IL5RA Antibodies

Interleukin-5 receptor subunit alpha (IL5RA)

This is the receptor for interleukin-5. The alpha chain binds to IL5.

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Gene Information

Human
Gene Name:	IL5RA
Uniprot:	Q01344
Entrez:	3568

Family

Belongs to:
type I cytokine receptor family

Alternative Names

CD125 antigen; CD125; CDw125CD125; HSIL5R3; IL-5 R alpha; IL-5 receptor subunit alpha; IL5R alpha; IL-5R subunit alpha; IL5R; IL5RA; IL-5Ra; IL-5R-alpha; interleukin 5 receptor type 3; interleukin 5 receptor, alpha; interleukin-5 receptor alpha chain; interleukin-5 receptor alpha subunit; interleukin-5 receptor subunit alpha; MGC26560

Molecular Weight

Mass (kDA):
47.685 kDA

Genomic Context

Human
Location:	3p26.2
Sequence:	3; NC_000003.12 (3066324..3110414, complement)

Tissue Specificity

Expressed on eosinophils and basophils.

Subcellular Localizations

Membrane; Single-pass type I membrane protein.

Diseases

• Asthma
• Eosinophilia
• Inflammation
• Malignant Neoplasms
• Neoplasms
• Cerebrovascular Accident
• Ischemic Stroke
• Leukemia
• Sclerosis
• Brain Ischemia
• Hypereosinophilic Syndrome
• Melanoma

• Neuromuscular Diseases
• Myeloid Leukemia, Chronic
• Lung Diseases
• Mastocytosis
• Malignant Neoplasm Of Urinary Bladder
• Opisthotonus
• Lung Diseases, Obstructive

Interacting Proteins

• CSF2RB
• IL5
• JAK2

Pathways

• Pathogenesis
• Eosinophil Differentiation
• Eosinophil Activation
• Cell Proliferation
• Eosinophil Development
• Cell Migration
• Cell Cycle
• Eosinophil Migration
• Glycosylation

• Regulation Of Gene Expression
• Metaphase
• Localization

PTMs

• Phosphorylation
• Glycosylation

• Deglycosylation
• Myristoylation

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/IL5RA

Best Uses Of The IL5RA Marker

The IL5RA Marker is a great option for researchers to evaluate IL-5Ra. The IL5RA marker can measure IL-5Ra levels in a variety of biological processes. There are many different uses for the IL5RA marker, including biomarkers for cancer, immune response, inflammatory response, inflammation, and many others. We will discuss the various uses of IL-5RA and the residues involved in binding the protein.

Anti-IL5RA Signer

Bostro Bio's AntiIL5RA Marker can be used as a test to determine the activity and sensitivity of antibodies against human IL-5Ra. This antibody is available in a single-use kit. It has been validated using known positive and negative samples. The product can be stored at up to -20°C for one year or at 4°C for one month. Boster Bio has a wide range of bioassay kits and reagents.

CEL was found to activate IL-5RA by the F/P cancerogene. F/P/IL-5RA coexpression promoted prominent activation of IL-5R kinase. Cells tested with an in vitro kinase analyzer were able to detect IL-5-induced Lyn phosphorylation. In addition, Lyn is involved in the cross-talk between IL-5 and chemotactic factors.

IL-5Ra also has been detected in neutrophils, noneosinophils, and other cells. These cells protect against sepsis. Moreover, high levels IL-5 can be associated with increased survival. These results are encouraging, but further studies are needed to determine how this marker impacts sepsis. Once this is determined, the anti-IL5RA bioassay can be used to monitor the inflammatory process in a patient with sepsis.

Key components of chronic eosinophilic lukemia are inflammation induced via F/P and IL-5RA cytokinase. Both cytokines infuse Lyn kinase into F/P-positive cell lines, which promotes cell proliferation as well as inhibits apoptosis. These pathways are inhibitory and can cause cell migration and proliferation to be inhibited. It also reduces cellular signaling.

The development of drugs to control inflammation has shifted attention to the role of IL-5 in eosinophilic inflammation. These agents can reduce asthma exacerbations. Further studies with this drug did not show significant differences on clinical parameters. The differences between the two groups were not statistically significant in terms of peak flow recordings and airway hyperresponsiveness.

Other residues involved with binding to IL-5Ra

IL-5Ra is a multidomain cytokine-receptor with D1 domain and D3 domains, and a pair FnIIIdomains. Each domain contains seven antiparallel b strands. Cysteine found on b5 does not play a role in disulfide-bond formation. Binding is performed by Cys269 and Cys316 in D2 domain. The protomer of IL-5 is composed of four ahelices. The two other domains are identical, but have different compositions.

