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 >  Protein>IL-33 >IL3-H82H5

Biotinylated Human IL-33 Protein, His,Avitag™ (MALS verified)

分子别名(Synonym)

IL33,DV27,C9ORF26,IL1F11,NFHEV,DKFZp586H0523,DVS27,NFEHEV,RP11-575C20.2

表达区间及表达系统(Source)

Biotinylated Human IL-33, His,Avitag (IL3-H82H5) is expressed from human 293 cells (HEK293). It contains AA His 109 - Thr 270 (Accession # O95760-1).

Predicted N-terminus: His

Request for sequence

蛋白结构(Molecular Characterization)

IL-33 Structure

This protein carries a polyhistidine tag at the N-terminus, followed by an Avi tag (Avitag™).

The protein has a calculated MW of 21.9 kDa. The protein migrates as 28-33 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.

标记(Labeling)

Biotinylation of this product is performed using Avitag™ technology. Briefly, the single lysine residue in the Avitag is enzymatically labeled with biotin.

蛋白标记度(Protein Ratio)

Passed as determined by the HABA assay / binding ELISA.

内毒素(Endotoxin)

Less than 1.0 EU per μg by the LAL method.

纯度(Purity)

>90% 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-33 SDS-PAGE

Biotinylated Human IL-33, His,Avitag on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 90%.

SEC-MALS

IL-33 SEC-MALS

The purity of Biotinylated Human IL-33, His,Avitag (Cat. No. IL3-H82H5) is more than 90% and the molecular weight of this protein is around 25-40 kDa verified by SEC-MALS.

Report

 

活性(Bioactivity)-ELISA

IL-33 ELISA

Immobilized Human IL-1RL1, Fc Tag (Cat. No. IL1-H5250) at 5 μg/mL (100 μL/well) can bind Biotinylated Human IL-33, His,Avitag (Cat. No. IL3-H82H5) with a linear range of 0.1-2 ng/mL (QC tested).

Protocol

 

活性(Bioactivity)-BLI

IL-33 BLI

Loaded Human IL-1RL1, Fc Tag (Cat. No. IL1-H5250) on Protein A Biosensor, can bind with Biotinylated Human IL-33, His,Avitag (Cat. No. IL3-H82H5) an affinity constant of 1.81 nM as determined in BLI assay (ForteBio Octet Red96e) (Routinely tested).

Protocol

 
评论(4)
  1. 176XXXXXXX2
  2. 1人赞
  3. 用来检测细胞中和细胞分泌的S蛋白含量,细胞培液是直接加到试剂盒提供的酶标板中,贴壁的细胞是加入细胞裂解液,4度裂解一段时间反复吹打后加入酶标板中,均可以检测出S蛋白含量
  4. 2021-10-22
  1. 135XXXXXXX7
  2. 0人赞
  3. 产品很好,冠状病毒S蛋白暴露于病毒表面并介导病毒进入宿主细胞,因此它是感染后中和抗体的主要靶标,也是药物开发和疫苗设计的重点。
  4. 2023-1-16
 
ACRO质量管理体系
 
 

背景(Background)

Interleukin 33 (IL33) is known as C9orf26, DKFZp586H0523, DVS27, NF-HEV, NFEHEV, RP11-575C20.2,and is a cytokine belonging to the IL-1 superfamily. IL-33 induces helper T cells, mast cells, eosinophils and basophils to produce type 2 cytokines. IL-33 mediates its biological effects by interacting with the receptors ST2 (aka IL1RL1) and IL-1 Receptor Accessory Protein (IL1RAP), activating intracellular molecules in the NF-κB and MAP kinase signaling pathways that drive production of type 2 cytokines (e.g. IL-5 and IL-13) from polarized Th2 cells. In vivo, IL-33 induces the expression of IL-4, IL-5, and IL-13 and leads to severe pathological changes in mucosal organs.

 

