Influenza A virus (strain A/Puerto Rico/8/1934 H1N1)
蛋白長(zhǎng)度:
Full Length
來(lái)源:
in vitro E.coli expression system
分子量:
12.5 kDa
表達(dá)區(qū)域:
1-97aa
氨基酸序列
MSLLTEVETPIRNEWGCRCNGSSDPLAIAANIIGILHLILWILDRLFFKCIYRRFKYGLKGGPSTEGVPKSMREEYRKEQQSAVDADDGHFVSIELE Note: The complete sequence may
include tag sequence, target protein sequence, linker sequence
and extra sequence that is translated with the protein sequence
for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant
protein is critical to your application, please explicitly
request the full and complete sequence of this protein before
ordering.
蛋白標(biāo)簽:
N-terminal 10xHis-tagged
產(chǎn)品提供形式:
Liquid or Lyophilized powder Note: We will
preferentially ship the format that we have in stock, however,
if you have any special requirement for the format, please
remark your requirement when placing the order, we will prepare
according to your demand.
緩沖液:
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose.
復(fù)溶:
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
儲(chǔ)存條件:
Store at -20°C/-80°C upon receipt, aliquoting is
necessary for
mutiple use. Avoid repeated freeze-thaw cycles.
保質(zhì)期:
The shelf life is related to many factors, storage
state,
buffer ingredients, storage temperature and the stability of the
protein
itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C.
The
shelf life of lyophilized form is 12 months at -20°C/-80°C.
貨期:
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
注意事項(xiàng):
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
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.
基因功能參考文獻(xiàn):
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
顯示更多
收起更多
亞細(xì)胞定位:
Virion membrane. Host apical cell membrane; Single-pass type III membrane protein.