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 >  Protein>HLA-A*0201 | B2M | HBV >HLT-H82E9

Biotinylated Human HLA-A*02:01&B2M&HBV (FLLTRILTI) Complex Protein (Monomer, MALS verified)

更有Streptavidin Protein-PESTN-NP117STN-NP119)快速支持您想要的MHC Tetramer组装!

分子别名(Synonym)

HLA-A*0201 | B2M | HBV

表达区间及表达系统(Source)

Biotinylated Human HLA-A*02:01&B2M&HBV (FLLTRILTI) Complex Protein (HLT-H82E9) is expressed from human 293 cells (HEK293). It contains AA Gly 25 - Ile 308 (HLA-A*02:01) & Ile 21 - Met 119 (B2M) & FLLTRILTI peptide (Accession # AAA59606.1 (HLA-A*02:01) & P61769-1 (B2M) & FLLTRILTI).

Predicted N-terminus: Gly 25 & Ile 21

Request for sequence

蛋白结构(Molecular Characterization)

Biotinylated Human HLA-A*02:01&B2M&HBV (FLLTRILTI) Complex Protein is produced by co-expression of HLA and B2M loaded with HBV peptide.

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

The protein has a calculated MW of 36.3 kDa and 11.7 kDa. The protein migrates as 40-42 kDa and 14 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.

>95% as determined by SEC-MALS.

制剂(Formulation)

Supplied as 0.2 μm filtered solution in PBS, pH7.4 with trehalose 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
 

电泳(SDS-PAGE)

HLA-A*0201 | B2M | HBV SDS-PAGE

Biotinylated Human HLA-A*02:01&B2M&HBV (FLLTRILTI) Complex Protein 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

HLA-A*0201 | B2M | HBV SEC-MALS

The purity of Biotinylated Human HLA-A*02:01&B2M&HBV (FLLTRILTI) Complex Protein (Cat. No. HLT-H82E9) is more than 95% and the molecular weight of this protein is around 46-56 kDa verified by SEC-MALS.

Report

 

活性(Bioactivity)-ELISA

HLA-A*0201 | B2M | HBV ELISA

Immobilized Biotinylated Human HLA-A*02:01&B2M&HBV (FLLTRILTI) Complex Protein (Cat. No. HLT-H82E9) at 1 μg/mL (100 μL/well) on streptavidin (Cat. No. STN-N5116) precoated (0.5 μg/well) plate can bind Anti-HLA class I Antibody, Human IgG1 (W6/32) with a linear range of 0.1-1 ng/mL (QC tested).

Protocol

HLA-A*0201 | B2M | HBV ELISA

Immobilized Biotinylated Human HLA-A*02:01&B2M&HBV (FLLTRILTI) Complex Protein (Cat. No. HLT-H82E9) at 1 μg/mL (100 μL/well) on streptavidin (Cat. No. STN-N5116) precoated (0.5 μg/well) plate can bind Anti-B2M Antibody, Human IgG1 with a linear range of 0.1-2 ng/mL (Routinely tested).

Protocol

 
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背景(Background)

Hepatitis B is a potentially life-threatening liver infection caused by the hepatitis B virus (HBV). The hepatitis B virus attacks the liver and can cause both acute and chronic diseases that put people at high risk of death from cirrhosis and liver cancer. The virus is most commonly transmitted from mother to child during birth and delivery, as well as through contact with blood or other body fluids. Hepatitis B virus (HBV) is a member of the hepadnaviral family. The virus particle (virion) consists of an outer lipid envelope and an icosahedral nucleocapsid core composed of the core protein. The nucleocapsid encloses the viral D and a D polymerase that has reverse transcriptase activity. The outer envelope contains embedded proteins that are involved in viral binding of, and entry into, susceptible cells. The surface antigens (HBsAg) decorating the lipid envelope of HBV are produced in excess during the life cycle of the virus, and its presence in blood indicates current hepatitis B infection. The Human HLA-A*0201 HBV ( FLLTRILTI) complex protein is a complex of HLA-A*0201 of the MHC Class I, B2M, and FLLTRILTI peptide of the HBV.

 

