Recombinant Influenza A Virus Matrix Protein 2 (M) Protein (His&Myc)

Name: Recombinant Influenza A Virus Matrix Protein 2 (M) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-01848P
Price: 680.8 USD
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: Featured viral antigens molecules, Influenza a/b antigen, Recombinant proteins, Viral antigen

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Product Overview

Description	Recombinant Influenza A Virus Matrix Protein 2 (M) Protein (His&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P06821
Target Symbol	M
Synonyms	M; Matrix protein 2; Proton channel protein M2
Species	Influenza A virus (strain A/Puerto Rico/8/1934 H1N1)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	DRLFFKCIYRRFKYGLKGGPSTEGVPKSMREEYRKEQQSAVDADDGHFVSIELE
Expression Range	44-97aa
Protein Length	Partial
Mol. Weight	13.8 kDa
Research Area	Tags & Cell Markers
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	Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation.
Subcellular Location	Virion membrane. Host apical cell membrane; Single-pass type III membrane protein.
Protein Families	Influenza viruses matrix protein M2 family
Database References	KEGG: vg:956528

Gene Functions References

The data demonstrated that immunization with recombinant L. plantarum expressing 3M2e-Fc markedly reduced the viral load in the lung and protected against H1N1 influenza virus and mouse-adapted H9N2 avian influenza virus (AIV) challenge in BALB/c mice [M2e]. PMID: 27908830
this work shows the production and isolation of a tetrameric and functional native M2 ion channel that will pave the way to structural and functional characterization of native M2, conformational antibody development, small molecules compounds screening towards vaccine treatment. PMID: 27825980
BST-2 restricts influenza A virus release and is countered by the viral M2 protein. PMID: 28087685
Host cellular protein TRAPPC6ADelta interacts with influenza A virus M2 protein and regulates viral propagation by modulating M2 trafficking. PMID: 27795429
M2 protein is translocated from the membrane to the cytoplasm by a retrograde route via endosomes and the Golgi network. PMID: 27942972
Studied the structure of the C-terminal juxtamembrane region (sites 50-60) of the full-length M2 protein using site-directed spin-labeling electron paramagnetic resonance (EPR) spectroscopy in lipid bilayers. PMID: 25545360
The tautomeric state and conformation of His37, a key residue in the M2 transmembrane four-helix bundle, controls the gating of the channel. PMID: 25317959
Results indicate that Fc receptors play a primary role in conferring M2e-specific antibody-mediated protection whereas T cells may contribute to the recovery at later stages of influenza infection. PMID: 24773389
Authors show that the cytoplasmic tail of influenza A virus M2 interacts directly with the essential autophagy protein LC3 and promotes LC3 relocalization to the unexpected destination of the plasma membrane. PMID: 24528869
Clustering between hemagglutinin (HA) and M2 is reduced upon disruption of HA's raft-association features (acylation, transmembranous VIL motif). PMID: 24561202
NS1,hemagglutinin and M2 are involved in stimulation of autophagy in infected cells. PMID: 24027311
Data suggest that solubilization of M2 construct into bicelles results in an increased ordering of the TMH-APH (transmembrane helix- amphipathic helix) linker resulting in a more fixed orientation between the TMH and APH. PMID: 24168642
Data show that that the M2 proton channel is properly targeted to cell membranes in Drosophila tissues and functions as a proton channel by altering intracellular pH. PMID: 21775472
Data show that M2 acts as a proton uniporter that occasionally allows K(+) to flow to maintain electrical neutrality. PMID: 20713739
the M2 cytoplasmic tail plays a role in infectious virus production by coordinating the efficient packaging of genome segments into influenza virus particles. PMID: 15731254
These results indicated that the M2 ion-channel protein is critical, but not essential, for virus replication in cell culture. PMID: 15831957
results demonstrate that a dramatic reduction in the levels of the M1 and M2 proteins in influenza A virus-infected cells results in reduced virus replication but does not significantly affect the composition and morphology of the virus particles PMID: 15919950
To better understand its H+ gating mechanism, we investigated M2 in lipid bilayers with a new combination of IR spectroscopies and theory. PMID: 19217395
Influenza A virus infection causes accumulation of autophagosomes by blocking their fusion with lysosomes, and one viral protein, matrix protein 2, is necessary and sufficient for this inhibition of autophagosome degradation. PMID: 19837376

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.