Molecular modeling has demonstrated that the transmembrane IL-5Ra Subunit is required to activate IL-5. The soluble IL-5Ra IL-5Ra unit sequesters IL-5 and inhibits signaling. As a potential candidate in asthma host genetic studies, genetic polymorphisms of the IL-5Ra genome are being studied. IL-5Ra also plays an important role in eosinophil function.

The D1 domain of IL-5RA interacts with IL-5 chain A through a series of salt bridges and interactions. It also forms an a3-a4 loop with IL-5. These interactions make it possible for the interface to remain stable between these two proteins. Hydrogen bonds are also used to mediate the interaction of IL-5RA with IL-5. Several IL-5 Receptors share the same bc Interface.

The transcriptional activity of IL-5Ra's soluble transcript isoform is higher than that found in the signaling competent, transmembrane. Thus, the soluble isoform of IL-5RA may be needed for boosting the development of eosinophil progenitors. Moreover, soluble IL-5Ra might also serve as a mediator against an active eosinophil response.

Three distinct interfaces characterize IL-5RA's binding site. Site 1 is a b3-b4 loop made up of the D3 domain, and b5-b6 loop consists of IL-5 chains A and B. The backbone Arg208 forms a hydrogen connection with Gln158, IL-5 link A. While the side chain of Arg208 interacts Glu64 and Gln120, IL-5 link B.

Other residues that are involved in binding to IL-5RA are position 80-pBpa which is the ectodomain and positions 21-335 of mature IL-5. The stoichometric IL-5*IL-5RA soluble IL-5 complex has a 2:1 ratio. The other residues involved in binding to IL-5RA are unknown and need to be characterized.

Chromatin immunoprecipitation was used as a method to determine IL5RA's promoter occupancy. It is a method that follows dynamic changes of transcription factor binding. C/EBPa, C/EBPb, and C/EBPb occupied the P1 promoters, while PU.1 (late differentiation stages) and GATA-1 were found at the P2 enhancer. After determining the presence of both PU.1 and C/EBPa/C-EBPa, these residues were identified as involved in binding to IL-5Ra.

The electrostatic map of the GM–CSF*GM–CSFRA is similar to that for IL-5*IL-5RA. However the D3 domain differs. These two domains are essentially superimposed upon GM-CSF*GM–CSFRA. Although they are closely related, the two complexes have distinct orientations that likely contribute to their distinct ligand-binding properties.

There are other ways to measure IL-5Ra

There are many ways to measure IL-5Ra. One method is quantitative ELISA. In this method, samples are diluted in a microplate reader before their Optical Density(OD) is measured. This method allows you to measure IL-5Ra concentrations without the need for a reagent, and get the results instantly. Other methods include Western blots, PCR assays, and Western blots.

The association of IL5RA polymorphisms with asthma is a strong indicator that this gene could potentially be a risk factor. The association is confirmed by further biological and functional evidence. The polymorphisms might provide valuable information to aid in asthma control. For example, IL5RA could be linked to a host’s susceptibility.

Another method to measure IL-5Ra is sandwich enzyme-linked immune-sorbent assays. This method measures the concentrations of IL-5RA within human serum and plasma. The plate is precoated with an antibody specific to human IL-5RA. The samples are then pipetted into a well plate measuring 96 x 96. The immobilized antibody binds to the IL-5RA within the samples. Next, an anti-Human IL-5RA antibody, HRP-conjugated streptavidin, and TMB substrate solution are added to the wells. Once these reagents have bound with the target, the plate's colour changes from blue to yellow. The amount of IL-5RA that is bound to the plate determines the intensity of the yellow color.

Recent research showed that soluble IL-5Ra mRNA peaked at an earlier stage, while the signaling competent transmembrane wasoform peaked around a moderate level. ChIP was used to test the binding sites for both transcription factors in human eosinophilic cell line lines. These results also suggest that eosinophilopoiesis favors increased expressions of IL-5Ra. The authors also found out that IL-5Ra's beta subunit is involved with IL-5-dependent generation eosinophils. This is due to multiple interacting transcription proteins and their signaling products.

You can also measure IL-5Ra concentration using blood eosinophils, and exhaled nitric oxygen levels. Biomarkers will enable clinicians to prescribe the best drugs based on the results of clinical trials. These new methods of evaluating IL-5Ra levels can help patients with inflammatory conditions to prescribe personalized medicines that are more tailored to their individual needs.

In asthmatic patients, increased eosinophil counts are associated with higher IL-5Ra mRNA levels. However, this method has some limitations so it should be used with caution. It is important that you remember that the IL-5RA subunit does not cause disease. There are other ways to determine IL-5Ra levels. This method is useful in determining if IL-5RA has caused eosinophilic inflammation in the lungs.