前沿进展

Characterization of a new mutation of mitochondrial ND6 gene in hepatocellular carcinoma and its effects on respiratory complex I
Bazzani, Kundnani, Redin et al
Sci Rep (2025) 15 (1), 10925
Abstract: Hepatocellular carcinoma (HCC) is the most common form of liver cancer, which often arises from previous liver pathologies such as HBV, HCV, and alcohol abuse. It is typically associated with an enlarged cirrhotic organ. In this study, we analyzed tumor and distal tissues from a patient who underwent liver resection for HCC with no previous pathologies and whose liver showed normal function without signs of cirrhosis. Genetic analysis of mitochondrial DNA (mtDNA) revealed a novel variant of the gene encoding the NADH dehydrogenase subunit 6 (ND6) protein in the tumor tissue. The deletion of a thymidine generated an early stop codon, resulting in a truncated form of the protein (ΔND6) with 50% of the C-terminal primary sequence missing. ND6 is a subunit of the NADH dehydrogenase complex, also known as Complex I, the largest complex in the electron transport chain. Previous studies have linked mtDNA Complex I mutations to mitochondrial disorders and cancer. Through biochemical analyses, we characterized this new mutation and showed that the expression of ΔND6 negatively affects the stability and functionality of Complex I. Data were confirmed by molecular dynamics simulations suggesting conformational rearrangements, overall revealing a leading role of ND6 in the assembly of Complex I.© 2025. The Author(s).
Circulating let-7 Predicts Hepatic Fibrogenesis of 12-Month Post-Nucleos(t)ide Analog Treatment in Patients With Hepatitis B Virus
Tsai, Liang, Lin et al
Kaohsiung J Med Sci (2025)
Abstract: Chronic hepatitis B virus (HBV) infection is associated with potential complications of liver cirrhosis and hepatocellular carcinoma. To date, there are no effective and noninvasive clinical markers that can predict the risk of liver fibrosis early and accurately in chronic hepatitis B (CHB) patients treated with nucleos(t)ide analogs (NAs). This study aimed to investigate the association of circulating let-7b/c/g levels with the severity of hepatic fibrosis with a FIB-4 index of 1.5-2.9 in CHB patients. We conducted a retrospective longitudinal study in patients with CHB after 6 months of NAs therapy to investigate whether serum let-7b/c/g levels can be monitored as an early biomarker for liver fibrogenesis based on multivariate logistic regression analyses. We also used the hepatic stellate cell line LX-2 treated with transforming growth factor-β (TGF-β) to evaluate the suppression effect of let-7b/c/g on hepatic fibrogenesis. The study showed that circulating let-7b/c/g could predict 12 months of antiviral treatment for HBV-related significant fibrosis (FIB-4 index ≥ 2.9) at baseline and was significantly negatively correlated with the FIB-4 score. Moreover, let-7b/c/g could directly target the TGF-βR1-3' untranslated region (3' UTR) and inhibit TGF-β induced p-SMAD2 phosphorylation to reduce α-smooth muscle actin levels, a fibrogenesis marker in LX-2 cells. These results confirm that let-7b/c/g could be a biomarker for monitoring HBV-induced fibrogenesis.© 2025 The Author(s). The Kaohsiung Journal of Medical Sciences published by John Wiley & Sons Australia, Ltd on behalf of Kaohsiung Medical University.
Bilirubin metabolism in the liver orchestrates antiviral innate immunity in the body
Du, He, Chen et al
Cell Rep (2025) 44 (4), 115481
Abstract: Bilirubin metabolism crucially maintains normal liver function, but whether it contributes to antiviral immunity remains unknown. Here, we reveal that the liver bilirubin metabolic pathway facilitates antiviral innate immunity of the body. We discovered that viral infection upregulates uridine diphosphate glucuronosyltransferase 1A1 (UGT1A1) expression in the liver, which in turn stabilizes IRF3 proteins to promote type I interferon (IFN-I) production. Moreover, we found that serum unconjugated bilirubin (UCB), a unique physiological substrate of UGT1A1, can competitively inhibit the binding of IFN-I to IFN-I receptor 2 (IFNAR2), thus attenuating IFN-I-induced antiviral signaling of the body. Accordingly, effective bilirubin metabolism in the liver promotes antiviral immunity of the body by specifically employing liver UGT1A1-mediated enhancement of IFN-I production and reducing serum bilirubin-mediated inhibition of IFN-I signaling. This study uncovers the significance of bilirubin metabolism in antiviral innate immunity and demonstrates that conventional IFN-I therapy is less efficient for patients with hepatitis B virus (HBV) with high levels of bilirubin.Copyright © 2025 The Author(s). Published by Elsevier Inc. All rights reserved.
Chimeric hBPI23-Fcγ protein shows bactericidal activity against drug-resistant Gram-negative bacteria and protects mice from lethal challenge
Ma, Wang, Huang et al
Arch Microbiol (2025) 207 (5), 103
Abstract: The antimicrobial peptides, such as host immune system-derived human bactericidal/permeability-increasing protein (hBPI), are the potential drugs for antibiotic-resistant Gram-negative bacterial infection. However, whether the purified chimeric hBPI23-Fcγ protein has bactericidal activity against drug-resistant Gram-negative bacteria (GNB) and the relevant mechanisms have not been fully elucidated. In this study, the chimeric hBPI23-Fcγ protein, which consisting of the functional N terminus of BPI and Fcγ1, were expressed and purified in a lab-scale. The chimeric hBPI23-Fcγ protein showed longer half-life up to 148.2 min in vivo. The hBPI23-Fcγ protein also showed significant bactericidal activity against standard and clinically isolated drug-resistant Acinetobacter baumannii (A. baumannii) and Escherichia coli (E. coli). In addition, the hBPI23-Fcγ protein markedly decreased biofilm formation, neutralized bacterial lipopolysaccharides (endotoxin) and enhanced the opsonization of phagocytes, as well as significantly improved the survival rate of minimal lethal dose (MLD) of drug-resistant E. coli -infected mice. These results indicate that the BPI23-Fcγ protein protected mice from drug-resistant GNB infection not only by direct bactericidal effect, but also by promoting opsonophagocytosis of macrophages. In conclusion, the chimeric BPI23-Fcγ protein may be as a promising candidate of non-antibiotic biological agent for drug-resistant GNB infection.© 2025. The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature.
Showing 1-4 of 56144 papers.
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