammation PMID: 26555705 These observations suggest that IL-4 and IL-13 likely operate through the Heteroreceptor and influence Th17 cells to convert to Th1 cells and to acquire increased sensitivity to suppression, leading to control of immune-mediated CNS inflammation. PMID: 28801358 MIF-deficient mice have reduced Nippostrongylus brasiliensis burden and mounted an enhanced type 2 immune response, including increased Gata3 expression and IL-13 production in the mesenteric lymph nodes PMID: 27049059 findings suggest that a leukotriene B4 receptor-2-linked cascade plays a pivotal role in LPS/TLR4 signaling for IL-13 synthesis in mast cells, thereby potentially exacerbating allergic response. PMID: 28600286 Study found IL-13 to be critically involved in the development of chemical-induced asthma, as shown by using IL-13 KO mice, and more specifically in the effector phase as confirmed by anti- IL-13 antibody treatment. PMID: 28704401 these studies show that fibrosis, steatosis, cholestasis, and ductular reaction are simultaneously controlled but distinctly regulated by interleukin-13 signaling PMID: 27421703 Our data support that impaired clearance of inhaled allergens triggering IL-13 production by multiple cell types in the airways plays an important role in the pathogenesis of type 2 airway inflammation and suggests therapeutic improvement of mucociliary clearance as a novel treatment strategy for children with allergen-induced asthma. PMID: 27865862 this study shows that wild-type mice develop an eosinophilic Th2 airway disease in response to Alternaria alternata exposure, whereas IL-13-deficient mice exhibit a primarily neutrophilic response PMID: 27815425 this study shows that IL-17A contributes to asthma pathophysiology by increasing the capacity of IL-13 to activate intracellular signaling pathways, such as STAT6 activation PMID: 27417023 RCM-1 reduced IL-13 and STAT6 (signal transducer and activator of transcription 6) signaling and prevented the expression of the STAT6 target genes Spdef and Foxa3, which are key transcriptional regulators of goblet cell differentiation. PMID: 28420758 IL-13 suppressed both the activation-induced apoptosis of CD4(+) T cells and the expression of p53 and FasL. PMID: 26189367 We clearly show that miR-155 has a previously unknown direct regulatory role in the ILC2 subset that affects IL-33 receptor expression, IL-33 responsiveness, and IL-13 production as well as proliferation capability, possibly due to defects in GATA-3 function. PMID: 27492144 The presented data substantiate the hypothesis that claudin-18 is a central barrier-forming component of tight junctions and show that IL-13 downregulates claudin-18. These data also suggest that the loss of claudin-18 is associated with increased sensitization to aeroantigens and airway responsiveness PMID: 27215490 Studies in colonic T84 cell monolayers revealed that barrier disruption by the colitis-associated Th2-type cytokines, IL-4 and IL-13, down-regulates matriptase as well as prostasin through phosphorylation of the transcriptional regulator STAT6 PMID: 28490634 These data demonstrate that multiple pathogenic strains of RSV induce IL-13-producing group 2 innate lymphoid cell proliferation and activation through a TSLP-dependent mechanism in a murine model and suggest the potential therapeutic targeting of TSLP during severe RSV infection. PMID: 27156176 The soluble antigen from A. cantonensis could promote the Chil3 expression in macrophage and microglial cell lines induced by interleukin-13. PMID: 27256220 The reduction in fibrosis observed when IL-13 signalling is suppressed is not dependent on increased IFN-gamma activity. Instead, by reducing compensatory increases in type 1-associated inflammation, therapeutic strategies that block IFN-gamma and IL-13 activity simultaneously can confer greater protection from progressive fibrosis than IL-13 blockade alone. PMID: 27125685 The IL-23/IL-17 axis plays a critical role in the immunopathology of hepatic amebiasis. IL-13 secreted by CD11b(+)Ly6C(lo) monocytes may be associated with recovery from liver damage. PMID: 26809113 PLD1 activation enhanced binding of ROCK1 to ATF-2 and leads to increased expression of IL-13 PMID: 26335962 Macrophages are critical to the maintenance of IL-13-dependent lung inflammation and fibrosis. PMID: 25921340 IL-25 and CD4(+) TH2 cells enhance type 2 innate lymphoid cell-derived IL-13 production, which promotes IgE-mediated experimental food allergy. PMID: 26560039 Placenta growth factor augments airway hyperresponsiveness via leukotrienes and IL-13. PMID: 26690703 Natural helper cells contribute to pulmonary eosinophilia by producing IL-13 via IL-33/ST2 pathway in a murine model of respiratory syncytial virus infection PMID: 26044350 review of IL-4 and IL-13 mast cell immunity and detail of the differences that exist between mouse and human mast cell responses to IL-4 and IL-13 [review] PMID: 26088754 Data (including data from studies in knockout/transgenic mice) suggest T cell-derived IL4/IL13 are required for immunologic memory and IgE response to helminth Nippostrongylus brasiliensis but are not required for expansion/proliferation of B cells. PMID: 26523376 Curcumin up-regulates mRNA and protein levels of IL-4 and IL-13 PMID: 25944087 These data indicate that distal airways might be less sensitive to IL-13-induced GC metaplasia and mucus production through lower expression of IL-13Ralpha1 and attenuated activation of downstream signalling. PMID: 25772331 IL-13 induces miR-142-5p and downregulates miR-130a-3p in macrophages, regulating macrophage profibrogenic gene expression in chronic inflammation. PMID: 26436920 IL-4 and IL-13 have a critical role in innate immune cells for protective immunity against gastrointestinal helminths. PMID: 25336167 These data demonstrate that dysregulated IL-25 expression contributes to lipid accumulation, whereas exogenous IL-25 protects against hepatic steatosis through IL-13 activation of STAT6. PMID: 26423151 TH2 cells and their cytokines IL-4 and IL-13 regulate formation and function of lymphatic vessels. PMID: 25648335 Mice with experimental Schistosoma-induced pulmonary hypertension (PH) had evidence of increased IL-4 and IL-13 signaling. IL-4(-/-)IL-13(-/-) mice, but not single knockout IL-4(-/-) or IL-13(-/-) mice, were protected from Schistosoma-induced PH. PMID: 26192556 regulates the expression of IL-17A in HIV-specific CD8 T cells following immunizations PMID: 25493691 These data establish for the first time a molecular mechanism by which Mac-1 regulates the signaling activity of IL-13 in macrophages. PMID: 26160172 Acidic pH augments Fc-epsilon-RI-mediated production of IL-6 and IL-13 in mast cells. PMID: 26196745 conjunctival goblet cells are IL-13 responsive cells that produce factors known to maintain epithelial barrier, stimulate mucin production, and modulate immune response in nonocular mucosa when treated with IL-13. PMID: 26132778 Enhanced IL-13 production by T cells can play a causative role in the exocrinopathy observed in Id3 knockout mice. PMID: 25010390

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.