Recombinant Measles virus Fusion glycoprotein F0 (F), partial, Biotinylated

中文名稱：

Recombinant Measles virus Fusion glycoprotein F0 (F), partial, Biotinylated
品名簡稱：

Recombinant Measles virus Fusion glycoprotein F0, partial, Biotinylated
貨號：

CSB-EP301654MCQ-B
說明書：

MSDS Datasheet
規格：

￥3324
圖片：
(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
其他：

產品詳情
產品評價
相關產品
靶點詳情

產品詳情

純度：

Greater than 85% as determined by SDS-PAGE.
生物活性：

Not Test
基因名：

F
Uniprot No.：

P69353
種屬：

Measles virus (strain Edmonston) (MeV) (Subacute sclerose panencephalitis virus)
蛋白長度：

Partial
來源：

E.coli
分子量：

99.0 kDa
表達區域：

24-494aa
氨基酸序列

QIHWGNLSKIGVVGIGSASYKVMTRSSHQSLVIKLMPNITLLNNCTRVEIAEYRRLLRTVLEPIRDALNAMTQNIRPVQSVASSRRHKRFAGVVLAGAALGVATAAQITAGIALHQSMLNSQAIDNLRASLETTNQAIEAIRQAGQEMILAVQGVQDYINNELIPSMNQLSCDLIGQKLGLKLLRYYTEILSLFGPSLRDPISAEISIQALSYALGGDINKVLEKLGYSGGDLLGILESRGIKARITHVDTESYFIVLSIAYPTLSEIKGVIVHRLEGVSYNIGSQEWYTTVPKYVATQGYLISNFDESSCTFMPEGTVCSQNALYPMSPLLQECLRGSTKSCARTLVSGSFGNRFILSQGNLIANCASILCKCYTTGTIINQDPDKILTYIAADHCPVVEVNGVTIQVGSRRYPDAVYLHRIDLGPPISLERLDVGTNLGNAIAKLEDAKELLESSDQILRSMKGLSSTS
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.
蛋白標簽：

N-terminal MBP-tagged and C-terminal 6xHis-Avi-tagged
產品提供形式：

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.
儲存條件：

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
保質期：

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：

Repeated freezing and thawing is not recommended. Store working aliquots at 4℃ for up to one week.
Datasheet & COA：

Please contact us to get it.

產品評價

靶點詳情

功能：

Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (F protein) probably interacts with H at the virion surface. Upon HN binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis.
基因功能參考文獻：
1. Cell-to-Cell Measles Virus Spread between Human Neurons Is Dependent on Hemagglutinin and Hyperfusogenic Fusion Protein. PMID: 29298883
2. L454W F mutant is activated independently of H or the cell receptor that enabled the efficient spread in the central nervous system. PMID: 25670774
3. Acquisition of enhanced fusion activity through substitutions in the extracellular domain of the F protein may be crucial for measles virus to the extensive spread in the central nervous system and development of subacute sclerosing panencephalitis. PMID: 25520515
4. Complementation of F mutants with a monomeric, fusion-inactive F variant enriched the F oligomers for heterotrimers containing a single disulfide bond, without affecting fusion complementation profiles compared with standard F protein. PMID: 25157143
5. F maturation prepares for complex separation after triggering, and the H head domains in prereceptor-bound conformation prevent premature stalk rearrangements and F activation. PMID: 25392208
6. Thermodynamically stabilized by the N465H substitution, the F protein required elevated temperature as high as 40 degrees C to promote cell-cell fusion, whereas all five DIII mutations caused destabilization of the F protein PMID: 25479085
7. Authors demonstrate that the measles virus H stalk represents the effector domain for measles virus F triggering. PMID: 23966411
8. Taken together, these findings reveal that the morbillivirus H protein must lower the activation energy barrier of metastable prefusion F for fusion triggering. PMID: 23077316
9. The F genes of measles virus isolated in china had no significant genetic variation. PMID: 20084883
10. The F genes of measles virus in China during 1999-2003 had no sig-nificant changes. PMID: 20077667
11. residues located in the head domain of the F trimer and the HR-B region contribute jointly to controlling F conformational stability PMID: 16415028
12. findings show that both M (a fraction of which is modified by ubiquitination) & F proteins individually promote formation of virus-like particles, but they do not act in synergy; we propose that M & F act separately in particle morphogenesis and release PMID: 17374768
13. These findings suggest a common molecular mechanism and a key role of the F protein for syncytium formation in cells expressing an unidentified third receptor for MV. PMID: 17825451
14. Tyrosine-based targeting motifs in the H and F glycoproteins play a crucial role for MV replication and spread within lymphocytes, the main target cells of acute MV infection. PMID: 18272759
15. The partitioning of F, CD46 and CD55 molecules in different membrane microdomains could account for the ability of F to escape complement regulation by the CD55 and CD46 regulators. PMID: 18455798
16. Alanine-scanning mutagenesis revealed that an F protein with a single mutation of a central TM region leucine (L507A) was more fusogenic than the unmodified F protein while retaining similar kinetics of proteolytic processing. PMID: 18786999
17. The H-protein and the F-protein mediates the virus cell entry. PMID: 19198562
18. findings argue against specific protein-protein contacts between the H head & F head domains; support a docking model characterized by short-range contacts between prefusion F head & attachment protein stalk, possibly involving H residues 111, 114 & 118 PMID: 19656895
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亞細胞定位：

Virion membrane; Single-pass type I membrane protein. Host cell membrane; Single-pass membrane protein.
蛋白家族：

Paramyxoviruses fusion glycoprotein family
數據庫鏈接：

KEGG: vg:1489800