Recombinant Rubella Virus spike glycoprotein E1 protein (Fc Chimera) is a Rubella virus strain Therien Fragment protein, in the 583 to 1025 aa range, expressed in HEK 293, with >=95% purity and suitable for SDS-PAGE, FuncS.
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Key facts
- Purity
- >=95% SDS-PAGE
- Expression system
- HEK 293 cells
- Tags
- Fc tag C-Terminus
- Applications
- SDS-PAGE, FuncS
- Biologically active
- No
Amino acid sequence
E E A F T Y L C T A P G C A T Q A P V P V R L A G V R F E S K I V D G G C F A P W D L E A T G A C I C E I P T D V S C E G L G A W V P A A P C A R I W N G T Q R A C T F W A V N A Y S S G G Y A Q L A S Y F N P G G S Y Y K Q Y H P T A C E V E P A F G H S D A A C W G F P T D T V M S V F A L A S Y V Q H P H K T V R V K F H T E T R T V W Q L S V A G V S C N V T T E H P F C N T P H G Q L E V Q V P P D P G D L V E Y I M N Y T G N Q Q S R W G L G S P N C H G P D W A S P V C Q R H S P D C S R L V G A T P E R P R L R L V D A D D P L L R T A P G P G E V W V T P V I G S Q A R K C G L H I R A G P Y G H A T V E M P E W I H A H T T S D P W H P P G P L G L K F K T V R P V A L P R T L A P P R N V R V T G C Y Q C G T P A L V E G L A P G G G N C H L T V N G E D L G A V P P G K F V T A A L L N T P P P Y Q V S C G G E S D R A T A R V I D P A A Q S F T G V V Y G T H T T A V S E T R Q T W A E W A
Reactivity data
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
Target data
Function
Capsid protein. Capsid protein interacts with genomic RNA and assembles into icosahedric core particles 65-70 nm in diameter. The resulting nucleocapsid eventually associates with the cytoplasmic domain of E2 at the cell membrane, leading to budding and formation of mature virions from host Golgi membranes. Phosphorylation negatively regulates RNA-binding activity, possibly delaying virion assembly during the viral replication phase. Capsid protein dimerizes and becomes disulfide-linked in the virion. Modulates genomic RNA replication. Modulates subgenomic RNA synthesis by interacting with human C1QBP/SF2P32. Induces both perinuclear clustering of mitochondria and the formation of electron-dense intermitochondrial plaques, both hallmarks of rubella virus infected cells. Induces apoptosis when expressed in transfected cells. Spike glycoprotein E2. Responsible for viral attachment to target host cell, by binding to the cell receptor. Its transport to the plasma membrane depends on interaction with E1 protein. The surface glycoproteins display an irregular helical organization and a pseudo-tetrameric inner nucleocapsid arrangement. Spike glycoprotein E1. Class II viral fusion protein (By similarity). Fusion activity is inactive as long as E1 is bound to E2 in mature virion. After virus attachment to target cell and clathrin-mediated endocytosis, acidification of the endosome would induce dissociation of E1/E2 heterodimer and concomitant trimerization of the E1 subunits (PubMed:15557740). This E1 homotrimer is fusion active, and promotes release of viral nucleocapsid in cytoplasm after endosome and viral membrane fusion. The cytoplasmic tail of spike glycoprotein E1 modulates virus release. The surface glycoproteins display an irregular helical organization and a pseudo-tetrameric inner nucleocapsid arrangement (By similarity).
Additional Targets
Rubella virus E1
Alternative names
Structural polyprotein, p110
Recommended products
Recombinant Rubella Virus spike glycoprotein E1 protein (Fc Chimera) is a Rubella virus strain Therien Fragment protein, in the 583 to 1025 aa range, expressed in HEK 293, with >=95% purity and suitable for SDS-PAGE, FuncS.
Key facts
- Purity
- >=95% SDS-PAGE
- Expression system
- HEK 293 cells
- Tags
- Fc tag C-Terminus
- Applications
- SDS-PAGE, FuncS
- Biologically active
- No
- Accession
- P07566-1
- Animal free
- No
- Species
- Rubella virus strain Therien
- Concentration
- Storage buffer
pH: 7 - 8
Constituents: PBS, 0.1% 3-[(3-Cholamidopropyl)dimethylammonio]-1-propanesulfonate
Sequence info
Amino acid sequence
- E E A F T Y L C T A P G C A T Q A P V P V R L A G V R F E S K I V D G G C F A P W D L E A T G A C I C E I P T D V S C E G L G A W V P A A P C A R I W N G T Q R A C T F W A V N A Y S S G G Y A Q L A S Y F N P G G S Y Y K Q Y H P T A C E V E P A F G H S D A A C W G F P T D T V M S V F A L A S Y V Q H P H K T V R V K F H T E T R T V W Q L S V A G V S C N V T T E H P F C N T P H G Q L E V Q V P P D P G D L V E Y I M N Y T G N Q Q S R W G L G S P N C H G P D W A S P V C Q R H S P D C S R L V G A T P E R P R L R L V D A D D P L L R T A P G P G E V W V T P V I G S Q A R K C G L H I R A G P Y G H A T V E M P E W I H A H T T S D P W H P P G P L G L K F K T V R P V A L P R T L A P P R N V R V T G C Y Q C G T P A L V E G L A P G G G N C H L T V N G E D L G A V P P G K F V T A A L L N T P P P Y Q V S C G G E S D R A T A R V I D P A A Q S F T G V V Y G T H T T A V S E T R Q T W A E W A
- Accession
- P07566
- Protein length
- Fragment
- Amino acids
- 583 to 1025
- Nature
- Recombinant
- Tags
- Fc tag C-Terminus
Specifications
- Form
- Liquid
- Additional notes
Buffered in DPBS, pH7.4.
