Specifications
Immunogen
Hepatitis B surface antigen
Applications
Application Notes
ELISA: 1/20 - 1/200; IF: 1/10 - 1/50; Western Blot: 1/10 - 1/50
Target
Alternative Names
HBsAg; HBV major surface antigen; HBV surface antigen; Hepatitis B Virus major surface antigen; Major surface antigen; S; Hepatitis B Surface Antigen; Hepatitis B Virus Surface Antigen;?Hepadnaviridae; Orthohepadnavirus; Hepatitis B virus; HBV
Citations
Publication ()
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Hepatitis B Virus Small Envelope Protein Promotes Hepatocellular Carcinoma Angiogenesis via Endoplasmic Reticulum Stress Signaling To Upregulate the Expression of Vascular Endothelial Growth Factor A
Wu SX, Ye SS, Hong YX, Chen Y, Wang B, Lin XJ, Lin X.
Applications: IHC
Reactive species: Mouse
"Abstract: Hepatocellular carcinoma (HCC) is a hypervascular tumor, and accumulating evidence has indicated that stimulation of angiogenesis by hepatitis B virus (HBV) may contribute to HCC malignancy. The small protein of hepatitis B virus surface antigen (HBsAg), SHBs, is the most abundant HBV protein and has a close clinical association with HCC; however, whether SHBs contributes to HCC angiogenesis remains unknown. This study reports that the forced expression of SHBs in HCC cells promoted xenograft tumor growth and increased the microvessel density (MVD) within the tumors. Consistently, HBsAg was also positively correlated with MVD counts in HCC patients' specimens. The conditioned media from the SHBs-transfected HCC cells increased the capillary tube formation and migration of human umbilical vein endothelial cells (HUVECs). Intriguingly, the overexpression of SHBs increased vascular endothelial growth factor A (VEGFA) expression at both the mRNA and protein levels."
Article snippet: The membrane was blocked for 1 h with Tris-buffered saline (TBS)–Tween 20 (50mmol/L Tris, 160mmol/L NaCl, 0.1% Tween 20 [pH 7.8]) containing 5% bovine serum albumin (BSA), and all subsequent steps were done in this buffer, followed by incubation overnight at 4°C with primary antibodies against HBsAg (Creative-Diagnostics, NY, USA). 
Figure 1. Immunochemical staining of HBsAg and VEGFA in HCC tissues (n=20).
Hepatitis B Surface Antigen Activates Unfolded Protein Response in Forming Ground Glass Hepatocytes of Chronic Hepatitis B
Yao Li, Yuchen Xia, Xiaoming Cheng, David E Kleiner, Stephen M Hewitt, Julia Sproch, Tong Li, Hui Zhuang, T Jake Liang
Applications: WB
Reactive species: Recombinant adenovirus (AdV) generated by inserting 1.3× full-length HBV genome, or genes encoding SHBsAg, HBeAg, HBcAg and HBx
"Abstract: Ground glass hepatocytes (GGHs), a histological hallmark of chronic hepatitis B virus (HBV) infection, contain excessive hepatitis surface antigen (HBsAg) in the endoplasmic reticulum (ER), which is linked to unfolded protein response (UPR). The mechanism by which HBV activates UPR has not been fully defined. To investigate this, HepG2-NTCP cells and primary human hepatocytes (PHHs) were either infected with HBV or transduced with adenoviral vectors expressing replication-competent HBV genome or individual HBV genes. UPR markers were evaluated by qPCR, Western blotting, and immunofluorescence. Apoptosis and cell viability were measured by Caspase-3/7 and ATPlite assay respectively. We found that UPR markers were induced by the overexpression of HBsAg in HepG2-NTCP cells and PHHs. Elevation of UPR-induced genes showed a dose-dependent correlation with HBsAg levels. In HBV-infected livers, GGHs also demonstrated excessive accumulation of HBsAg associated with increased BIP/GRP78 staining, a marker of UPR. Prolonged activation of UPR by HBsAg overexpression induced signs of apoptosis. Overexpression of HBsAg can induce ER stress through protein kinase RNA-like endoplasmic reticulum kinase (PERK) pathway in vitro, and may be linked to the appearance of GGHs. The activation of UPR by HBsAg may sensitize hepatocytes to cell death and result in possible subsequent cellular changes leading to a premalignant phenotype."
Article snippet: Antibodies against BIP/GRP78 (*), HBsAg (Creative-Diagnostics, Shirley, NY, USA) and GAPDH (*) were used for Western blot. 
Figure 1. Expression of HBsAg and BIP/GRP78 were determined by Western blotting in AdVs-transduced HepG2-NTCP cells
Ubiquitin-dependent proteasomal degradation of small hepatitis B virus surface antigen mediated by TRIM21 and antagonized by OTUD4
Wu S, Chen Z, Zhang Z, Xu J, Li H, Lin M, Xie W, Chen Y, Lin X, Lin X. Ubiquitin-dependent proteasomal degradation of small hepatitis B virus surface antigen mediated by TRIM21 and antagonized by OTUD4.
