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AB54100

重组Hepatitis A Virus蛋白

Recombinant Hepatitis A Virus protein

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Recombinant Hepatitis A Virus protein is a Human hepatitis A virus Hu/Los Angelos/LA/1975 Fragment protein, in the 722 to 830 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, ELISA, WB.

查看别名

Genome polyprotein

关键信息

纯度

>90% SDS-PAGE

表达系统

Escherichia coli

标签

His tag C-Terminus

应用

ELISA, SDS-PAGE, WB

applications

生物活性

No

访问

P06441

不含动物源

No

不含载体蛋白

No

种属

Human hepatitis A virus Hu/Los Angelos/LA/1975

存储溶液

pH: 9.6 Constituents: 50% Glycerol (glycerin, glycerine), 9.009% Urea, 0.158% Tris HCl

storage-buffer

反应性数据

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "ELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

产品详情

Reacts strongly with human Hepatitis A Virus positive serum.

序列信息

[{"sequence":"","proteinLength":"Fragment","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":830,"aminoAcidStart":722,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"P06441","tags":[{"tag":"His","terminus":"C-Terminus"}]}]

性能和储存信息

运输条件
Blue Ice
推荐的短期储存时间
1-2 weeks
推荐的短期储存条件
+4°C
推荐的长期储存条件
-20°C
分装信息
Upon delivery aliquot
储存信息
Avoid freeze / thaw cycle
False

补充信息

This supplementary information is collated from multiple sources and compiled automatically.

The Hepatitis A Virus (HAV) is a small non-enveloped virus belonging to the Picornaviridae family. It possesses a single-stranded RNA genome that measures about 7.5 kilobases in length. The capsid of HAV with a mass around 27 kDa consists of proteins VP1 VP2 and VP3 which form a protective shell that facilitates the virus's stability and transmission. This virus is primarily found in the liver where it causes infection although it can also circulate in the bloodstream and be excreted in the feces.
Biological function summary

HAV plays a significant role in human health by causing liver inflammation. It does not form complexes with other proteins but its replication predominantly occurs in hepatocytes. Although HAV is not directly involved in forming complexes it effectively interacts with host cell machinery to produce viral proteins and new viral particles. These interactions ensure the virus thrives in a new environment by altering the cell's normal functions to favor its replication.

Pathways

HAV significantly influences immune response and inflammation pathways. The virus triggers these pathways to counter the body's antiviral defenses leading to liver inflammation and damage. During the infection HAV interacts with host proteins such as those regulating the interferon response potentially altering their normal biological roles. These interactions can modulate the signaling further complicating the immune response and enhancing viral replication.

HAV is most associated with acute hepatitis a liver disease characterized by jaundice fatigue and fever. The immune response exacerbates liver damage as the body attempts to clear the virus. Unlike some other hepatotropic viruses HAV does not cause chronic liver disease. The interaction of HAV with proteins involved in the inflammatory response such as cytokines exacerbates symptoms and impacts disease progression.

特殊说明

形式

Liquid

常规信息

功能

Capsid protein VP1. Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell.. Capsid protein VP2. Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell.. Capsid protein VP3. Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell.. Capsid protein VP0. VP0 precursor is a component of the immature procapsids.. Capsid protein VP4. Plays a role in the assembly of the 12 pentamers into an icosahedral structure. Has not been detected in mature virions, supposedly owing to its small size.. Protein VP1-2A. Precursor component of immature procapsids that corresponds to an extended form of the structural protein VP1. After maturation, possibly by the host Cathepsin L, the assembly signal 2A is cleaved to give rise to the mature VP1 protein.. Protein 2B. Functions as a viroporin. Affects membrane integrity and causes an increase in membrane permeability. Involved in host intracellular membrane rearrangements probably to give rise to the viral factories. Does not disrupt calcium homeostasis or glycoprotein trafficking. Antagonizes the innate immune response of the host by suppressing IFN-beta synthesis, which it achieves by interfering with the RIG-I/IFIH1 pathway.. Protein 2BC. Affects membrane integrity and causes an increase in membrane permeability.. Protein 2C. Associates with and induces structural rearrangements of intracellular membranes. Displays RNA-binding activity.. Protein 3ABC. The precursor 3ABC is targeted to the mitochondrial membrane where protease 3C activity cleaves and inhibits the host antiviral protein MAVS, thereby disrupting activation of IRF3 through the IFIH1/MDA5 pathway. In vivo, the protease activity of 3ABC precursor is more efficient in cleaving the 2BC precursor than that of protein 3C. The 3ABC precursor may therefore play a role in the proteolytic processing of the polyprotein. Possible viroporin.. Protein 3AB. Interacts with the 3CD precursor and with RNA structures found at both the 5'- and 3'-termini of the viral genome. Since the 3AB precursor contains the hydrophobic domain 3A, it probably anchors the whole viral replicase complex to intracellular membranes on which viral RNA synthesis occurs.. Protein 3A. May serve as membrane anchor to the 3AB and 3ABC precursors via its hydrophobic domain. May interact with RNA.. Viral protein genome-linked. Acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome.. Protease 3C. Cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind cooperatively to the protease. Cleaves IKBKG/NEMO to impair innate immune signaling. Cleaves host PABPC1 which may participate in the switch of viral translation to RNA synthesis.. Protein 3CD. Interacts with the 3AB precursor and with RNA structures found at both the 5'- and 3'-termini of the viral genome. Disrupts TLR3 signaling by degrading the host adapter protein TICAM1/TRIF.. RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals.

