Recombinant EBV Latent Membrane Protein 1 (His tag) is a Epstein-Barr virus Fragment protein, in the 185 to 366 aa range, expressed in Yeast, with >90% purity and suitable for SDS-PAGE, MS.
>90% SDS-PAGE
Yeast
His tag N-Terminus
SDS-PAGE, MS
No
Y F H G P R H T D E H H H D D S L P H P Q Q A T D D S S H E S D S N S N E G R H H L L V S G A G D G P P L C S Q N L G A P G G G P D N G P Q D P D N T D D N G P Q D P D N T D D N G N T D D N G P Q D P D N T D D N G P H D P L P H N P S D S A G N D G G P P N L T E E V E N K G G D R G P P S M T D G G G G D P H L P T L L L G T S G S G G D D D D P H G P V Q L S Y Y D
Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application MS | Reactivity Reacts | Dilution info - | Notes - |
Acts as a CD40 functional homolog to prevent apoptosis of infected B-lymphocytes and drive their proliferation. Functions as a constitutively active tumor necrosis factor receptor that induces the activation of several signaling pathways, including those of the NF-kappa-B family. LMP1 signaling leads to up-regulation of antiapoptotic proteins and provide growth signals in latently infected cells. Interacts with host UBE2I and subsequently affects the sumoylation state of several cellular proteins. For example, induces the sumoylation of host IRF7 thereby limiting its transcriptional activity and modulating the activation of innate immune responses.
EBV Latent Membrane Protein 1
Latent membrane protein 1, LMP-1, Protein p63, BNLF1, LMP1
Recombinant EBV Latent Membrane Protein 1 (His tag) is a Epstein-Barr virus Fragment protein, in the 185 to 366 aa range, expressed in Yeast, with >90% purity and suitable for SDS-PAGE, MS.
>90% SDS-PAGE
Yeast
His tag N-Terminus
SDS-PAGE, MS
No
No
Epstein-Barr virus
pH: 7.2 - 7.4
Constituents: Tris buffer, 50% Glycerol (glycerin, glycerine)
Y F H G P R H T D E H H H D D S L P H P Q Q A T D D S S H E S D S N S N E G R H H L L V S G A G D G P P L C S Q N L G A P G G G P D N G P Q D P D N T D D N G P Q D P D N T D D N G N T D D N G P Q D P D N T D D N G P H D P L P H N P S D S A G N D G G P P N L T E E V E N K G G D R G P P S M T D G G G G D P H L P T L L L G T S G S G G D D D D P H G P V Q L S Y Y D
Fragment
20.8 kDa
185 to 366
Recombinant
His tag N-Terminus
Liquid
Acts as a CD40 functional homolog to prevent apoptosis of infected B-lymphocytes and drive their proliferation. Functions as a constitutively active tumor necrosis factor receptor that induces the activation of several signaling pathways, including those of the NF-kappa-B family. LMP1 signaling leads to up-regulation of antiapoptotic proteins and provide growth signals in latently infected cells. Interacts with host UBE2I and subsequently affects the sumoylation state of several cellular proteins. For example, induces the sumoylation of host IRF7 thereby limiting its transcriptional activity and modulating the activation of innate immune responses.
Belongs to the herpesviridae LMP-1 family.
Ubiquitinated on the N-terminus.
Blue Ice
-20°C
-20°C
Avoid freeze / thaw cycle
This supplementary information is collated from multiple sources and compiled automatically.
EBV Latent Membrane Protein 1 also known as LMP1 is an important oncoprotein of Epstein-Barr virus (EBV). It acts mechanically to modulate cellular signaling pathways. LMP1 weighs approximately 63 kDa. This protein is highly expressed on the surface of lymphocytes and epithelial cells during latent EBV infection. LMP1 comprises several functional domains including Cytoplasmic Tail 1 (CS1) Cytoplasmic Tail 2 (CS2) and Cytoplasmic Tail 3 (CS3). Researchers often study its presence through methods like LMP1 immunohistochemistry (IHC)
The protein plays a role in cellular transformation and proliferation acting as a mimic of CD40 receptor signaling. Within cells LMP1 aggregates to form oligomeric complexes that actively recruit TRAF and TRADD adapter proteins. This aggregation leads to the activation of NF-κB signaling and the MAPK pathways contributing to increased cell survival and proliferation. LMP1 functions as a major factor in sustaining EBV latency in infected cells and is essential for the virus's oncogenic potential.
LMP1 is an integral component of the NF-κB and AP-1 signaling pathways. By engaging with the host cell machinery LMP1 recruits proteins such as IκB kinase complexes leading to the nuclear translocation of NF-κB transcription factors. This results in the transcription of genes related to cell growth and inflammation. LMP1 also interacts with p38 MAPK further enhancing pathways that contribute to EBV’s ability to foster an environment suitable for its persistence and propagation within the host.
LMP1 has strong associations with various malignancies especially nasopharyngeal carcinoma and Hodgkin's lymphoma. The protein’s role in disrupting normal cellular function relates it closely to the pathology of these cancers. It affects the expression of other proteins like c-Myc and Bcl-2 which are often found altered in malignancy. EBV antibodies particularly those targeting LMP1 are used to study the presence and progression of these diseases in infected individuals.
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(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) analysis with 5% enrichment gel and 15% separation gel of ab240835.
Based on the SEQUEST from database of Yeast host and target protein, the LC-MS/MS analysis result of ab240835 could indicate that this peptide derived from Yeast-expressed Epstein-Barr virus (strain GD1) (HHV-4) (Human herpesvirus 4) EBV Latent Membrane Protein 1.
Based on the SEQUEST from database of Yeast host and target protein, the LC-MS/MS analysis result of ab240835 could indicate that this peptide derived from Yeast-expressed Epstein-Barr virus (strain GD1) (HHV-4) (Human herpesvirus 4) EBV Latent Membrane Protein 1.
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