General info
- Function
Capsid protein
- Post-translational modifications
Structural polyprotein: Specific enzymatic cleavages in vivo yield mature proteins. Two signal peptidase-mediated cleavages within the polyprotein produce the structural proteins capsid, E2, and E1. The E2 signal peptide remains attached to the C-terminus of the capsid protein after cleavage by the signal peptidase. Another signal peptide at E2 C-terminus directs E1 to the ER, with a similar mechanism.
- Subcellular localisation
- Host mitochondrion
Storage
- Shipped at conditions
- Dry Ice
- Appropriate short-term storage conditions
- -80°C
- Appropriate long-term storage conditions
- -80°C
- Storage information
- Avoid freeze / thaw cycle
Supplementary info
- This supplementary information is collated from multiple sources and compiled automatically.
- Activity summary
The Rubella virus E1 also known as the envelope glycoprotein E1 performs a critical role in the rubella virus life cycle. This protein with an approximate molecular mass of 58 kDa facilitates viral entry into host cells. It expresses on the surface of the rubella virus and enables fusion between the viral envelope and host cell membranes. Through interaction with host cell receptors E1 triggers endocytosis which allows the viral genome to enter the cytoplasm of the host cell initiating infection.
- Biological function summary
The E1 protein contributes to the formation of the rubella virus envelope complex working in tandem with another glycoprotein called E2. This complex is essential for virion assembly and maturation. The interaction between E1 and E2 is necessary for maintaining structural integrity and for ensuring the infectivity of the rubella virus. The envelope complex also plays a role in the immune evasion strategies of the virus helping it to avoid host immune surveillance.
- Pathways
The E1 protein's role in viral entry places it within the endocytic and membrane fusion pathways. These processes are important for host-pathogen interactions and involve coordination with cellular proteins like clathrin and dynamin. Additionally E1 works in conjunction with proteins involved in the cellular response to virus infection including interferon-induced antiviral effectors. Its interaction with these pathways highlights its importance in ensuring successful establishment and spread of infection within host tissues.
- Associated diseases and disorders
The Rubella virus E1 protein is closely associated with congenital rubella syndrome (CRS) and rubella infection itself. CRS results from maternal infection with rubella virus during pregnancy leading to severe developmental abnormalities in the fetus. E1 facilitates viral replication within the host contributing to the pathogenicity of the virus. The interaction between E1 and host cell proteins disrupts normal cellular functions which can exacerbate disease progression and lead to complications.
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3 product images
SDS-PAGE - Recombinant Rubella Virus spike glycoprotein E1 protein (Fc Chimera) (ab256429)
SDS-PAGE analysis of 3.2 μg (Lane 1) and 1.7 μg (Lane 2) of ab256429 under reducing conditions.
Functional Studies - Recombinant Rubella Virus spike glycoprotein E1 protein (Fc Chimera) (ab256429)
Detection of anti-Rubella IgG in human serum.
Plate coated with 50 ng/well of antigens. E1 = ab256429
Antigens coated in bicarbonate-carbonate buffer pH 9.6 for 1 hour at RT. Blocked with 2% BSA/PBS for 2 hours at RT.
Washed x3 with Tris washing buffer.
Serum samples (Public Health England) diluted 1/201 in 1% BSA in PBS-T.
Secondary antibody was anti-Human-IgG-HRP diluted 1/10000 in 1% BSA in PBS-T. TMB detection.
Functional Studies - Recombinant Rubella Virus spike glycoprotein E1 protein (Fc Chimera) (ab256429)
Detection of anti-Rubella IgM in human serum.
Plate coated with 100 ng/well of antigens. E1 = ab256429
Washed x3 with Tris washing buffer.
Serum samples (Public Health England) diluted 1/201 in 1% BSA in PBS-T + 4% IgG/RF stripper. After standing for 30 minutes the diluted samples were centrifuged at 17,000 x g for 1 minute and the supernatant used for ELISA.
Secondary antibody was anti-Human-IgM-HRP diluted 1/10000 in 1% BSA in PBS-T. TMB detection.
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