序列相似性

Belongs to the picornaviridae polyprotein family.

翻译后修饰

Genome polyprotein. Specific enzymatic cleavages by viral protease in vivo yield a variety of precursors and mature proteins. Polyprotein processing intermediates are produced, such as P1-2A which is a functional precursor of the structural proteins, VP0 which is a VP4-VP2 precursor, VP1-2A precursor, 3ABC precursor which is a stable and catalytically active precursor of 3A, 3B and 3C proteins, 3AB and 3CD precursors. The assembly signal 2A is removed from VP1-2A by a host protease, possibly host Cathepsin L. This cleavage occurs over a region of 3 amino-acids probably generating VP1 proteins with heterogeneous C-termini.. Capsid protein VP0. During virion maturation, immature virions are rendered infectious following cleavage of VP0 into VP4 and VP2. This maturation seems to be an autocatalytic event triggered by the presence of RNA in the capsid and is followed by a conformational change of the particle.. Protein VP1-2A. The assembly signal 2A is removed from VP1-2A by a host protease, possibly host Cathepsin L in naked virions. This cleavage does not occur in enveloped virions. This cleavage occurs over a region of 3 amino-acids probably generating VP1 proteins with heterogeneous C-termini.. Viral protein genome-linked. VPg is uridylylated prior to priming replication into VPg-pUpU.. Capsid protein VP4. Unlike other picornaviruses, does not seem to be myristoylated.

亚细胞定位

Host endosome

产品实验方案

靶点信息

Capsid protein VP1. Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell.. Capsid protein VP2. Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell.. Capsid protein VP3. Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell.. Capsid protein VP0. VP0 precursor is a component of the immature procapsids.. Capsid protein VP4. Plays a role in the assembly of the 12 pentamers into an icosahedral structure. Has not been detected in mature virions, supposedly owing to its small size.. Protein VP1-2A. Precursor component of immature procapsids that corresponds to an extended form of the structural protein VP1. After maturation, possibly by the host Cathepsin L, the assembly signal 2A is cleaved to give rise to the mature VP1 protein.. Protein 2B. Functions as a viroporin. Affects membrane integrity and causes an increase in membrane permeability. Involved in host intracellular membrane rearrangements probably to give rise to the viral factories. Does not disrupt calcium homeostasis or glycoprotein trafficking. Antagonizes the innate immune response of the host by suppressing IFN-beta synthesis, which it achieves by interfering with the RIG-I/IFIH1 pathway.. Protein 2BC. Affects membrane integrity and causes an increase in membrane permeability.. Protein 2C. Associates with and induces structural rearrangements of intracellular membranes. Displays RNA-binding activity.. Protein 3ABC. The precursor 3ABC is targeted to the mitochondrial membrane where protease 3C activity cleaves and inhibits the host antiviral protein MAVS, thereby disrupting activation of IRF3 through the IFIH1/MDA5 pathway. In vivo, the protease activity of 3ABC precursor is more efficient in cleaving the 2BC precursor than that of protein 3C. The 3ABC precursor may therefore play a role in the proteolytic processing of the polyprotein. Possible viroporin.. Protein 3AB. Interacts with the 3CD precursor and with RNA structures found at both the 5'- and 3'-termini of the viral genome. Since the 3AB precursor contains the hydrophobic domain 3A, it probably anchors the whole viral replicase complex to intracellular membranes on which viral RNA synthesis occurs.. Protein 3A. May serve as membrane anchor to the 3AB and 3ABC precursors via its hydrophobic domain. May interact with RNA.. Viral protein genome-linked. Acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome.. Protease 3C. Cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind cooperatively to the protease. Cleaves IKBKG/NEMO to impair innate immune signaling. Cleaves host PABPC1 which may participate in the switch of viral translation to RNA synthesis.. Protein 3CD. Interacts with the 3AB precursor and with RNA structures found at both the 5'- and 3'-termini of the viral genome. Disrupts TLR3 signaling by degrading the host adapter protein TICAM1/TRIF.. RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals.
See full target information Genome polyprotein

其他靶点

Hepatitis A Virus,

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