Recombinant Vesicular Stomatitis Indiana Virus Matrix Protein (M) Protein (His&Myc)

Name: Recombinant Vesicular Stomatitis Indiana Virus Matrix Protein (M) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-01885P
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 Vesicular Stomatitis Indiana Virus Matrix Protein (M) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P03519
Target Symbol	M
Species	Vesicular stomatitis Indiana virus (strain San Juan) (VSIV)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	MSSLKKILGLKGKGKKSKKLGIAPPPYEEDTSMEYAPSAPIDKSYFGVDEMDTYDPNQLRYEKFFFTVKMTVRSNRPFRTYSDVAAAVSHWDHMYIGMAGKRPFYKILAFLGSSNLKATPAVLADQGQPEYHTHCEGRAYLPHRMGKTPPMLNVPEHFRRPFNIGLYKGTIELTMTIYDDESLEAAPMIWDHFNSSKFSDFREKALMFGLIVEKKASGAWVLDSISHFK
Expression Range	1-229aa
Protein Length	Full Length
Mol. Weight	33.5 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	Plays a major role in assembly and budding of virion, by recruiting cellular partners of the ESCRT complexes that play a key role in releasing the budding particle from the host membrane. Condensates the ribonucleocapsid core during virus assembly.; Inhibits mRNA nuclear export through direct interaction with host RAE1-NUP98 complex, thereby preventing interferon signaling and establishment of antiviral state in infected cells. Induces cell-rounding, cytoskeleton disorganization and apoptosis in infected cell. Inhibits host transcription, possibly through interaction with host DNA repair factor IIH/TFIIH GTF2H5 subunit.
Subcellular Location	Virion membrane; Peripheral membrane protein. Host endomembrane system; Peripheral membrane protein. Host nucleus membrane; Peripheral membrane protein. Host nucleus. Host cytoplasm.
Protein Families	Vesiculoviruses matrix protein family
Database References	KEGG: vg:1489833

Gene Functions References

VEGF-D-enhanced metastasis was evidently reversed by MP. MP significantly reduced the invasion of VEGFD-SK cells, tumor volume, lymphatic metastasis rates and lymphatic vessel density compared with control groups PMID: 27211072
vesicular stomatitis virus M protein interacted efficiently with Rae1-Nup98 complexes associated with the chromatin fraction of host nuclei, consistent with an effect on host transcription PMID: 23028327
These findings indicate that the PSAP motif plays a direct role in regulating cytopathogenicity in a species-dependent manner, and suggest that the intact PSAP motif may be important for maintaining virus persistence in an insect host. PMID: 23170175
study re-examined the contribution of the PSAP motif to VSV budding; VSV M binds TSG101 [tumour susceptibility gene 101] through its PSAP motif; double mutant with point mutations in both PSAP and PPPY motifs is impaired compared with a single mutant in the PPPY motif, indicating the PSAP motif partially compensates for lack of the PPPY motif PMID: 22190013
VSV M protein inactivates the cellular Akt signaling pathway. PMID: 20980511
These findings indicate that the host shut-off activity of the M protein dominates vesicular stomatitis virus cytotoxicty, whilst the fusion-active G protein is mainly responsible for the cytotoxicity remaining with M-mutant vesicular stomatitis virus. PMID: 20631091
hyperphosphorylation of VSV M protein was observed in both cell lysates and viral particles from IFN-beta-treated neuronal cells. Hyperphosphorylated VSV M protein was found to inhibit its association with VSV nucleocapsid PMID: 19951173
VSV expressing the mutant M protein induces apoptosis via the death receptor apoptotic pathway, a mechanism distinct from that induced by VSV expressing the wt M protein. PMID: 15767418
first evidence that M protein alone is able to impose the correct budding curvature on the membrane PMID: 16298982
Glycoprotein (G protein) and M protein microdomains were not colocalized in the plasma membrane outside the virus budding sites PMID: 18367537
M protein mutants of VSV are less virulent than wild type and can induce an antibody response similar to that in mice infected with the wt virus. PMID: 18614644
The authors propose that low-pH conformational changes in G protein promote acidification of the virus interior, which facilitates the release of M from ribonucleoprotein particles during uncoating. PMID: 19776119

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.