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 >  Protein>IL-17 RC >ILC-H5259

Human IL-17 RC Protein, Fc Tag (MALS verified)

分子别名(Synonym)

IL-17 RC,IL-17RC,IL17Rhom,IL-17 receptor C,IL-17RL,ZcytoR14

表达区间及表达系统(Source)

Human IL-17 RC, Fc Tag (ILC-H5259) is expressed from human 293 cells (HEK293). It contains AA Leu 21 - His 465 (Accession # NP_703190.2).

Predicted N-terminus: Leu 21

Request for sequence

蛋白结构(Molecular Characterization)

IL-17 RC Structure

This protein carries a human IgG1 Fc tag at the C-terminus.

The protein has a calculated MW of 75.9 kDa. The protein migrates as 90-115 kDa when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition (SDS-PAGE) due to glycosylation.

内毒素(Endotoxin)

Less than 1.0 EU per μg by the LAL method.

纯度(Purity)

>95% as determined by SDS-PAGE.

>90% as determined by SEC-MALS.

制剂(Formulation)

Lyophilized from 0.22 μm filtered solution in PBS, pH7.4 with trehalose as protectant.

Contact us for customized product form or formulation.

重构方法(Reconstitution)

Please see Certificate of Analysis for specific instructions.

For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

存储(Storage)

For long term storage, the product should be stored at lyophilized state at -20°C or lower.

Please avoid repeated freeze-thaw cycles.

This product is stable after storage at:

  1. -20°C to -70°C for 12 months in lyophilized state;
  2. -70°C for 3 months under sterile conditions after reconstitution.

质量管理控制体系(QMS)

  1. 质量管理体系(ISO, GMP)
  2. 质量优势
  3. 质控流程
 

电泳(SDS-PAGE)

IL-17 RC SDS-PAGE

Human IL-17 RC, Fc Tag on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 95% (With Star Ribbon Pre-stained Protein Marker).

SEC-MALS

IL-17 RC SEC-MALS

The purity of Human IL-17 RC, Fc Tag (Cat. No. ILC-H5259) is more than 90% and the molecular weight of this protein is around 200-230 kDa verified by SEC-MALS.

Report

 

活性(Bioactivity)-ELISA

IL-17 RC ELISA

Immobilized Human IL17A, Tag Free (Cat. No. ILA-H5219) at 2 μg/mL (100 μL/well) can bind Human IL-17 RC, Fc Tag (Cat. No. ILC-H5259) with a linear range of 5-160 ng/mL (QC tested).

Protocol

IL-17 RC ELISA

Immobilized Human IL-17F, His Tag (Cat. No. ILF-H5244) at 2 μg/mL (100 μL/well) can bind Human IL-17 RC, Fc Tag (Cat. No. ILC-H5259) with a linear range of 0.02-0.25 μg/mL (Routinely tested).

Protocol

 

活性(Bioactivity)-SPR

IL-17 RC SPR

Human IL-17A Protein, Tag Free immobilized on CM5 Chip can Human IL-17 RC, Fc Tag (Cat. No. ILC-H5259) with an affinity constant of 72.8 nM as determined in a SPR assay (Biacore T200) (Routinely tested).

Protocol

IL-17 RC SPR

Biotinylated Human IL-17A Protein, His,Avitag™ (Cat. No. ILA-H82Q1) captured on Biotin CAP - Series S sensor Chip can bind Human IL-17 RC, Fc Tag (Cat. No. ILC-H5259) with an affinity constant of 40.9 nM as determined in a SPR assay (Biacore T200) (Routinely tested).

Protocol

 

活性(Bioactivity)-BLI

IL-17 RC BLI

Loaded Biotinylated Human IL17A, His,Avitag (Cat. No. ILA-H82Q1) on SA Biosensor, can bind uman IL-17 RC, Fc Tag (Cat. No. ILC-H5259) with an affinity constant of 13.8 nM as determined in BLI assay (ForteBio Octet Red96e) (Routinely tested).

Protocol

IL-17 RC BLI

Loaded Human IL-17A&IL-17F Heterodimer Protein, Twin Strep&His Tag (Cat. No. ILF-H52W6) on NTA Biosensor, can bind Human IL-17 RC, Fc Tag (Cat. No. ILC-H5259) with an affinity constant of 92.3 nM as determined in BLI assay (ForteBio Octet Red96e) (Routinely tested).

Protocol

IL-17 RC BLI

Loaded Human IL-17F, His Tag (Cat. No. ILF-H5244) on NTA Biosensor, can bind Human IL-17 RC, Fc Tag (Cat. No. ILC-H5259) with an affinity constant of 100 nM as determined in BLI assay (ForteBio Octet Red96e) (Routinely tested).

Protocol

 
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背景(Background)

Interleukin-17 receptor C (IL-17 RC), also known as IL17Rhom, IL-17RL, is the receptor for IL17A and IL17F homodimers as part of a heterodimeric complex with IL17RA. IL-17A activity is inhibited by IL-17RA, IL-17F is inhibited by IL-17RC, and a combination of soluble IL-17RA/IL-17RC receptors is required for inhibition of the IL-17F/IL-17A activity. Furthermore, activation of IL17RC can lead to the induction of expression of inflammatory chemokines and cytokines such as CXCL1.

