Recombinant Human cytomegalovirus Capsid scaffolding protein (UL80) (A143V,V207A), partial

SKU: P16753

Size: 100ug. Other sizes are also available.

Activity: Not tested

Research Areas: Microbiology

Uniprot ID: P16753

Gene Names: UL80

Alternative Name(s): (Protease precursor)(pPR)

Abbreviation: Recombinant Human cytomegalovirus UL80 protein (A143V,V207A), partial

Organism: Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5)

Source: E.coli

Expression Region: 1-256aa(A143V,V207A)

Protein Length: Partial

Tag Info: N-terminal 6xHis-tagged

Target Protein Sequence: MTMDEQQSQAVAPVYVGGFLARYDQSPDEAELLLPRDVVEHWLHAQGQGQPSLSVALPLNINHDDTAVVGHVAAMQSVRDGLFCLGCVTSPRFLEIVRRASEKSELVSRGPVSPLQPDKVVEFLSGSYAGLSLSSRRCDDVEVATSLSGSETTPFKHVALCSVGRRRGTLAVYGRDPEWVTQRFPDLTAADRDGLRAQWQRCGSTAADASGDPFRSDSYGLLGNSVDALYIRERLPKLRYDKQLVGVTERESYVKA

MW: 34.0 kDa

Purity: Greater than 90% 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: [Capsid scaffolding protein]: Acts as a scaffold protein by binding major capsid protein in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as major capsid protein forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interaction with major capsid protein. Cleavages products are evicted from the capsid before or during DNA packaging.; [Assemblin]: Protease that plays an essential role in virion assembly within the nucleus. Catalyzes the cleavage of the assembly protein after formation of the spherical procapsid. By that cleavage, the capsid matures and gains its icosahedral shape. The cleavage sites seem to include -Ala-Ser-, -Ala-Ala-, as well as Ala-Thr bonds. Assemblin and cleavages products are evicted from the capsid before or during DNA packaging.; [Assembly protein]: Plays a major role in capsid assembly. Acts as a scaffold protein by binding major capsid protein. Multimerizes in the nucleus such as major capsid protein forms the icosahedral T=16 capsid. Cleaved by assemblin after capsid completion. The cleavages products are evicted from the capsid before or during DNA packaging.

Reference: "Molecular mechanism for dimerization to regulate the catalytic activity of human cytomegalovirus protease." Batra R., Khayat R., Tong L. Nat Struct Biol 8: 810-817(2001)

Function: