登录 | 注册    关注公众号  
微信公众号
搜索
 >  Protein>IL23A & IL12B >ILB-H5219

Human IL-23 alpha & IL-12 beta Heterodimer Protein, premium grade

分子别名(Synonym)

IL-23 alpha & IL-12 beta

表达区间及表达系统(Source)

Human IL-23A&IL-12B Heterodimer Protein, premium grade (ILB-H5219) is expressed from human 293 cells (HEK293). It contains AA Ile 23 - Ser 328 (IL-12B) & Arg 20 - Pro 189 (IL-23A) (Accession # P29460-1 (IL-12B) & Q9NPF7-1 (IL-23A)).

Predicted N-terminus: Ile 23

It is produced under our rigorous quality control system that incorporates a comprehensive set of tests including sterility and endotoxin tests. Product performance is carefully validated and tested for compatibility for cell culture use or any other applications in the early preclinical stage. When ready to transition into later clinical phases, we also offer a custom GMP protein service that tailors to your needs. We will work with you to customize and develop a GMP-grade product in accordance with your requests that also meets the requirements for raw and ancillary materials use in cell manufacturing of cell-based therapies.

Request for sequence

蛋白结构(Molecular Characterization)

This protein carries no "tag".

The protein has a calculated MW of 55.0 kDa. The protein migrates as 58 kDa±3 kDa under reducing (R) condition, and 58 kDa when calibrated against Star Ribbon Pre-stained Protein Marker under non-reducing (NR) condition (SDS-PAGE) due to glycosylation.

内毒素(Endotoxin)

Less than 0.1 EU per μg by the LAL method.

无菌(Sterility)

Negative

支原体(Mycoplasma)

Negative.

纯度(Purity)

>95% as determined by SDS-PAGE.

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 24 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)

IL23A & IL12B SDS-PAGE

Human IL-23A&IL-12B Heterodimer Protein, premium grade on SDS-PAGE under reducing (R) and non-reducing (NR) conditions. 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

IL23A & IL12B SEC-MALS

The purity of Human IL-23A&IL-12B Heterodimer Protein, premium grade (Cat. No. ILB-H5219) is more than 85% and the molecular weight of this protein is around 50-70 kDa verified by SEC-MALS.

Report

 

活性(Bioactivity)-CELL BASE

IL23A & IL12B CELL

Human IL-23A&IL-12B Heterodimer Protein, premium grade (Cat. No. ILB-H5219) stimulates proliferation of Human IL-23 R/IL-12 R beta 1(Luc) HEK293 Reporter Cell. The specific activity of Human IL-23A&IL-12B Heterodimer Protein, premium grade is > 1.80 X 10^3 U/mg (QC tested).

Protocol

 

活性(Bioactivity)-ELISA

IL23A & IL12B ELISA

Immobilized Human IL-23A&IL-12B Heterodimer Protein, premium grade (Cat. No. ILB-H5219) at 1 μg/mL (100 μL/well) can bind Monoclonal Anti-Human IL23A&IL12B P40 domain Antibody, Human IgG1 with a linear range of 0.02-1 ng/mL (QC tested).

Protocol

IL23A & IL12B ELISA

Immobilized Human IL-23A&IL-12B Heterodimer Protein, premium grade (Cat. No. ILB-H5219) at 5 μg/mL (100 μL/well) can bind Human IL-12 R beta 1, Fc Tag (Cat. No. ILB-H5255) with a linear range of 0.2-3 ng/mL (Routinely tested).

Protocol

 
评论(2)
 
ACRO质量管理体系
 
 

背景(Background)

Interleukin-23 subunit alpha (IL-23 alpha) can associates with IL12B to form the IL-23 interleukin, a heterodimeric cytokine which functions in innate and adaptive immunity. IL-23 may constitute with IL-17 an acute response to infection in peripheral tissues. IL-23 binds to a heterodimeric receptor complex composed of IL12RB1 and IL23R, activates the Jak-Stat signaling cascade, stimulates memory rather than naive T-cells and promotes production of proinflammatory cytokines. IL-23 induces autoimmune inflammation and thus may be responsible for autoimmune inflammatory diseases and may be important for tumorigenesis.

 

