,

Recombinant Human adenovirus C serotype 5 Hexon protein (L3) (T273A), partial

Recombinant Human adenovirus C serotype 5 Hexon protein (L3) (T273A), partial — Major capsid protein that self-associates to form 240 hexon trimers, each in the shape of a hexagon, building most of the pseudo T=25 capsid. Purity >85%.

SKU: BCRECP-003233 Categories: ,

Product Specifications

Product SkuBCRECP-003233
Product DescriptionRecombinant Human adenovirus C serotype 5 Hexon protein (L3) (T273A) Protein is expressed from E.coli with N-terminal 10xHis-tagged and C-terminal Myc-tagged. It contains 133-324aa(T273A). [Accession | P04133].
Uniprot No.P04133
Gene NamesL3
PurityGreater than 85% as determined by SDS-PAGE.
Expression SystemE.coli
Expression Region133-324aa(T273A)
SpeciesHuman adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5)
Tag InfoN-terminal 10xHis-tagged and C-terminal Myc-tagged
Molecular weight28.8kDa
ActivityPlease contact us to obtain bioactivity data.
BufferIf 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.
StorageStore at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Research AreasMicrobiology

Function

Major capsid protein that self-associates to form 240 hexon trimers, each in the shape of a hexagon, building most of the pseudo T=25 capsid. Assembled into trimeric units with the help of the chaperone shutoff protein. Transported by pre-protein VI to the nucleus where it associates with other structural proteins to form an empty capsid.

Biological Context

Subcellular Location: Virion; Host nucleus

Product Specifications

Recombinant Human adenovirus C serotype 5 Hexon protein (L3) (T273A), partial is a recombinant protein from Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5), expressed in E.coli, covering amino acids 133-324aa(T273A), with N-terminal 10xHis-tagged and C-terminal Myc-tagged tag, molecular weight 28.8kDa, purity Greater than 85% as determined by SDS-PAGE.. Suitable for ELISA and Western Blot applications.

Recommended applications depend on the target, product format, and product-specific validation data. Refer to the product datasheet or Certificate of Analysis (CoA), or contact BioCrest Sci for application guidance.

Biological Activity: Please contact us to obtain bioactivity data.

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

Shipping & Lead Time: Availability, shipping conditions, and estimated lead time are confirmed in the formal quotation or order confirmation based on the product format, destination, and order requirements.

Protein Biology

Function

Major capsid protein that self-associates to form 240 hexon trimers, each in the shape of a hexagon, building most of the pseudo T=25 capsid. Assembled into trimeric units with the help of the chaperone shutoff protein. Transported by pre-protein VI to the nucleus where it associates with other structural proteins to form an empty capsid. Might be involved, through its interaction with host dyneins, in the intracellular microtubule-dependent transport of incoming viral capsid to the nucleus

Subcellular Location

Virion; Host nucleus

Subunit

Homotrimer. Interacts with the capsid vertex protein; this interaction binds the peripentonal hexons to the neighboring penton base. Interacts with the hexon-linking protein VIII; this interaction tethers the hexons surrounding the penton to those situated in the central plate of the facet (PubMed:28978703, PubMed:30121295). Interacts with the hexon-interlacing protein IX; this interaction lashes the hexons together (PubMed:28978703, PubMed:30121295). Interacts with pre-protein VI; this interaction probably allows nuclear import of hexon trimers and possibly pre-capsid assembly (PubMed:14633984). Interacts with endosome lysis protein (PubMed:28978703). Interacts with pVIn (PubMed:28978703, PubMed:30121295). Interacts with pVIIn2 (PubMed:28978703). Interacts with host dyneins DYNC1LI1 and DYNC1I2; this interaction might be involved in intracellular microtubule-dependent transport of incoming viral capsid (PubMed:20006841). Interacts with the shutoff protein; this interaction allows folding and formation of hexons trimers. Interacts with host NUP214 (via N-terminus); this interaction might be essential for the release of the virus genome to the nucleus (By similarity) (PubMed:25410864). Interacts with host LTF/Lactoferrin (via N-terminus); this interaction seems to be part of the mechanisms of cellular entry by the virus (PubMed:38323814). Interacts with host blood coagulation factor F10 (via Gla domain); this interaction allows the virus to be shielded from its host immune system (PubMed:39528527)

Gene: L3  |  Organism: Human adenovirus C serotype 5  |  Synonyms: Protein II
Key Publications

Frequently Asked Questions

How do I order or inquire about this product?

Submit the Online Inquiry form with your required quantity and specifications, or email sales@biocrestsci.com. Available sizes, pricing, stock status, documentation, and estimated lead time are confirmed in the formal quotation.

What is the shipping and delivery time?

Availability, dispatch timing, shipping conditions, and delivery estimates depend on the product format, destination, and order requirements. These details are confirmed in the formal quotation or order confirmation.

How should this product be stored?

Follow the storage and handling instructions in the product-specific datasheet and Certificate of Analysis (CoA). Requirements may vary by product form and formulation; contact BioCrest Sci if product-specific guidance is needed.

What quality controls are performed on your products?

Quality-control data such as identity, purity, endotoxin level, or biological activity are provided only when specified on this product page, the datasheet, or Certificate of Analysis (CoA). Biological activity is not implied unless explicitly stated.

Shopping Cart
Scroll to Top