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Biotinylated Human STEAP1 Full Length Protein, Avitag™,Flag&His Tag (Detergent)

分子别名(Synonym)

STEAP1, PRSS24, STEAP

表达区间及表达系统(Source)

Biotinylated Human STEAP1 Full Length Protein, Avitag,Flag&His Tag (ST1-H82D3) is expressed from human 293 cells (HEK293). It contains AA Gln 2 - Leu 339 (Accession # Q9UHE8-1).

Predicted N-terminus: Asp

Request for sequence

蛋白结构(Molecular Characterization)

STEAP1 Structure

This protein carries a Flag tag at the N-terminus, and a polyhistidine tag at the C-terminus, followed by an Avi tag (Avitag™). The protein has a calculated MW of 44.7 kDa. The protein migrates as 40-43 kDa and 65-70 kDa when calibrated against Star Ribbon Pre-stained Protein Marker 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.

制剂(Formulation)

This product is not suitable for cell based experiments due to cytotoxicity of detergent.
Detergent buffer is INDISPENSABLE to keep membrane protein soluble and active, under no circumastance should you remove detergent.
Detergent buffer is sold separately and not included in protein, and please contact us if you need the buffer.
If glycerol is not compatible to your application, remove glycerol just before immediate experiment, and NEVER store glycerol-free protein solution.

Supplied as 0.2 μm filtered solution in 50 mM HEPES, 150 mM NaCl, Buffer A, pH7.5 with glycerol as protectant.

Contact us for customized product form or formulation.

运输(Shipping)

This product is supplied and shipped with dry ice, please inquire the shipping cost.

存储(Storage)

Please avoid repeated freeze-thaw cycles.

This product is stable after storage at:

  1. The product MUST be stored at -70°C or lower upon receipt;
  2. -70°C for 3 months under sterile conditions.

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
*The detergent Buffer A (Cat. No. DN-12) is sold separately and not included in protein, you can follow this link for product information.
 

电泳(SDS-PAGE)

STEAP1 SDS-PAGE

Biotinylated Human STEAP1 Full Length Protein, Avitag,Flag&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% (With Star Ribbon Pre-stained Protein Marker).

 

活性(Bioactivity)-ELISA

STEAP1 ELISA

Immobilized Biotinylated Human STEAP1 Full Length Protein, Avitag,Flag&His Tag (Cat. No. ST1-H82D3) at 1 μg/mL (100 μL/well) on streptavidin (Cat. No. STN-N5116) precoated (0.5 μg/well) plate can bind Anti-STEAP1 Antibody with a linear range of 0.002-0.156 μg/mL (QC tested).

Protocol

 

活性(Bioactivity)-SPR

STEAP1 SPR

Anti-STEAP1 Antibody captured on Protein A Chip can bind Biotinylated Human STEAP1 Full Length Protein, Avitag,Flag&His Tag (Cat. No. ST1-H82D3) with an affinity constant of 12.8 nM as determined in a SPR assay (in presence of DDM and CHS) (Biacore 8K) (Routinely tested).

Protocol

 

活性(Bioactivity)-BLI

STEAP1 BLI

Loaded Anti-STEAP1 Antibody on Protein A Biosensor, can bind Biotinylated Human STEAP1 Full Length Protein, Avitag,Flag&His Tag (Cat. No. ST1-H82D3) with an affinity constant of 8.26 nM as determined in BLI assay (in presence of DDM and CHS) (ForteBio Octet R8) (Routinely tested).

Protocol

 
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背景(Background)

Six-transmembrane epithelial antigen of the prostate 1 (STEAP1) is an integral membrane protein that is highly up-regulated on the cell surface of several human cancers, making it a promising therapeutic target to manage these diseases. It shares sequence homology with three enzymes (STEAP2-STEAP4) that catalyze the NADPH-dependent reduction of iron(III). Taking into account its high specificity and overexpression in human cancers, STEAP1 is nowadays a promising candidate to be imposed as a therapeutic target.

 

前沿进展

Design, Synthesis and Anti-Influenza Virus Activity of 4-Tert-Butyl-N-(3-Oxo-1-Thia-4-Azaspiro[4.5]Dec-4-yl)Benzamide Derivatives That Target Hemagglutinin-Mediated Fusion
Çınar, Alikadıoğlu, Soylu-Eter et al
Drug Dev Res (2025) 86 (2), e70080
Abstract: Hemagglutinin (HA) is a viral glycoprotein that mediates influenza virus entry into the host cell and is considered a relevant viral target. We here report the identification of a class of 4-tert-butylphenyl-substituted spirothiazolidinones as HA-mediated fusion inhibitors with specific activity against influenza A/H3N2 virus. The novel spirocyclic compounds were achieved by using one-pot cyclocondensation method and the chemical structures were characterized by IR, 1H NMR, 13C NMR, and elemental analysis. Compound 2c, bearing methyl substitutions at positions 2- and 8- of the spiro ring displayed an EC50 value against influenza A/H3N2 virus of 1.3 μM and an antiviral selectivity index of 30. The fusion-inhibiting effect of compound 2c was revealed in the polykaryon assay which is based on cell-cell fusion when influenza virus H3 HA-transfected cells are exposed to low pH. Computer-aided docking was performed to predict the possible binding pocket in the H3 HA trimer. Resistance data and in silico studies indicated that compound 2c has an overlapping binding pocket in the stem region of H3 HA with the known fusion inhibitors TBHQ and arbidol.© 2025 The Author(s). Drug Development Research published by Wiley Periodicals LLC.
Modulation of lipid nanoparticle-formulated plasmid DNA drives innate immune activation promoting adaptive immunity
Tursi, Tiwari, Bedanova et al
Cell Rep Med (2025)
Abstract: Nucleic acid vaccines have grown in importance over the past several years, with the development of new approaches remaining a focus. We describe a lipid nanoparticle-formulated DNA (DNA-LNP) formulation which induces robust innate and adaptive immunity with similar serological potency to mRNA-LNPs and adjuvanted protein. Using an influenza hemagglutinin (HA)-encoding construct, we show that priming with our HA DNA-LNP demonstrated stimulator of interferon genes (STING)-dependent upregulation and activation of migratory dendritic cell (DC) subpopulations. HA DNA-LNP induced superior antigen-specific CD8+ T cell responses relative to mRNA-LNPs or adjuvanted protein, with memory responses persisting beyond one year. In rabbits immunized with HA DNA-LNP, we observed immune responses comparable or superior to mRNA-LNPs at the same dose. In an additional model, a SARS-CoV-2 spike-encoding DNA-LNP elicited protective efficacy comparable to spike mRNA-LNPs. Our study identifies a platform-specific priming mechanism for DNA-LNPs divergent from mRNA-LNPs or adjuvanted protein, suggesting avenues for this approach in prophylactic and therapeutic vaccine development.Copyright © 2025 The Authors. Published by Elsevier Inc. All rights reserved.
Electro-active evanescent-wave cavity ring-down spectroscopy immunosensor for influenza virus detection
Alnaanah, Qatamin, Mendes et al
Biomed Opt Express (2025) 16 (3), 982-994
Abstract: The early and accurate detection of viral pathogens is critical for effective disease management and public health safety. This study introduces an immunosensor that integrates an electro-active evanescent-wave cavity ring-down spectroscopy (EW-CRDS) platform with a sandwich-type bioassay for label-free detection of the influenza A (H5N1) hemagglutinin (HA) protein, achieving a detection limit of 15 ng/mL. The sensor is constructed by functionalizing the EW-CRDS platform within a micro-electrochemical flow cell with a monoclonal antibody specific to the target antigen. Upon antigen binding, a secondary polyclonal antibody conjugated with a redox-active methylene blue dye is captured. This dye undergoes reversible optical signal changes during redox transitions, which are electrochemically modulated and detected with high sensitivity. Unlike conventional approaches, this sensor employs electrochemical modulation to amplify surface-specific optical signals while reducing processing time and minimizing background noise. The results demonstrate the potential of this technology for real-time monitoring and rapid, reliable diagnosis of infectious diseases, offering excellent sensitivity and ease of operation in detecting influenza viruses. This work highlights the promise of the electro-active EW-CRDS platform for antigen detection in clinical settings.© 2025 Optica Publishing Group.
Pathogenicity and transmissibility of bovine-derived HPAI H5N1 B3.13 virus in pigs
Kwon, Trujillo, Carossino et al
bioRxiv (2025)
Abstract: Since the first emergence of highly pathogenic avian influenza (HPAI) H5N1 viruses in dairy cattle, the virus has continued to spread, reaching 17 states and at least 970 dairy herds in the United States. Subsequently, spillovers of the virus from dairy cattle to humans have been reported. Pigs are an important reservoir in influenza ecology because they serve as a mixing vessel in which novel reassortant viruses with pandemic potential can be generated. Here, we show that oro-respiratory infection of pigs resulted in productive replication of a bovine-derived HPAI H5N1 B3.13 virus. Infectious virus was mainly identified in the lower respiratory tract of principal infected pigs, and sero-conversion was observed in most of the principal pigs at later time points. In one animal, we detected the emergence of a mutation in hemagglutinin (HA) previously associated with increased affinity for "mammalian-type" α2,6-linked sialic acid receptors, but this mutation did not reach consensus levels. Sentinel contact pigs remained sero-negative throughout the study, indicating lack of transmission. The results support that pigs are susceptible to a bovine-derived HPAI H5N1 B3.13 virus, but this virus did not replicate as robustly in pigs as mink-derived HPAI H5N1 and swine-adapted influenza viruses.
Showing 1-4 of 4977 papers.
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STEAP1靶点信息
英文全称:Six-transmembrane epithelial antigen of the prostate 1
中文全称:前列腺六跨膜上皮抗原1
种类:Homo sapiens
上市药物数量:0详情
临床药物数量:6详情
最高研发阶段:临床三期
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