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 >  Protein>EphA10 >EP0-H52H3

Human EphA10 Protein, His Tag

分子别名(Synonym)

Ephrin type-A receptor 10

表达区间及表达系统(Source)

Human EphA10, His Tag (EP0-H52H3) is expressed from human 293 cells (HEK293). It contains AA Pro 27 - Pro 564 (Accession # Q5JZY3-1).

Predicted N-terminus: Pro 27

Request for sequence

蛋白结构(Molecular Characterization)

EphA10 Structure

This protein carries a polyhistidine tag at the C-terminus.

The protein has a calculated MW of 60.2 kDa. The protein migrates as 65-75 kDa 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)

>90% 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 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)

EphA10 SDS-PAGE

Human EphA10, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 90%.

 

活性(Bioactivity)-ELISA

EphA10 ELISA

Immobilized Human EphA10, His Tag (Cat. No. EP0-H52H3) at 5 μg/mL (100 μL/well) can bind Human Ephrin-A3, Fc Tag (Cat. No. EA3-H5258) with a linear range of 0.1-2 ng/mL (QC tested).

Protocol

EphA10 ELISA

Immobilized Human Ephrin-A3, Fc Tag (Cat. No. EA3-H5258) at 5 μg/mL (100 μL/well) can bind Human EphA10, His Tag (Cat. No. EP0-H52H3) with a linear range of 0.005-0.313 μg/mL (Routinely tested).

Protocol

 
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背景(Background)

At present, the proportion of breast cancer, cervical cancer and ovarian cancer in the occurrence of tumors that cause women's death has remained high. EPHA10 belongs to the EPH family, which is the largest known tyrosine kinase family, with 16 members. These members play a normal physiological function after interacting with their ligand Ephrin, and have been studied in sugar metabolism, new tissue construction, angiogenesis and other aspects. EPHA10 gene is located in 1p34 and mainly expressed in testis.

 

前沿进展

Mayaro virus detection by integrating sample preparation with isothermal amplification in portable devices
Alipanah, Manzanas, Hai et al
Anal Bioanal Chem (2023) 415 (23), 5605-5617
Abstract: Mayaro virus (MAYV) is an emerging mosquito-borne alphavirus that causes clinical symptoms similar to those caused by Chikungunya virus (CHIKV), Dengue virus (DENV), and Zika virus (ZIKV). To differentiate MAYV from these viruses diagnostically, we have developed a portable device that integrates sample preparation with real-time, reverse-transcription, loop-mediated isothermal amplification (rRT-LAMP). First, we designed a rRT-LAMP assay targeting MAYV's non-structural protein (NS1) gene and determined the limit of detection of at least 10 viral genome equivalents per reaction. The assay was specific for MAYV, without cross-reactions with CHIKV, DENV, or ZIKV. The rRT-LAMP assay was integrated with a sample preparation device (SPD) wherein virus lysis and RNA enrichment/purification were carried out on the spot, without requiring pipetting, while subsequent real-time amplification device (RAD) enables virus detection at the point of care (POC). The functions of our platform were demonstrated using purified MAYV RNA or blood samples containing viable viruses. We have used the devices for detection of MAYV in as short as 13 min, with limit of detection to as low as 10 GEs/reaction.© 2023. The Author(s), under exclusive licence to Springer-Verlag GmbH, DE part of Springer Nature.
A nonstructural protein 1 capture enzyme-linked immunosorbent assay specific for dengue viruses
Lim, Ramapraba, Loy et al
PLoS One (2023) 18 (5), e0285878
Abstract: Dengue non-structural protein (NS1) is an important diagnostic marker during the acute phase of infection. Because NS1 is partially conserved across the flaviviruses, a highly specific DENV NS-1 diagnostic test is needed to differentiate dengue infection from Zika virus (ZIKV) infection. In this study, we characterized three newly isolated antibodies against NS1 (A2, D6 and D8) from a dengue-infected patient and a previously published human anti-NS1 antibody (Den3). All four antibodies recognized multimeric forms of NS1 from different serotypes. A2 bound to NS1 from DENV-1, -2, and -3, D6 bound to NS1 from DENV-1, -2, and -4, and D8 and Den3 interacted with NS1 from all four dengue serotypes. Using a competition ELISA, we found that A2 and D6 bound to overlapping epitopes on NS1 whereas D8 recognized an epitope distinct from A2 and D6. In addition, we developed a capture ELISA that specifically detected NS1 from dengue viruses, but not ZIKV, using Den3 as the capture antibody and D8 as the detecting antibody. This assay detected NS1 from all the tested dengue virus strains and dengue-infected patients. In conclusion, we established a dengue-specific capture ELISA using human antibodies against NS1. This assay has the potential to be developed as a point-of-care diagnostic tool.Copyright: © 2023 Lim et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Comparative specificity and sensitivity of NS1-based serological assays for the detection of flavivirus immune response
Mora-Cárdenas, Aloise, Faoro et al
PLoS Negl Trop Dis (2020) 14 (1), e0008039
Abstract: Flaviviruses are relevant animal and human pathogens of increasing importance worldwide. The similarities of the initial clinical symptoms and the serological cross-reactivity of viral structural antigens make a laboratory diagnosis of flavivirus infection problematic. The main aim of the present study was the comparative specificity and sensitivity analysis of the non-structural protein NS1 as an antigen to detect flavivirus antibodies in sera from exposed individuals. A strategy for the purification of native recombinant non-structural protein 1 of representative flaviviruses including tick-borne encephalitis, West Nile, Zika and dengue virus was developed. The immunological properties of the purified antigens were analyzed using sera of immunized mice and of infected individuals in comparison with standard commercial assays. Recombinant NS1 protein was confirmed as a valuable option for the detection of flavivirus antibodies with reduced cross-reactivity and high sensitivity offering additional advantages for the detection of vaccine breakthrough cases.
Human antibodies targeting Zika virus NS1 provide protection against disease in a mouse model
Bailey, Duehr, Dulin et al
Nat Commun (2018) 9 (1), 4560
Abstract: Zika virus is a mosquito-borne flavivirus closely related to dengue virus that can cause severe disease in humans, including microcephaly in newborns and Guillain-Barré syndrome in adults. Specific treatments and vaccines for Zika virus are not currently available. Here, we isolate and characterize four monoclonal antibodies (mAbs) from an infected patient that target the non-structural protein NS1. We show that while these antibodies are non-neutralizing, NS1-specific mAbs can engage FcγR without inducing antibody dependent enhancement (ADE) of infection in vitro. Moreover, we demonstrate that mAb AA12 has protective efficacy against lethal challenges of African and Asian lineage strains of Zika virus in Stat2-/- mice. Protection is Fc-dependent, as a mutated antibody unable to activate known Fc effector functions or complement is not protective in vivo. This study highlights the importance of the ZIKV NS1 protein as a potential vaccine antigen.
Showing 1-4 of 6 papers.
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EphA10靶点信息
英文全称:Ephrin type-A receptor 10
中文全称:肝配蛋白受体A10
种类:
上市药物数量:0详情
临床药物数量:0详情
最高研发阶段:临床前
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