Recombinant Human Receptor-Interacting Serine/Threonine-Protein Kinase 2 (RIPK2) Protein (His)

Name: Recombinant Human Receptor-Interacting Serine/Threonine-Protein Kinase 2 (RIPK2) Protein (His)
Brand: Beta LifeScience
SKU: BLC-06460P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Receptor-Interacting Serine/Threonine-Protein Kinase 2 (RIPK2) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	O43353
Target Symbol	RIPK2
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	C-6His
Target Protein Sequence	MNGEAICSALPTIPYHKLADLRYLSRGASGTVSSARHADWRVQVAVKHLHIHTPLLDSERKDVLREAEILHKARFSYILPILGICNEPEFLGIVTEYMPNGSLNELLHRKTEYPDVAWPLRFRILHEIALGVNYLHNMTPPLLHHDLKTQNILLDNEFHVKIADFGLSKWRMMSLSQSRSSKSAPEGGTIIYMPPENYEPGQKSRASIKHDIYSYAVITWEVLSRKQPFEDVTNPLQIMYSVSQGHRPVINEESLPYDIPHRARMISLIESGWAQNPDERPSFLKCLIELEPVLRTFEEITFLEAVIQLKKTKLQSVSSAIHLCDKKKMELSLNIPVNHGPQEESCGSSQLHENSGSPETSRSLPAPQDNDFLSRKAQDCYFMKLHHCPGNHSWDSTISGSQRAAFCDHKTTPCSSAIINPLSTAGNSERLQPGIAQQWIQSKREDIVNQMTEACLNQSLDALLSRDLIMKEDYELVSTKPTRTSKVRQLLDTTDIQGEEFAKVIVQKLKDNKQMGLQPYPEILVVSRSPSLNLLQNKSM
Expression Range	1-540aa
Protein Length	Full Length
Mol. Weight	62.0 kDa
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	Serine/threonine/tyrosine kinase that plays an essential role in modulation of innate and adaptive immune responses. Upon stimulation by bacterial peptidoglycans, NOD1 and NOD2 are activated, oligomerize and recruit RIPK2 through CARD-CARD domains. Contributes to the tyrosine phosphorylation of the guanine exchange factor ARHGEF2 through Src tyrosine kinase leading to NF-kappaB activation by NOD2. Once recruited, RIPK2 autophosphorylates and undergoes 'Lys-63'-linked polyubiquitination by E3 ubiquitin ligases XIAP, BIRC2 and BIRC3. The polyubiquitinated protein mediates the recruitment of MAP3K7/TAK1 to IKBKG/NEMO and induces 'Lys-63'-linked polyubiquitination of IKBKG/NEMO and subsequent activation of IKBKB/IKKB. In turn, NF-kappa-B is released from NF-kappa-B inhibitors and translocates into the nucleus where it activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis. Plays also a role during engagement of the T-cell receptor (TCR) in promoting BCL10 phosphorylation and subsequent NF-kappa-B activation. Plays a role in the inactivation of RHOA in response to NGFR signaling.
Subcellular Location	Cytoplasm.
Protein Families	Protein kinase superfamily, TKL Ser/Thr protein kinase family
Database References	HGNC: 10020 OMIM: 603455 KEGG: hsa:8767 STRING: 9606.ENSP00000220751 UniGene: PMID: 30332343 Nine compounds from the ZINC database show satisfactory results, yielding among those selected, the compound ZINC01540228, as the most promising RIPK2 inhibitor. After binding free energy calculations, the following molecular dynamics simulations showed that the receptor protein's backbone remained stable after the introduction of ligands. PMID: 30088101 Results showed that the expressions of RIP2 and BclxL were positively correlated with the malignant grade of astrocytoma. RIP2 promoted human glioblastoma cell proliferation by inducing expression of BclxL. PMID: 29693188 Together, these data show that RIP2 promotes survival of breast cancer cells through NF-kappaB activation and that targeting RIP2 may be therapeutically beneficial for treatment of TNBC. PMID: 29421659 RIP2 kinase auto-phosphorylation is intimately coupled to dimerization. PMID: 28545134 study provides structural and dynamic insights into the NOD1-RIP2 oligomer formation, which will be crucial in understanding the molecular basis of NOD1-mediated CARD-CARD interaction in higher and lower eukaryotes PMID: 28114344 a new function of PAX5 in regulating RIP1 and RIP2 activation, which is at least involved in chemotherapeutic drug resistance in B-lymphoproliferative disorders, is reported. PMID: 27122187 this study reveals that LRRK2 is a new positive regulator of Rip2 and promotes inflammatory cytokine induction through the Nod1/2-Rip2 pathway. PMID: 27830463 Data indicate that receptor-interacting protein 2 (Rip2) polymorphisms are associated with increased risk of subclinical atherosclerosis (SA) and with some clinical and metabolic parameters. PMID: 27939575 Together, the data demonstrate that the NOD2-RIP2 pathway is activated in murine and human visceral leishmaniasis and plays a role in shaping adaptive immunity toward a Th1 profile. PMID: 27651416 RIP2 and RhoGDI bind to p75(NTR) death domain at partially overlapping epitopes with over 100-fold difference in affinity, revealing the mechanism by which RIP2 recruitment displaces RhoGDI upon ligand binding. PMID: 26646181 that Rip2 modifies VEGF-induced signalling and vascular permeability in myocardial ischaemia PMID: 26130752 up-regulated in failing hearts PMID: 26463597 NOD2 downregulates colonic inflammation by IRF4-mediated inhibition of K63-linked polyubiquitination of RICK and TRAF6. PMID: 24670424 RIP2 protein, human is involved in human colon tumorigenesis and could be a predictive marker for colon carcinoma progression PMID: 25374171 Data indicate that receptor-interacting protein kinase 2 (RIP2) is an activator of the NF-kappa B and c-Jun N-terminal kinase