Interleukin-23 receptor Antibodies

Interleukin-23 receptor (IL23R)

Associates with IL12RB1 to form the interleukin-23 receptor. Binds IL23 and mediates T-cells, NK cells and possibly certain macrophage/myeloid cells stimulation probably through activation of the Jak-Stat signaling cascade.

IL23 functions in innate and adaptive immunity and might take part in acute response to infection in peripheral tissues. IL23 might cause autoimmune inflammatory diseases and be important for tumorigenesis.

Gene Information

Human
Gene Name:	IL23R
Uniprot:	Q5VWK5
Entrez:	149233

Family

Belongs to:
type I cytokine receptor family

Alternative Names

IBD17; IL-23 R; IL-23 receptor; IL23R; IL-23R; interleukin 23 receptor; interleukin-23 receptor

Molecular Weight

Mass (kDA):
71.722 kDA

Genomic Context

Human
Location:	1p31.3
Sequence:	1; NC_000001.11 (67138639..67259979)

Tissue Specificity

Expressed by monocytes, Th1, Th0, NK and dendritic cells. Isoform 1 is specifically expressed in NK cells.

Subcellular Localizations

Cell membrane; Single-pass type I membrane protein.

Diseases

• Crohn Disease
• Inflammatory Bowel Diseases
• Intestinal Diseases
• Ulcerative Colitis
• Colitis
• Ulcer
• Autoimmune Reaction
• Psoriasis
• Inflammation
• Autoimmune Diseases
• Ankylosing Spondylitis
• Spondylitis
• Arthritis

• Rheumatoid Arthritis
• Autoimmunity
• Sclerosis
• Dysequilibrium Syndrome
• Cholangiocarcinoma
• Malignant Neoplasms
• Arthritis, Psoriatic

Interacting Proteins

• C1D
• Jak2

Pathways

• Pathogenesis
• Autophagy
• Immune Response
• Secretion
• Cell Differentiation
• Cytokine Production
• Lymphocyte Differentiation
• Cell Activation
• T Cell Activation
• Adaptive Immune Response
• Inflammatory Response
• Innate Immune Response
• Glycosylation

• Methylation
• Transport
• Cell Adhesion
• Hyperphosphorylation
• Dna Hypomethylation
• Cytokine Secretion
• Cell Fate Determination

PTMs

• Phosphorylation
• Methylation

• Glycosylation
• Demethylation

• Cleavage

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/IL23R

Best Uses Of The IL-23R Marker

This article focuses on the IL-23R cytokine receptor, one of the subunits of IL-23. Find out more about this polypeptide, and its applications. This article is applicable to scientists from any nation. It provides information about the various forms of markers known as IL-23R. Here are some examples. It is a good way to determine the presence of a specific illness by using IL-23R markers in a scientific study.

The IL-23R receptor is a type I cytokine receptor.

Recent research has found that IL23R is more prominent on memory/effector cells than the cells that are not naive. This confirms previous findings. Additionally, the loss of IL-23R receptor does no interfere with T-cell activation or exhaustion. Boster Bio's mouse model suggests that IL-23R is high on lymphocytes.

The IL-23 protein, which is responsible for tissue inflammation in humans and can also be responsible for autoimmune diseases. Studies have revealed that IL-23 polymorphisms could be linked to ankylosing spondylitis and thyroiditis caused by autoimmune. One such SNP, R381Q, encodes the mutation R381Q that is found in the IL-23R gene's Exon. However, R381Q seems to be protective for Crohn's disease patients as well as patients suffering from ulcerative colitis.

The IL-23R receptor is essential for the expression of epithelial Reg3b, which regulates the recruitment of neutrophils into secreting cells of IL-22. Furthermore, this cytokine could have a direct regenerative effect. It has been suggested that IL-23R could regulate the composition and health of colonic microbiota.

IL-23R is a subunit of IL-23

The IL-23R cytokine is tiny and membrane-bound, with multiple functional domains. It has a high amount, which is in contrast to other receptors for cytokine. It is found in a variety of tissues, including the skin and intestine. Its extracellular domains are accountable to bind HIL-23. It is unclear what functions these domains perform in the body.

The dimeric cytokine IL-23R is composed of two disulfide linked subunits of cytokine. One for each beta IL-12R, and the other one for IL-23. Although they play different roles in signaling, these subunits are structurally similar. The IL-23R subunit has a unique WQPWS structure in the transmembrane cytokine receiver domain. The IL-23R gene is located on the chromosome 1 (1p31.2-32.1) and is comprised of three Src homology 2 domains, as well as two STAT-binding sites.

The IL-23R receptor interacts with the IL-23 protein, a type of cell cytokine that regulates the function of immune cells. When IL-23 is bound to the receptor, it activates an array of chemical signals within the cell including those that trigger inflammation and coordinate the immune response to foreign invaders. In addition to its regulatory roles as a regulator, IL-23 also regulates a variety of inflammatory diseases as well as immune system functions.

The IL-23R can be utilized as an oligopeptide

IL-23R is a ligand that is found on the surface of the human immune system. The ligand needs to interact with its receptors to inhibit its activity. Boster Bio has created a polypeptide with the IL23R sequence. This is a highly purified and purified polypeptide. The antibody is made in E. coli. It is capable of recognizing P19 ligand and IL-23R.

