Recombinant Human Interleukin-22 Receptor Subunit Alpha-1 (IL22RA1) Protein (His-SUMO)

Name: Recombinant Human Interleukin-22 Receptor Subunit Alpha-1 (IL22RA1) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-10103P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: Cytokines, Cytokines and growth factors, Interleukins and receptors, Recombinant proteins

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Product Overview

Description	Recombinant Human Interleukin-22 Receptor Subunit Alpha-1 (IL22RA1) Protein (His-SUMO) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q8N6P7
Target Symbol	IL22RA1
Synonyms	CRF2 9; CRF2-9; Cytokine receptor class-II member 9; cytokine receptor classII member 9; Cytokine receptor family 2 member 9; I22R1_HUMAN; IL-22 receptor subunit alpha-1; IL-22R-alpha-1; IL-22RA1; IL22 Receptor Alpha; IL22R; IL22R1; Il22ra1; ILTIF R1 chain; Interleukin 22 Receptor alpha 1; Interleukin 22 Receptor; Interleukin-22 receptor subunit alpha-1; ZcytoR11
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	SYRYVTKPPAPPNSLNVQRVLTFQPLRFIQEHVLIPVFDLSGPSSLAQPVQYSQIRVSGPREPAGAPQRHSLSEITYLGQPDISILQPSNVPPPQILSPLSYAPNAAPEVGPPSYAPQVTPEAQFPFYAPQAISKVQPSSYAPQATPDSWPPSYGVCMEGSGKDSPTGTLSSPKHLRPKGQLQKEPPAGSCMLGGLSLQEVTSLAMEESQEAKSLHQPLGICTDRTSDPNVLHSGEEGTPQYLKGQLPLLSSVQIEGHPMSLPLQPPSRPCSPSDQGPSPWGLLESLVCPKDEAKSPAPETSDLEQPTELDSLFRGLALTVQWE
Expression Range	250-573aa
Protein Length	Partial
Mol. Weight	50.8kDa
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	Component of the receptor for IL20, IL22 and IL24. Component of IL22 receptor formed by IL22RA1 and IL10RB enabling IL22 signaling via JAK/STAT pathways. IL22 also induces activation of MAPK1/MAPK3 and Akt kinases pathways. Component of one of the receptor for IL20 and IL24 formed by IL22RA1 and IL20RB also signaling through STATs activation. Mediates IL24 antiangiogenic activity as well as IL24 inhibitory effect on endothelial cell tube formation and differentiation.
Subcellular Location	Membrane; Single-pass type I membrane protein.
Protein Families	Type II cytokine receptor family
Database References	HGNC: 13700 OMIM: 605457 KEGG: hsa:58985 STRING: 9606.ENSP00000270800 UniGene: Hs.110915
Tissue Specificity	Expressed in colon, liver, lung, pancreas and kidney. No expression in immune cells such as monocytes, T-cells, and NK-cells. Expressed in keratinocytes of normal skin as well as in psoriatic skin lesion. Detected in normal blood brain barrier endothelial

Gene Functions References

increased expression of IL-22Ralpha therefore promotes keratinocyte proliferation and pro-inflammatory cytokine production during UVB-induced skin inflammation, suggesting that UVB facilitates skin inflammation by increasing the responsiveness of keratinocytes to IL-22 PMID: 28558005
IL-22 and its receptor have a crucial role in the development and pathogenesis of uveitis by facilitating inflammatory cell infiltration. PMID: 27166675
high expression profile of IL-22R1 in nonsmall cell lung cancer is an independent indicator of poor overall survival PMID: 26846835
phosphorylation of STAT3 and AKT was highly induced by treatment with IL-22 via IL-22R1. IL-22R1 was also consistently overexpressed in recurrent NSCLC tissues PMID: 26983629
These data suggest that imbalance of IL-22/IL-22R1 signaling regulates the pathogenesis of chronic rhinosinusitis with nasal polyps, including local eosinophilia, via alteration of MUC1 expression. PMID: 27502468
FBXW12 functions as an E3 ligase constituent to ubiquitinate and degrade IL-22R and that therapeutic FBXW12 inhibition may enhance IL-22 signaling and bolster mucosal host defense and infection containment. PMID: 26171402
IL-22R1 is over-expressed in primary Sjogren's syndrome and Sjogren-associated non-Hodgkin lymphomas and is regulated by IL-18. PMID: 25880879
IL-22 has restricted tissue specificity as its unique receptor IL-22R1 is exclusively expressed on epithelial and tissue cells, but not immune cells. PMID: 24856143
serum IL-22 levels are significantly higher in patients with pituitary macroadenomas than in healthy controls and IL-22R is variably expressed in both prolactinoma and non-functioing pituitary adenoma cells. PMID: 23512698
High expression of interleukin-22 receptor is associated with pancreatic ductal adenocarcinoma. PMID: 24132627
the CC genotype of rs3795299 polymorphism in the IL-22R1 gene is associated with the reduced risk of IgAN, and this genetic association was supported by the higher renal expression of IL-22R1 in healthy controls compared with patients with IgAN. PMID: 23659670
Letter: calcipotriol inhibits the IL-22-induced epidermal hyperplasia by decreasing keratinocyte proliferation and down-modulating IL-22R expression. PMID: 23688404
Data show that IL-17RA, IL-17RC, IL-22R1, ERK1/2 MAPK and NF-kappaB pathways are involved in Th17 cytokine-induced proliferation. PMID: 22898922
IL-22R1 mRNA and protein expressions in HASMCs were significantly increased after stimulation by serum from asthmatic patients, but decreased after co-stimulation with dexamethasone. PMID: 21690049
This study documents a previously unknown role of IL-22R1 in inflammation and identifies the involvement of IL-22R1/IL-22 in anaplastic lymphoma kinase-positive anaplastic large cell lymphoma PMID: 20971950
Tyr251 and Tyr301 of IL-22R1 are required for Shp2 binding and IL-22-induced Erk1/2 activation. PMID: 20671117
study demonstrated IL-22R1 mRNA and protein expression on nasal epithelial cells; failure of medical and surgical therapy in chronic rhinosinusitis with nasal polyps is associated with significantly decreased expression of IL-22R1 PMID: 17906500
The islets of Langerhans are the local site for IL-22R1 expression in the human pancreas. PMID: 18376313
Molecular basis for the distinct affinities and specificities of IL-22 and IL-10 receptor chains that regulate cellular targeting and signal transduction to elicit effective immune responses. PMID: 18599299
A 1.9A crystal structure of the IL-22/IL-22R1 complex is reported. PMID: 18675809
identifies those amino acid side chains of IL-22 that are individually important for optimal binding to IL-22R PMID: 18675824
Comparison of IL-22/IL-22BP and IL-22/IL-22R1 crystal structures shows that both receptors display an overlapping IL-22 binding surface, which is consistent with the inhibitory role played by IL-22 binding protein. PMID: 19285080
Data show that deletion of the C-terminal part of IL-22R dramatically decreased its ability to activate STAT3. PMID: 19632985
Increased IL-22R expression in epidermal keratinocytes contributes to the pathogenesis of psoriasis through enhancing the coordinated effects of IL-22 and IL-17, inducing the production of the IL-20 subfamily, chemokines, and growth factors. PMID: 19731362

FAQs

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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.