Recombinant Influenza A virus Matrix protein 2 (M), partial

Code CSB-YP356944IFZ1
MSDS
Size Pls inquire
Source Yeast
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-EP356944IFZ1-B
MSDS
Size Pls inquire
Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-BP356944IFZ1
MSDS
Size Pls inquire
Source Baculovirus
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-MP356944IFZ1
MSDS
Size Pls inquire
Source Mammalian cell
Have Questions? Leave a Message or Start an on-line Chat

Product Details

Purity
>85% (SDS-PAGE)
Target Names
M
Uniprot No.
Alternative Names
M; Matrix protein 2; Proton channel protein M2
Species
Influenza A virus (strain A/Puerto Rico/8/1934 H1N1)
Protein Length
Partial
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
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.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
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.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
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.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

Customer Reviews and Q&A

 Customer Reviews

There are currently no reviews for this product.

Submit a Review here

Target Background

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.
Gene References into Functions
  1. 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
  2. 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
  3. BST-2 restricts influenza A virus release and is countered by the viral M2 protein. PMID: 28087685
  4. Host cellular protein TRAPPC6ADelta interacts with influenza A virus M2 protein and regulates viral propagation by modulating M2 trafficking. PMID: 27795429
  5. M2 protein is translocated from the membrane to the cytoplasm by a retrograde route via endosomes and the Golgi network. PMID: 27942972
  6. 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
  7. 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
  8. 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
  9. 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
  10. Clustering between hemagglutinin (HA) and M2 is reduced upon disruption of HA's raft-association features (acylation, transmembranous VIL motif). PMID: 24561202
  11. NS1,hemagglutinin and M2 are involved in stimulation of autophagy in infected cells. PMID: 24027311
  12. 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
  13. 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
  14. Data show that M2 acts as a proton uniporter that occasionally allows K(+) to flow to maintain electrical neutrality. PMID: 20713739
  15. 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
  16. These results indicated that the M2 ion-channel protein is critical, but not essential, for virus replication in cell culture. PMID: 15831957
  17. 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
  18. To better understand its H+ gating mechanism, we investigated M2 in lipid bilayers with a new combination of IR spectroscopies and theory. PMID: 19217395
  19. 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

Show More

Hide All

Subcellular Location
Virion membrane. Host apical cell membrane; Single-pass type III membrane protein.
Protein Families
Influenza viruses matrix protein M2 family
Database Links

KEGG: vg:956528

CUSABIO guaranteed quality
icon of phone
Call us
301-363-4651 (Available 9 a.m. to 5 p.m. CST from Monday to Friday)
icon of address
Address
7505 Fannin St., Ste 610, Room 7 (CUBIO Innovation Center), Houston, TX 77054, USA
icon of social media
Join us with

Subscribe newsletter

Leave a message

* To protect against spam, please pass the CAPTCHA test below.
CAPTCHA verification
© 2007-2024 CUSABIO TECHNOLOGY LLC All rights reserved. 鄂ICP备15011166号-1