前沿进展

The Novel Oncolytic Herpes Simplex Virus Type-1 (HSV-1) Vaccine Strain VC2 Constitutively Expressing GM-CSF Causes Increased Intratumoral T Cell Infiltration and Inhibition of Tumor Metastasis in the 4T1/Balb/c Mouse Model of Stage Four Breast Cancer
Nabi, Chouljenko, Musarrat et al
J Med Virol (2025) 97 (2), e70220
Abstract: Oncolytic virotherapy (OVT) aims to disrupt the tumor microenvironment and provide a unique therapeutic approach against solid tumors. Herpes simplex virus type-1 (HSV-1) has shown strong promise for treating various solid tumors and has been approved to treat melanoma and glioma in human patients. Previously, we reported the generation of an engineered HSV-1 vaccine strain VC2, which has shown exceptional promise as an oncolytic and immunotherapeutic virus. In the present work, we engineered VC2 to constitutively express the murine granulocyte-macrophage colony-stimulating factor (GM-CSF) gene inserted in place of HSV-1 Glycoprotein C (gC). We tested the efficacy of VC2-GMCSF for its ability to generate antitumor response in the 4T1 stage four metastatic breast cancer mouse model. GM-CSF expression enhanced VC2 viral replication and infectious virus production. Tumors formed after 7 days of engraftment in the mammary fat pad of Balb/CJ mice were treated by injecting ~5 × 104 plaque forming units (PFU) of VC2/VC2-GMCSF once. Intratumor treatment did not appreciably reduce average primary tumor sizes. However, metastatic foci were significantly reduced in mice lungs treated with VC2-GMCSF compared to VC2 or mock treatment. VC2-GMCSF intratumoral treatment induced a stronger intratumor T cell infiltration but not an increased cytotoxic activity. A significant T cell infiltration was observed in the metastatic areas in VC2-GMCSF treated animals, which was associated with reduced pro-tumor marker PDL1 and VEGF gene expression. These results show that constitutive expression of GM-CSF enhanced the overall efficacy of VC2 for OVT. VC2-GMCSF holds promise as oncolytic and immunotherapeutic virotherapy for breast and other cancers.© 2025 Wiley Periodicals LLC.
Enhancement of HSV-1 cell-free virion release by the envelope protein gC
Frost, Salnikov, Rice
Virology (2024) 596, 110120
Abstract: Glycoprotein C (gC), one of ∼12 HSV-1 envelope glycoproteins, carries out several important functions during infection, including the enhancement of virion attachment by binding to host cell heparan sulfate proteoglycans (HSPG). Here we report that gC can also enhance the release of cell-free progeny virions at the end of the infectious cycle. This activity was observed in multiple cellular contexts including Vero cells and immortalized human keratinocytes. In the absence of gC, progeny virions bound more tightly to infected cells, suggesting that gC promotes the detachment of virions from the infected cell surface. Given this finding, we analyzed the biochemical interactions that tether progeny virions to cells and report evidence for two distinct modes of binding. One is consistent with a direct interaction between gC and HSPG, whereas the other is gC-independent and likely does not involve HSPG. Together, our results i) identify a novel function for a long-studied HSV-1 glycoprotein, and ii) demonstrate that the extracellular release of HSV-1 virions is a dynamic process involving multiple viral and host components.Copyright © 2024 The Authors. Published by Elsevier Inc. All rights reserved.
Decrease in Heparan Sulphate Binding in Tropism-Retargeted Oncolytic Herpes Simplex Virus (ReHV) Delays Blood Clearance and Improves Systemic Anticancer Efficacy
Vannini, Parenti, Forghieri et al
Cancers (Basel) (2024) 16 (6)
Abstract: The role of the interaction with cell-surface glycosaminoglycans (GAGs) during in vivo HSV infection is currently unknown. The rationale of the current investigation was to improve the anticancer efficacy of systemically administered retargeted oHSVs (ReHVs) by decreasing their binding to GAGs, including those of endothelial cells, blood cells, and off-tumor tissues. As a proof-of-principle approach, we deleted seven amino acids critical for interacting with GAGs from the glycoprotein C (gC) of R-337 ReHV. The modification in the resulting R-399 recombinant prolonged the half-life in the blood of systemically administered R-399 and enhanced its biodistribution to tumor-positive lungs and to the tumor-negative liver. Ultimately, it greatly increased the R-399 efficacy against metastatic-like lung tumors upon IV administration but not against subcutaneous tumors upon IT administration. These results provide evidence that the increased efficacy seen upon R-399 systemic administration correlated with the slower clearance from the circulation. To our knowledge, this is the first in vivo evidence that the partial impairment of the gC interaction with GAGs resulted in a prolonged half-life of circulating ReHV, an increase in the amount of ReHV taken up by tissues and tumors, and, ultimately, an enhanced anticancer efficacy of systemically administered ReHV.
Glycoprotein C of Herpes Simplex Virus 1 Shields Glycoprotein B from Antibody Neutralization
Komala Sari, Gianopulos, Nicola
J Virol (2020) 94 (5)
Abstract: Viruses have evolved strategies to avoid neutralization by the host antibody response. Herpes simplex virus (HSV) glycoprotein C (gC) functions in viral entry and binds to complement component C3b, inhibiting complement-mediated immunity. We investigated whether gC protects HSV from antibody neutralization. HSV-1 that lacks gC was more sensitive to complement-independent neutralization by a panel of gB monoclonal antibodies than a wild-type gC rescuant virus. The presence of gC decreased neutralization by 2- to 16-fold. The gB in the native envelope of HSV-1 had reduced reactivity with antibodies in comparison to gB from the gC-null virus, suggesting that gC hampers the recognition of gB epitopes in the viral particle. The protein composition of the gC-null virus, including the surface glycoproteins essential for entry, was equivalent to that of the wild type, suggesting that gC is directly responsible for the reduced antibody recognition and neutralization. The neutralizing activity of antibodies to gD and gH antibodies was also increased in HSV lacking gC. Together, the data suggest that HSV-1 gC protects the viral envelope glycoproteins essential for entry, including gB, by shielding them from neutralization as a potential mechanism of immune evasion.IMPORTANCE HSV-1 causes lifelong infection in the human population and can be fatal in neonatal and immunocompromised individuals. There is no vaccine or cure, in part due to the ability of HSV to escape the host immune response by various mechanisms. The HSV particle contains at least 15 envelope proteins, four of which are required for entry and replication. This work suggests a novel role for gC in shielding the HSV entry glycoproteins. gC may function to help HSV escape neutralization by antibodies.Copyright © 2020 American Society for Microbiology.
Showing 1-4 of 143 papers.
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IL-33靶点信息
英文全称:Interleukin-33
中文全称:白细胞介素-33
种类:Homo sapiens
上市药物数量:0详情
临床药物数量:10详情
最高研发阶段:临床三期
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