The IL-23R protein is a type I cytokine receptor which is paired with IL12RB1. This protein binds to the transcription activator STAT3. Boster's IL-23R is able to recognize the IL-23R structure in both bacterial and human samples. Antibodies that target IL 23R are highly specific, allowing them to inhibit the cytokine signaling pathway IL-23.

In addition to blocking the IL-23 ligand, this anti-IL-23R polypeptide could be utilized for many other purposes. It can be used to target ribosome display. It could be used to identify binders that will bind specifically to the receptor IL-23. The human IL-23 receptor gene consists of 10 exons, which encode the transmembrane polypeptide, which has a total of 629 amino acids. It also contains five sequences and five cysteine pairs that are associated with Fibronectin type III. Moreover, it also contains an Ig-like terminal domain that assists in the creation of disulphide bridges. Boster Bio successfully expressed human IL23 receptors by using an E. coli SHuffle strain.

IL-23R is a biomarker

It is a cytokine that is now recognized as a reliable biomarker used to detect cancerous cells. IL-23R is present in both cancer cells as well as normal cells. A variety of cancers have higher levels of IL-23R. IL-23R plays an important role in cell growth and differentiation regulation. However, the exact mechanism of IL-23R is not known.

Target engagement in IL 23R is a powerful instrument for identifying the efficacy of immunotherapy treatments. The target engagement process involves identifying biomarkers that are relevant to pharmacodynamics and the correlation of these biomarkers with efficacy readouts for murine and human TNBS models of colitis. This research is led by a group of experts who have a wealth of experience in oral delivery and translating early stages of research into clinical outcomes.

This study revealed that mice treated with IL-24R had a lower IL-23R biomarker. In addition, calprotectin and Reg3g were elevated in colon epithelial cells throughout the disease, but LCN2 was only identified in the lamina propria. The biomarkers can be useful for CD research, but more studies are required to understand the role of IL23 within colon cancer.

It is safer than IL-12Rb1 than IL-23R.

The development of specific IL-23R antagonists is delayed because of the lack of available drugs that specifically target this receptor. Recently, IL-23Ra was crystallized and studied using mass spectrometry using hydrogen and deuterium. It was revealed that IL-23 has a binding affinity to IL-23R of molecular affinity 44 nM. This is in contrast to the 2 mM exhibited by the IL-12Rb1. In addition the IL-23 complex and IL-23R shows a cooperating effect due to a conformational change within IL-23.

In a different experiment the safety of IL-23R over IL-12Rb1 has been assessed using a T-cell activation bead. A flow cytometric analysis revealed that activated cells containing the IL23R gene were higher than the rest. The results were similar in four tests. Although more research is needed to determine the exact function of IL-23R, it remains safe to use in patients with inflammation-related disorders.

IL-23R has been linked with inflammatory bowel diseases, despite concerns about its safety. A genome-wide association study has revealed that the gene responsible for the IL-23R gene is strongly linked to Crohn's disease, while an unusual coding variant offers strong protection. This confirms previous findings and highlights the potential for new therapies to target the IL-23 receptor.

The IL-23R protein is a potential target for monoclonal antibodies

Interleukin-23 is a member of the IL-12 family and plays an important role in the pro-inflammatory T-helper17 cell response. IL-23 has been linked to various inflammatory and autoimmune disorders. The structure of IL23R receptor complexes was elusive until recently. We have shown that IL-23R is bound to IL-23 through its immunoglobulindomain N-terminal. The IL-12p40 subunit is restrained to cooperate with the IL-12Rb1 binder.

The multifaceted roles of IL 23 are discovered in autoimmune and inflammation-related disorders. The IL-23/IL-17 axis regulates immune responses and plays a key role in chronic inflammatory disorders. Therefore, 15 different monoclonal antibodies are currently in preclinical or clinical development targeting the IL-23 receptor. These antibodies are being developed by 12 companies.

We tested antibodies against the p19 subunits to determine if IL-23R was a target. The presence of 50 percent human serum was utilized to determine the possibility of non-specific binding of proteins. Each antibody displayed an amount of two in serum compared to the buffer. This indicated that the antibodies were specific to the targets. We identified four monoclonal antigens that blocked the production of cytokines in a subsequent study.

IL-23R Marker is a humanized anti-IL-23R antibody

The marker IL23R is a humanized anti-IL-27 antibody that recognizes receptor p19 on the cell's surface. This antibody that is humanized blocks p19's binding to receptor IL23R by targeting the surface-exposed epitopes. The two most effective clones for inhibiting contain a random cysteine residue in the interloop between helices 2 & 3 and an intrinsic symmetry.

For the production of this ELISA the p19 subunit that is part of the IL-23 receptor has been isolated from E. coli cells and affinity purified by Ni-NTA. An anti-human IL23 antibody was developed to identify the subunit p19. The ELISA confirmed the binding of DHMBP-p19 soluble with the anti-p19 antibody.

The REX Ligands blocked binding of the IL-23R human cells. The REX binding ligands had a strong affinity to THP-1 and K-562 cells and were correlated with the expression of IL-23R. Jurkat cells however, showed a lower level of IL-23R/cell. This is the case for all REX ligands as well as the IL-23R marker.