Applications: WB
Reactive species: HBV
"Abstract: The small hepatitis B surface antigen (SHBs) is the most abundant hepatitis B virus (HBV) protein in individuals infected with HBV, and clearance of HBV surface antigen, which is primarily composed of SHBs, is considered a surrogate biomarker for achieving a functional cure of chronic HBV. Understanding SHBs degradation is crucial for its elimination and targeted eradication strategies. This study demonstrates that SHBs undergoes degradation via a ubiquitin/proteasome pathway, primarily through K48-linked ubiquitination, with K122 as the critical ubiquitination site. Utilizing immunoprecipitation and mass spectrometry, we identified TRIM21 (an E3 ubiquitin ligase) and OTUD4 (a deubiquitinase) as key regulators of SHBs. We verified the direct interaction between SHBs and TRIM21's coiled-coil domain, as well as the N-terminal amino acids 1-180 of OTUD4, using coimmunoprecipitation and glutathione S-transferase (GST) pull-down assays in both in vivo and in vitro settings. TRIM21 was observed to reduce SHBs stability and abundance by promoting its polyubiquitination, whereas OTUD4 acted to negate the effects of TRIM21-induced polyubiquitination, thereby stabilizing and increasing the levels of SHBs. Notably, TRIM21-mediated degradation of SHBs substantially impaired subviral particle and virion production and its biological activities such as migratory and angiogenic capabilities, opposite to the effect produced by the introduction of OTUD4. These findings suggest that TRIM21 and OTUD4 modulate SHBs protein stability and function through a ubiquitination-dependent proteasomal pathway, offering new insights into clearing SHBs and intervening in the progression of HBV-related liver diseases.IMPORTANCEThe small hepatitis B surface antigen (SHBs) is a key structural component of the hepatitis B virus (HBV) virion and subviral particles and is the most abundant HBV protein in individuals with chronic infection. Gaining a better understanding of its degradation pathways may help inform strategies to reduce SHBs levels and potentially support the design of targeted therapies. However, the specific mechanisms and processes involved in the degradation of SHBs remain largely unexplored. This study reveals that SHBs is degraded via the ubiquitin/proteasome pathway, specifically through K48-linked ubiquitination at the K122 site. TRIM21 promotes SHBs degradation by enhancing its polyubiquitination, while OTUD4 stabilizes SHBs by counteracting TRIM21's effects. TRIM21 reduces SHBs stability, subviral particle and virion production, and its related biological activities, whereas OTUD4 stabilizes SHBs, promoting its accumulation. These findings highlight the roles of TRIM21 and OTUD4 in regulating SHBs stability and function, offering new insights into potential interventions for HBV-related liver diseases."
Article snippet: Membranes were blocked with Tris-buffered saline (TBS)-Tween 20 containing 5% bovine serum albumin (BSA) and incubated overnight at 4°C with primary antibodies against HBsAg (Creative-Diagnostics, #DMABT-51328MH)*** 
Figure 1. Analysis of K48-linked polyubiquitination of HBsAg by immunoprecipitation and immunoblotting.
SHBs Mitigates Sorafenib‐Induced Apoptosis in Hepatocellular Carcinoma via Activation of RAF1/MEK/ERK Signaling Pathway
Wu S, Hong Y, Li H, Lin M, Lin X, Lin X, Lin X
Applications: Immunoprecipitation
Reactive species: HBV
"Abstract: Hepatocellular carcinoma (HCC) is one of the most prevalent cancers worldwide, with a significant association to hepatitis B virus (HBV) infection, which has been shown to drive HCC progression. Sorafenib, a multi-kinase inhibitor, is the first-line treatment for advanced HCC. However, recent studies indicate that HBV infection may confer resistance to sorafenib treatment. The small hepatitis B surface antigen (SHBs), the most abundant HBV viral protein, has been implicated in HCC development, yet its role in sorafenib resistance is unclear. This study demonstrates that SHBs promotes sorafenib resistance in HCC cells and xenograft models by inhibiting apoptosis. Upon sorafenib treatment, SHBs expression was found to enhance the RAF1/MEK/ERK signaling pathway, as evidenced by increased phosphorylation of ERK and MEK. Inhibition of ERK activity with U0126 countered SHBs effects on sorafenib-induced apoptosis, cleaved caspase-3, and cellular proliferation. Mechanistically, SHBs binds to protein tyrosine phosphatase non-receptor type 1 (PTPN1), enhancing its phosphorylation, which subsequently dephosphorylates the protein tyrosine phosphatase interacting protein 51 (PTPIP51). This dephosphorylation promotes RAF1 recruitment to the 14-3-3β complex, leading to activation of the RAF1/MEK/ERK pathway. These findings suggest that SHBs prevents sorafenib-induced apoptosis in HCC cells by binding to PTPN1 and stimulating the formation of the PTPIP51/14-3-3β/RAF1 complex, thereby activating the RAF1/MEK/ERK signaling pathway. This mechanism provides insight into HBV-induced sorafenib resistance in HCC, highlighting SHBs as a potential target for overcoming treatment resistance in HBV-related HCC."
Article snippet: anti-SHBs (DMABT-51328MH; Creative Diagnostics) from Creative Diagnostics 
Figure 1. SHBs interacts with PTPN1.
COA
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