Recombinant Bovine leukemia virus Envelope glycoprotein (env), partial

SKU: P25057

Size: 100ug. Other sizes are also available.

Activity: Not tested

Research Areas: Others

Uniprot ID: P25057

Gene Names: env

Alternative Name(s): Env polyprotein;SU;Glycoprotein 51;gp51;TM;Glycoprotein 30;gp30

Abbreviation: Recombinant Bovine leukemia virus env protein, partial

Organism: Bovine leukemia virus (isolate Australian) (BLV)

Source: Mammalian cell

Expression Region: 34-301aa

Protein Length: Partial

Tag Info: C-terminal hFc1-tagged

Target Protein Sequence: WRCSLSLGNQQWMTAYNQEAKFSISIDQILEAHNQSPFCAKSPRYTLDSVNGYPKIYWPPPQGRRRFGARAMVTYDCEPRCPYVGADRFDCPHWDNASQADQGSFYVNHQILFLHLKQCHGIFTLTWEIWGYDPLITFSLHKIPDPPQPDFPQLNSDWVPSVRSWALLLNQTARAFPDCAICWEPSPPWAPEILVYNKTISSSGPGLALPDAQIFWVNTSSFNTTQGWHHPSQRLLFNVSQGNALLLPPISLVNLSTASSAPPTRVRR

MW: 59.3 kDa

Purity: Greater than 95% as determined by SDS-PAGE.

Endotoxin: Not test

Biological_Activity:

Form: Liquid or Lyophilized powder

Buffer: 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, 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.

Storage: 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℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.

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

Relevance: The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane. ; The transmembrane protein (TM) acts as a 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 target cell membrane fusion, the coiled coil regions (heptad repeats) 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 target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.

Reference:

Function: