Recombinant Epstein-Barr Virus Latent Membrane Protein 2 (LMP2) Protein (His-SUMO)

Name: Recombinant Epstein-Barr Virus Latent Membrane Protein 2 (LMP2) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-03513P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Epstein-Barr Virus Latent Membrane Protein 2 (LMP2) Protein (His-SUMO) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P13285
Target Symbol	LMP2
Synonyms	LMP2; Latent membrane protein 2; Terminal protein
Species	Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MGSLEMVPMGAGPPSPGGDPDGYDGGNNSQYPSASGSSGNTPTPPNDEERESNEEPPPPYEDPYWGNGDRHSDYQPLGTQDQSLYLGLQHDGNDGLPPPPYSPRDDSSQHIYEEAGRGSMNPVCLPVIVAPYLFWLAAIAASCFTAS
Expression Range	1-147aa
Protein Length	Partial
Mol. Weight	31.6kDa
Research Area	Cell Biology
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Isoform LMP2A maintains EBV latent infection of B-lymphocyte, by preventing lytic reactivation of the virus in response to surface immunoglobulin (sIg) cross-linking. Acts like a dominant negative inhibitor of the sIg-associated protein tyrosine kinases, LYN and SYK. Also blocks translocation of the B-cell antigen receptor (BCR) into lipid rafts, preventing the subsequent signaling and accelerated internalization of the BCR upon BCR cross-linking. Serves as a molecular scaffold to recruit SYK, LYN and E3 protein-ubiquitin ligases, such as ITCH and NEDD4L, leading to ubiquitination and potential degradation of both tyrosines kinases. Possesses a constitutive signaling activity in non-transformed cells, inducing bypass of normal B lymphocyte developmental checkpoints allowing immunoglobulin-negative cells to colonize peripheral lymphoid organs.; Isoform LMP2B may be a negative regulator of isoform LMP2A.
Subcellular Location	[Isoform LMP2A]: Host cell membrane; Multi-pass membrane protein.; [Isoform LMP2B]: Host endomembrane system; Multi-pass membrane protein. Host cytoplasm, host perinuclear region.
Protein Families	Herpesviridae LMP-2 family
Database References	KEGG: vg:3783751

Gene Functions References

In EBV-positive Hodgkin's lymphoma LMP2A-expressing HRS cells lacking BCR signalling functions cannot induce EGR1 and are consequently protected from entry to the virus lytic cycle. PMID: 23592216
Epstein-Barr virus latent membrane protein 2A contributes to anoikis resistance through ERK activation. PMID: 23698301
LMP2A, but not LMP2B, is critical for efficient long-term growth of B cells in vitro. PMID: 23308294
LMP2A plays a role in the alteration of a cytokine that is important for both tumour survival and anti-tumour responses. PMID: 23303827
LMP2A can affect a number of signaling pathways by regulating the phosphorylation of the ITSN1 and Shb adaptors. PMID: 22975684
Data show that LMP2A enhances antigen presentation function. PMID: 22616025
hnRNP K, when co-expressed with EBNA2, strongly enhances viral latent membrane protein 2A (LMP2A) expression. PMID: 22879910
Epstein-Barr virus latent membrane protein-2A induces ITAM/Syk- and Akt-dependent epithelial migration through alphav-integrin membrane translocation PMID: 22837212
Fra-1 was induced by Epstein-Barr virus LMP2A and is essential for LMP2A-triggered MMP9 expression. PMID: 22514348
Widespread sequence variations in the LMP2A gene were found PMID: 22470549
Studies suggest that LMP2A can also participate in EBV-induced epithelial cell growth transformation. PMID: 22249143
EBV LMP2A is expressed in nasopharyngeal cancer. Cases with nasopharyngeal inflammation showed negative expression of LMP2A. PMID: 16124641
Results confirmed that HPV L1 protein is potential to deliver multiepitope of EBV LMP2 as immunogen. PMID: 20705592
LMP2A induces an epithelial-mesenchymal transition and increases the number of side population stem-like cancer cells in nasopharyngeal carcinoma. PMID: 20532215
LMP2A uniquely makes resting B-cells sensitive to NF-kappaB inhibition and apoptosis and suggest that NF-kappaB may be a novel target to eradicate latently EBV-infected B-cells. PMID: 20484564
LMP2A induces a heightened sensitivity to TLR ligand stimulation PMID: 16920914
Expression of the EBV genes for latent membrane protein 1 and latent membrane protein 2A decreases FoxO1 expression.[LMP-2A] PMID: 16943287
Phosphorylation of LMP2A is prevented by LMP2B. PMID: 17035319
results indicate that cholesterol-dependent LMP2A trafficking determines the fate of LMP2A degradation PMID: 17150237
The signalling scaffold Shb associates through SH2 and PTB domain interactions with phosphorylated tyrosine motifs in the LMP2A N-terminal tail. PMID: 17311000
These results suggest that constitutive activation of the Ras/PI3-K/Akt pathway by LMP2A is a key factor for LMP2A-mediated transformation. PMID: 17582000
All isolates from 7 Japanese nasal NK/T cell lymphomas showed the same amino acid change from serine to threonine at codon 348 in the CTL epitope SSCSSCPLSK of LMP2A. PMID: 17657160
A role for LMP2A as an indispensable BCR mimic in certain B cells from which human B-cell tumors such as Hodgkin lymphoma originate. PMID: 17682125
The results suggest that the combinatorial effects of DNA methylation, histone acetylation, and H3K4me2 modulate the activity of LMP2A promoter. PMID: 17898065
These results demonstrate that LMP2A activates the Notch pathway in both B cells and epithelial cells, and exploits this pathway to regulate its own expresison. PMID: 17980397
EBV uses its latent protein, LMP2A, to activate the NF-kappaB-survivin pathway to rescue EBV-infected epithelial cells from serum deprivation PMID: 18316606
Despite the lack of pre-BCR expression, bone marrow B cells from TgE LMP2A mice proliferate and survive in low concentrations of interleukin 7, similar to wild-type cells. PMID: 18559925
This demonstrates that the UGDH transcript and protein quantities, the enzyme activity, and glycosaminoglycan contents increase in LMP2A overexpressed human embryonic kidney 293 (HEK293) cells. PMID: 18717819
LMP2A and the Notch1 pathway may cooperate to induce the alterations in B-cell identity seen in Hodgkin Reed-Sternberg cells PMID: 18815281
LMP2B modulates the activity of LMP2A contributing to maintenance of Epstein-Barr virus latency. PMID: 18835714
the immunoreceptor tyrosine-based activation motif (ITAM) of LMP-2A is important for HERV-K18 env transactivation PMID: 19070345
c-Cbl promoted LMP2A degradation through ubiquitination, specifically degraded the Syk protein tyrosine kinase in the presence of LMP2A, and inhibited LMP2A induction of the EBV lytic cycle PMID: 19081591
EBV LMP2A promotes tumor development by protecting pre-tumor B cells that would normally apoptose after the c-myc translocation. PMID: 19182823
LMP2A can permit tumorigenesis in the presence of an intact p53 pathway, identifying an important contribution of EBV to Burkitt's lymphoma PMID: 19815507
Our findings emphasize the role of miR-BART22 in modulating LMP2A expression PMID: 19881953

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.