pathways. PMID: 24642040 NOD1 and RIP2 interact with bacterial peptidoglycan on endosomes to promote autophagy and inflammatory signaling. PMID: 24746552 the NOD1-RIP2 signaling axis is more complex than previously assumed, that simple engagement of RIP2 is insufficient to mediate signaling PMID: 24958724 Receptor interacting protein-2 plays a critical role in human lung epithelial cells survival in response to Fas-induced cell-death. PMID: 24658576 The Nod1/2-Rip2 axis was critical to induce optimal cytokine and chemokine responses to A. baumannii infection. PMID: 24366254 LRRK2 and RIPK2 variants in the NOD 2-mediated signaling pathway are associated with susceptibility to Mycobacterium leprae in Indian populations. PMID: 24015287 Our findings identify RIP2 as a substrate for Pellino3 and Pellino3 as an important mediator in the Nod2 pathway and regulator of intestinal inflammation. PMID: 23892723 In an attempt to explore TRAF3 binding partners that may be involved in TRAF3-regulated signaling, a yeast two-hybrid screen of a human spleen cDNA library was undertaken. RIP2 was identified as a TRAF3 binding partner. PMID: 23333941 inositol phosphatase SHIP-1 inhibits NOD2-induced NF-kappaB activation by disturbing the interaction of XIAP with RIP2 PMID: 22815893 RIPK2 might play an important role in hepatic cell migration. These findings could shed new light on carcinogenesis and on liver regeneration. PMID: 22993319 Association has been found between RIPK2 (rs42490) and cancer risk. PMID: 22504414 regulates reduced prostaglandin E2 production in chronic periodontitis PMID: 22828789 RIP2 tyrosine kinase activity is not only required for NOD2-dependent autophagy but plays a dual role in this process. PMID: 22665475 These findings mechanisms whereby HBeAg modulates intracellular signaling pathways by targeting RIPK2, supporting the concept that HBeAg could impair both innate and adaptive immune responses to promote chronic HBV infection. PMID: 22615316 IL-4 failed to up-regulate expression of RP105 at the cell surface. In conclusion, the anti-inflammatory actions of IL-4 occur independently of IL-10, RP105, and the kinase activity of RIPK2 PMID: 22484241 RIP2 gene polymorphisms may be associated with susceptibility to systemic lupus erythematosus in the Chinese population. PMID: 22075569 GEF-H1 mediated the activation of Rip2 during signaling by NOD2, but not in the presence of the 3020insC variant of NOD2 associated with Crohn's disease. GEF-H1 functioned downstream of NOD2 as part of Rip2-containing signaling complexes. PMID: 21887730 the CARD of procaspase-1 is differently involved in the formation of procaspase-1 activating platforms and procaspase-1-mediated, RIP2-dependent NF-kappaB activation. PMID: 21862576 Tri-DAP interacts directly with the LRR domain of NOD1 and consequently increases RICK/NOD1 association and RICK phosphorylation activity PMID: 21757725 RIP2 polymorphisms are not associated with inflammatory bowel diseases. PMID: 20645315 RIP2 undergoes autophosphorylation on Tyr 474 and this event is necessary for effective NOD2 signaling PMID: 21123652 MS80 inhibits CD40-NF-kappaB pathway via targeting RIP2. PMID: 19911254 detected on all female reproductive tract tissues PMID: 19406482 Data suggest that inhibition of rip2 upregulation after wounding might contribute to the reduced and delayed wound re-epithelialization phenotype seen in glucocorticoid-treated patients. PMID: 20025869 Elevated RIP-2 protein levels promote NF-kappaB function via interaction with IKK gamma PMID: 19693652 the NOD2/RIP2 pathway has a role in recognition of Yersinia, but caspase-12 does not modulate innate host defense against Y. pestis PMID: 19721713 Involvement of receptor-interacting protein 2 in innate and adaptive immune responses PMID: 11894097 These results implicate RIP2 in a previously unrecognized role: a checkpoint for myogenic proliferation and differentiation. PMID: 12138198 equilibrium and kinetic folding of a unique protein domain, caspase recruitment domain (CARD), of the RIP-like interacting CLARP kinase (RICK) (RICK-CARD), which adopts a alpha-helical Greek key fold PMID: 12755636 role in CARD6 modulation of NF-kappa B activation PMID: 12775719 Rip2 has an important role in TCR-induced NF-kappaB activation and T-cell function PMID: 14638696 NOD2-dependent ubiquitinylation of NEMO (a key component of the NF-kB signaling complex) is dependent on the scaffolding protein kinase RIP2. PMID: 15620648 Caspase-1-mediated cell death is regulated, at least in part, by the balance of Rip2 and Cop; alterations of this balance may contribute to aberrant caspase-1-mediated pathogenesis in Huntington's disease. PMID: 16354923 CARD6 is a regulator of NF-kappaB activation that modulates the functions of RICK protein PMID: 16418290 NOD2-S interacts with both, NOD2 and receptor-interacting protein kinase 2 and inhibits the "nodosome" assembly by interfering with the oligomerization of NOD2 PMID: 16492792

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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.

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