 

前沿进展

Siglec-targeted liposomes to identify sialoglycans present on fungal pathogens
Ambati, Choudhury, Peter et al
Antimicrob Agents Chemother (2025)
Abstract: The sialic acid Ig-like lectins Siglec-3 and Siglec-15 are pathogen receptors that bind sialic acid-modified glycoproteins, best characterized in metastatic cancers. Because fungi produce sialoglycans and sialo-glycoproteins, we wondered if Siglecs had the potential for targeted delivery of antifungal drugs. We purified the extracellular V-region Ig-like C2 ligand-binding domains and stalk regions of SIG3 and SIG15. We floated the two polypeptides on the surface of liposomes loaded with amphotericin B (AmB) and labeled with rhodamine B to prepare SIG3-Ls and SIG15-Ls. Using these two reagents, we explored the sialoglycans of two evolutionarily distant and deadly human fungal pathogens, the Mucormycete Rhizopus delemar and the Ascomycete Aspergillus fumigatus. We found that SIG3-Ls and SIG15-Ls localized in a continuous layer over the cell wall surface of germ tubes and hyphae of both fungal species and to the conidia of A. fumigatus. Binding was Neu5Ac-specific and appeared confined to N-linked sialoglycans on fungal proteins. SIG3 and SIG15 proteins bound to diverse sialo-glycoproteins extracted from the hyphae of both species. SIG3-Ls and SIG15-Ls delivering sub-micromolar concentrations of AmB were moderately more effective at inhibiting and/or killing both species relative to control liposomes. We discuss the roles that sialo-glycoproteins may play in fungal pathogens.
Mediating Role of Blood Metabolites in the Relationship Between Immune Cell Traits and Heart Failure: A Mendelian Randomization and Mediation Analysis
Liu, Shen, Cao
J Am Heart Assoc (2025) 14 (6), e037265
Abstract: Observational studies have shown a significant association between immune cells and heart failure (HF). Nevertheless, the precise biological mechanisms underlying this association remain unclear.To investigate the causative relationships and underlying mechanisms between immune cell traits and adult HF, 3 main methods of Mendelian randomization were used: 2-sample Mendelian randomization, multivariable Mendelian randomization with controlling for several factors affecting HF, and mediation analysis. Results from the inverse variance-weighted model indicated that genetic predispositions for human leukocyte antigen-type DR (HLA DR) on CD33dim HLA DR+ CD11b+ (odds ratio, 0.967 [95% CI, 0.939-0.996]; P=0.028) may be associated with a reduced risk of HF. Although the association between HF and HLA DR on CD33 dim HLA DR+ CD11b+ did not withstand multiple-testing correction, the Mendelian randomization results (PIVW <0.05) decrease the likelihood that the observational results are due to chance.Our 2-step mediation analysis demonstrated that genetic predispositions for HLA DR on CD33dim HLA DR+ CD11b+ (odds ratio,1.085 [95% CI, 1.020-1.155]; P=0.010) was associated with increased levels of the metabolite Octadecanedioate, while genetic predispositions for Octadecanedioate levels (odds ratio, 0.917 [95% CI, 0.849-0.991]; P=0.028) was associated with a reduced risk of HF. Moreover, our results also demonstrated that the association between HLA DR on CD33dim HLA DR+ CD11b+ and HF was possibly mediated by Octadecanedioate levels, with a mediation proportion of 21.4% [95% CI, 43.7 -0.998].These findings underscore the importance of HLA DR on CD33dim HLA DR+ CD11b+ in the development of HF, with Octadecanedioate levels acting as a possible mediator in this pathway.
Structure of the CD33 Receptor and Implications for the Siglec Family
Vu, Situ, Dai et al
Biochemistry (2025) 64 (7), 1450-1462
Abstract: In the innate immune system, the CD33 receptor modulates microglial activity. Its downregulation promises to slow Alzheimer's disease, and it is already targeted in blood cancers. The mechanism underlying CD33 signaling is unresolved. Starting from the available crystal structure of its extracellular IgV-IgC1 domains, we have assembled a model of the human CD33 receptor by characterizing the oligomerization and structure of IgC1, transmembrane, and cytosolic domains in solution. IgC1 homodimerizes via intermolecular β-strand pairing and packing. In contrast, the 21-residue transmembrane helix of CD33 appears monomeric and straight, with a conserved thin neck and thick belly appearance followed by a positively charged cytosolic patch. The cytosolic domain is dynamically unstructured. Sequence alignment and AlphaFold models indicate that IgC domains in the family of human Siglecs, to which CD33 belongs, are surprisingly variable. Only Siglec-6 is identified to analogously dimerize via IgC1. Our CD33 structural model suggests that the receptor is not signaling via a monomer-dimer shift. Rather, we propose that, aided but also constrained by dimerization, multivalent ligands may concentrate the receptor transmembrane and cytosolic domains sufficiently to trigger colocalization with an activating kinase.
HIV-Induced Sialoglycans on Infected Cells Promote Immune Evasion from Myeloid Cell-Mediated Killing
Singh, Islam, Liu et al
bioRxiv (2025)
Abstract: Sialic acid-containing glycans (sialoglycans) on pathological cells interact with Siglecs, glycol-immune checkpoint receptors expressed on myeloid cells such as monocytes and neutrophils. This interaction suppresses the cytotoxic functions of these immune cells. We show that HIV infection reprograms the glycosylation machinery of infected cells to increase the expression of specific sialoglycan ligands for Siglecs-3, -7, and -9. These ligands engage Siglecs on myeloid cells, impairing their ability to target HIV-infected cells. Selective disruption of these interactions using 10-1074-Sia, an HIV-specific antibody conjugated to sialidase-an enzyme that removes sialic acids-significantly enhances monocyte- and neutrophil-mediated killing of HIV-infected cells in autologous assays. Treatment with 10-1074-Sia in humanized mice infected with HIV reduces viral load and decreases inflammation. These findings reveal a novel immune evasion mechanism exploited by HIV to evade myeloid cell immune surveillance and highlight the potential of targeting sialoglycan-Siglec interactions to improve immune clearance of HIV-infected cells.
Showing 1-4 of 1139 papers.
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