Recombinant Mouse Interleukin-23 Subunit Alpha (IL23A) Protein (His)

Name: Recombinant Mouse Interleukin-23 Subunit Alpha (IL23A) Protein (His)
Brand: Beta LifeScience
SKU: BLC-08722P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: Antibody / cell therapy targets, Antibody therapeutic / adc target proteins, Cytokines, Cytokines and growth factors, Interleukins and receptors, Recombinant proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Mouse Interleukin-23 Subunit Alpha (IL23A) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9EQ14
Target Symbol	IL23A
Synonyms	Il23a; Interleukin-23 subunit alpha; IL-23 subunit alpha; IL-23-A; Interleukin-23 subunit p19; IL-23p19
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	VPRSSSPDWAQCQQLSRNLCMLAWNAHAPAGHMNLLREEEDEETKNNVPRIQCEDGCDPQGLKDNSQFCLQRIRQGLAFYKHLLDSDIFKGEPALLPDSPMEQLHTSLLGLSQLLQPEDHPRETQQMPSLSSSQQWQRPLLRSKILRSLQAFLAIAARVFAHGAATLTEPLVPTA
Expression Range	22-196
Protein Length	Partial
Mol. Weight	23.7kDa
Research Area	Immunology
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
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	Associates with IL12B to form the IL-23 interleukin, a heterodimeric cytokine which functions in innate and adaptive immunity. IL-23 may constitute with IL-17 an acute response to infection in peripheral tissues. IL-23 binds to a heterodimeric receptor complex composed of IL12RB1 and IL23R, activates the Jak-Stat signaling cascade, stimulates memory rather than naive T-cells and promotes production of proinflammatory cytokines. IL-23 induces autoimmune inflammation and thus may be responsible for autoimmune inflammatory diseases and may be important for tumorigenesis.
Subcellular Location	Secreted. Note=Secreted upon association with IL12B.
Protein Families	IL-6 superfamily
Database References	KEGG: mmu:83430 STRING: 10090.ENSMUSP00000026449 UniGene: Mm.125482
Tissue Specificity	Secreted by activated dendritic cells (at protein level). Detected in various tissues with higher expression in polarized Th1 cells and activated macrophages.

Gene Functions References

JunB has an essential role in IL-23-dependent pathogenicity of Th17 cells PMID: 28555647
HO-1 enhanced STAT3 phosphorylation, which enriched to Il12b and Il23a loci and negatively regulated their transcription. These findings demonstrate the underlying mechanism through which a nutritional can interfere with the immune response. CUR silences IL-23/Th17-mediated pathology by enhancing HO-1/STAT3 interaction in dendritic cells. PMID: 28290522
This study defines a critical IL-36/IL-23/IL-22 cytokine network instrumental for antimicrobial peptide production and host defense in intestinal mucosa damage using a mouse inflammatory bowel disease model. PMID: 29760082
IL-23 drives differentiation of peripheral gamma-delta 17 T cells from adult bone marrow-derived precursors. PMID: 28855306
In mice on a C57BL/6 background, neither IL-23p19 nor IL-17A plays a role for immune protection against L. major in the physiological context of natural infections. PMID: 27297018
The hormone levels are significantly reduced and lymphocytic infiltration in the lacrimal gland in ovariectomized mice, whereas the frequency of Th17 cells in the blood and spleen and IL-17A and IL-23 expression in the lacrimal glands are increased, leading to reduced tear production and positive fluorescein staining in the cornea. PMID: 27341090
this study unveiled the role of IL-23-dependent IL-17 induction in LdCen-/- parasite-induced immunity and subsequent protection against visceral leishmaniasis PMID: 29187586
Results reveal the importance of the IL-23/IL-17 inflammatory axis in secondary brain injury after intracerebral hemorrhage. PMID: 27729335
RIG-I expression is markedly increased in the affected skin derived from psoriasis patients and from both IL-23- and imiquimod -induced psoriasis-like mouse model. PMID: 28377495
results show that IL-23 accounts for the main aspects of human and murine lupus including the expansion of double negative T cells, decreased IL-2, and increased IL-17 production PMID: 28646040
this study shows that IL-23 but not IL-1 contributes to the IL-17A expression induced by subacute O3 exposure PMID: 27043160
IL-23 released by keratinocytes in response to endogenous TLR4 ligands causes skin DCs, which selectively express IL-23R, to up-regulate their endogenous IL-23 production and drive an IL-22 response in naive CD4(+) T cells that mediates epidermal thickening. PMID: 27551155
In mice overexpressing IL23, enthesis-resident gamma/delta T cells accumulate in the enthesis, ciliary body, and aortic valve. PMID: 27111864
we describe here a new IL-12 member IL-39 (IL-23p19/Ebi3) secreted by activated B cells that mediate inflammatory responses in lupus-like mice. Thus, IL-39 might contribute to immunopathogenic mechanisms of SLE. PMID: 27019190
These data identify the important contributions of IL-23 to the development of elastase-induced pulmonary inflammation and emphysema. PMID: 27351934
The inflammatory phenotype in barrier-defective skin is shaped by counterregulation between the TSLP/type 2 and IL-23/type 17 axes. PMID: 26993035
IL-23 is another important bronchial epithelial cell-driven cytokine which may contribute to the development of house dust mite allergic sensitization and asthma. PMID: 27864285
this study shows that elevated iserum IL-23 is associated with mortality in lipopolysaccharide/d-galactosamine -induced acute liver injury, and that IL-23 neutralizing antibodies attenuated liver injury by reducing the expression of Th17-related inflammatory cytokines, neutrophil chemoattractants and stabilization factors within the liver tissue PMID: 28282579
IL-23 is a considerable molecular in tumor progression, which simultaneously facilitates processes of pro-tumor inflammation, such as angiogenesis, immunosuppressive cytokines as well as infiltrations of M2 macrophages and neutrophils, and suppresses antitumor immune responses through reduction of CD4(+) T cells and CD8(+) T cells PMID: 27956175
this study shows that that IL-23 signaling is required for monocyte recruitment during Clostridium difficile colitis PMID: 27995603
data suggest that systemic IL-23/STAT3 axis is responsible for enhanced airway inflammation during psoriasis PMID: 27984001
this study shows that madecassoside ointment ameliorates imiquimod-induced skin inflammation and abnormal keratinocyte proliferation by regulating the IL-23/IL-17 axis PMID: 27540765
this study shows that IL-18, cooperatively with IL-23, induced prominent inflammation and enhanced psoriasis-like epidermal hyperplasia PMID: 28299442
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
CD11c(+) monocyte/macrophages promote chronic Helicobacter hepaticus-induced intestinal inflammation through the production of IL-23. PMID: 26242598
These results suggest that Il23a expression in DCs is synergistically triggered by the PG E2-EP4-cAMP-PKA pathway and canonical/non-canonical NF-kappaB pathways and CREB activated by CD40 stimulation. PMID: 26189370
IL-23-induced GM-CSF mediates the pathogenicity of CD4(+) T cells in experimental autoimmune myocarditis. PMID: 26660726
Endogenous IL-23 production at the site of antigen sensitization facilitates type-2 immune responses, whereas IL-23 production and subsequent IL-17A synthesis in the airways suppresses allergic inflammation. PMID: 26344076
IL-23, but not IL-17a or IL-22, promotes neutrophil recruitment and inflammatory cytokine and chemokine expression in the colon in response to C. difficile infection. PMID: 26455347
IL-23/IL-1/IFNgamma/TNFalpha/T-bet/Eomesodermin-driven circuit drives GM-CSF/IFNgamma-producing Th17 cell development PMID: 26511769
This study showed thatIL-23 is significantly increased in infected mice with a myeloid cell-specific deletion of IL-10, and the addition of IL-10 reduces IL-23 production by intestinal macrophages. PMID: 25959063
Both IL-23 and isolated lymphoid follicles are associated with inflammatory bowel disease, suggesting that disruption to this pathway may have an important role in the breakdown of microbiota-immune homeostasis. PMID: 25249168
The data define a novel pathway that is used by IL-23 in myeloid cells and identify a major mechanism for the stimulation of osteoclastogenesis in inflammatory arthritis. PMID: 25452564
IL-23-mediated mononuclear phagocyte crosstalk protects mice from Citrobacter rodentium-induced colon immunopathology. PMID: 25761673
p19 inhibition decreased IL-17A+IFN-g+ double-positive T cells in the colon to almost naive quantities. PMID: 26431947
Data indicate that sensory neurons directly sense Candida albicans and augment interleukin 23 (IL-23) production. PMID: 26377898
Results confirm that IL-23p19 gene knockdown efficiently suppresses the IL-23/IL-17 axis, decreases the IL-17/IFN-gamma ratio and promotes Foxp3 expression, eventually improving the outcomes of later cerebral ischemia PMID: 25637493
Data show the contribution of IL-23/IL-23 receptor and IL-7/IL-7 receptor signaling in Th17 and Th1 cell dynamics during experimental autoimmune encephalomyelitis (EAE). PMID: 26223651
that IL-23, but not IL-17 is crucial for the development of OVA-induced AR PMID: 26239416
Study provides evidence that IL-23/IL-23R plays a critical role in brain ischemic injury PMID: 25600958
Interleukin-23 production by the thymic dendritic cells promotes apoptosis of the CD4(hi)CD8(hi) double-positive thymocytes. PMID: 25001511
Our results reveal a novel role for the IL-23-ILC3s axis in the pathogenesis of neonatal intestinal inflammation. PMID: 25160819
Results suggest that increased activation of the IL-23/IL-17 pathway has detrimental effects on sepsis-induced lung inflammation. PMID: 24978886
the role of IL-23 in Francisella tularensis LVS resistance PMID: 25296161
Knocking down the expression of MMP2 in melanoma cells resulted in inhibition of IL-23-induced invasiveness PMID: 25639230
Expression of the p19 and p40 subunits of IL-23, a c-Rel-dependent cytokine, was enhanced in p100-deficient cells, although expression of a RelA-dependent cytokine, TNF-alpha, was reduced PMID: 25305492
The action of GM-CSF that promotes advanced plaque progression is mediated by interleukin-23-inducing activity. PMID: 25348165
The IL-23 was required for the development of a Chlamydia-specific Th17 response in the lymph nodes and for production of IL-22 and IL-17 in the genital tract. PMID: 24238108
suggest that Hmgb1-IL-23-IL-17-IL-6-Stat3 axis plays a pivotal role in tumor development in murine models of melanoma PMID: 24453427
In response to systemic beta-1,3-glucan, intestinal IL-23 provokes local mucosal dysregulation and cytokines driving the spondyloarthritis syndrome, including IL-17/IL-22-dependent enthesitis. PMID: 24664521

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.