前沿进展

Conformational equilibrium of an ABC transporter analyzed by luminescence resonance energy transfer
Zoghbi, Nouel Barreto, Hernandez
Biophys J (2025)
Abstract: Humans have three known ATP-binding cassette (ABC) transporters in the inner mitochondrial membrane (ABCB7, ABCB8, and ABCB10). ABCB10, the most studied of them thus far, is essential for normal red blood cell development and protection against oxidative stress, and it was recently found to export biliverdin, a heme degradation product with antioxidant properties. The molecular mechanism underlying the function of ABC transporters remains controversial. Their nucleotide binding domains (NBDs) must dimerize to hydrolyze ATP, but capturing the transporters in such conformation for structural studies has been experimentally difficult, especially for ABCB10 and related eukaryotic transporters. Purified transporters are commonly studied in detergent micelles, or after their reconstitution in nanodiscs, usually at nonphysiological temperature and using nonhydrolyzable ATP analogs or mutations that prevent ATP hydrolysis. Here, we have used luminescence resonance energy transfer to evaluate the effect of experimental conditions on the NBD dimerization of ABCB10. Our results indicate that all conditions used for determination of currently available ABCB10 structures have failed to induce NBD dimerization. ABCB10 in detergent responded only to MgATP at 37°C, whereas reconstituted protein shifted toward dimeric NBDs more easily, including in response to MgAMP-PNP and even present NBD dimerization with MgATP at room temperature. The nanodisc's size affects the nucleotide-free conformational equilibrium of ABCB10 and the response to ATP in the absence of magnesium, but for all analyzed sizes (scaffold proteins MSP1D1, MSP1E3D1, and MSP2N2), a conformation with dimeric NBDs is clearly preferred during active ATP hydrolysis (MgATP, 37°C). These results highlight the sensitivity of this human ABC transporter to experimental conditions and the need for a more cautious interpretation of structural models obtained under far from physiological conditions. A dimeric NBD conformation that has been elusive in previous studies seems to be dominant during MgATP hydrolysis at physiological temperature.Copyright © 2025 Biophysical Society. Published by Elsevier Inc. All rights reserved.
ABC transporter activity is affected by the size of lipid nanodiscs
Nouel Barreto, Cuello, Zoghbi
FEBS Lett (2025) 599 (4), 502-511
Abstract: Lipid nanodiscs have become a widely used approach for studying membrane proteins thanks to several advantages they offer. They have been especially useful for studying ABC transporters, despite the growing concern about the possible restriction of the conformational changes of the transporters due to the small size of the discs. Here, we performed a systematic study to determine the effect of the nanodisc size on the ATPase activity of model ABC transporters from human, plant, and bacteria. Our data confirm that the activity of the transporters and their response to regulatory molecules is affected by the nanodisc size. Our findings suggest the use of larger membrane scaffold proteins (MSPs), such as MSP2N2 nanodiscs, to minimize alterations caused by the commonly used small MSP1D1.© 2025 The Author(s). FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.
Electrochemical studies of the mitochondrial ROMK2 potassium channel activity reconstituted into the free-standing and tethered bilayer lipid membranes
Stefanowska, Koprowski, Bednarczyk et al
Bioelectrochemistry (2023) 151, 108372
Abstract: The renal-outer-medullary‑potassium (ROMK2) channel modulates potassium transport in the kidney. It has been postulated that the ROMK2 is the pore-forming subunit of the mitochondrial ATP-sensitive potassium channel as a mediator of cardioprotection. In this study, cell-free synthesis of the ROMK2 was performed in presence of membrane scaffold protein (MSP1D1) nanodiscs. Activity measurements were achieved after channel reconstitution into the planar lipid bilayer and tethered bilayer lipid membranes. Both methods allowed for monitoring of channel function, verified with channel blocking and activation/re-activation experiments. The primary function of the mitochondrial potassium channels is to regulate the potential of the mitochondrial membrane, which allows them to play an important role in cytoprotection. This work focuses on obtaining the ROMK2 using a cell-free expression system, followed by the incorporation of the channel protein into the lipid bilayer and studying the influence of voltage changes and molecular modulators on channel activity. Channel activity was measured after its reconstitution into two models of lipid bilayers - BLM (Bilayer Lipid Membrane) and tBLM (Tethered Bilayer Lipid Membrane) deposited on a solid gold electrode. These two model membranes and electrochemical measurements made it possible to measure the flux of K+ ions in the presence of channel modulators.Copyright © 2023 Elsevier B.V. All rights reserved.
Structures and Dynamics of Anionic Lipoprotein Nanodiscs
Sweeney, Krueger, Sen et al
J Phys Chem B (2022) 126 (15), 2850-2862
Abstract: Nanolipoprotein particles known as nanodiscs (NDs) have emerged as versatile and powerful tools for the stabilization of membrane proteins permitting a plethora of structural and biophysical studies. Part of their allure is their flexibility to accommodate many types of lipids and precise control of the composition. However, little is known about how variations in lipid composition impact their structures and dynamics. Herein, we investigate how the introduction of the anionic lipid POPG into POPC NDs impacts these features. Small-angle X-ray and neutron scattering (SAXS and SANS) of variable-composition NDs are complemented with molecular dynamics simulations to interrogate how increasing the concern of POPG impacts the ND shape, structure of the lipid core, and the dynamics of the popular membrane scaffold protein, MSP1D1(-). A convenient benefit of including POPG is that it eliminates D2O-induced aggregation observed in pure POPC NDs, permitting studies by SANS at multiple contrasts. SAXS and SANS data could be globally fit to a stacked elliptical cylinder model as well as an extension of the model that accounts for membrane curvature. Fitting to both models supports that the introduction of POPG results in strongly elliptical NDs; however, MD simulations predict the curvature of the membrane, thereby supporting the use of the latter model. Trends in the model-independent parameters suggest that increases in POPG reduce the conformational heterogeneity of the MSP1D1(-), which is in agreement with MD simulations that show that the incorporation of sufficient POPG suppresses disengagement of the N-terminal helix from the lipid core. These studies highlight novel structural changes in NDs in response to an anionic lipid and will inform the interpretation of future structural studies of membrane proteins embedded in NDs of mixed lipid composition.
Showing 1-4 of 18 papers.
Powered by BizGenius
 
 
货号/价格
文档
联系电话:
+86 400-682-2521(全国)
010-53681107(北京)
021-50850665(上海)
运输方式
订单邮箱:
order.cn@acrobiosystems.com
技术支持邮箱:
tech.cn@acrobiosystems.com
IL23A & IL12B靶点信息
英文全称:Interleukin-23
中文全称:白细胞介素-23复合体
种类:Homo sapiens
上市药物数量:8详情
临床药物数量:12详情
最高研发阶段:批准上市
查看更多信息
前沿进展
点击查看详细

消息提示

请输入您的联系方式,再点击提交!

确定