Recombinant Salmon pancreas disease virus Structural polyprotein

Lyophilized powder
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Avoid repeated freeze-thaw cycles. Store working aliquots at 4°C for up to one week.

Centrifuge the vial briefly before opening to collect the contents. Reconstitute the protein in sterile, deionized water to a concentration of 0.1-1.0 mg/mL. For long-term storage, we recommend adding 5-50% glycerol (final concentration) and aliquoting at -20°C/-80°C. Our standard glycerol concentration is 50% and can serve as a reference.

Shelf life depends on various factors including storage conditions, buffer composition, temperature, and protein stability. Generally, liquid formulations have a 6-month shelf life at -20°C/-80°C, while lyophilized formulations have a 12-month shelf life at -20°C/-80°C.

Store at -20°C/-80°C upon receipt. Aliquot for multiple uses. Avoid repeated freeze-thaw cycles.

Tag type is determined during manufacturing.
The tag type is determined during production. Specify your desired tag type during ordering to prioritize its implementation.

Tris/PBS-based buffer, 6% Trehalose.

Please contact us to get it.

860-1320

Full Length of Mature Protein

Salmon pancreas disease virus (SPDV)

YEHTVVVPMDPRAPSYEAVINRNGYDPLKLTISVNFTVISPTTALEYWTCAGVPIVEPPH VGCCTSVSCPSDLSTLHAFTGKAVSDVHCDVHTNVYPLLWGAAHCFCSTENTQVSAVAAT VSEFCAQDSERAEAFSVHSSSVTAEVLVTLGEVVTAVHVYVDGVTSARGTDLKIVAGPIT TDYSPFDRKVVRIGEEVYNYDWPPYGAGRPGTFGDIQARSTNYVKPNDLYGDIGIEVLQP TNDHVHVAYTYTTSGLLRWLQDAPKPLSVTAPHGCKISANPLLALDCGVGAVPMSINIPD AKFTRKLKDPKPSALKCVVDSCEYGVDYGGAATITYEGHEAGKCGIHSLTPGVPLRTSVV EVVAGANTVKTTFSSPTPEVALEVEICSAIVKCAGECTPPKEHVVATRPRHGSDPGGYIS GPAMRWAGGIVGTLVVLFLILAVIYCVVKKCRSKRIRIVKS

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The recombinant Salmon pancreas disease virus structural polyprotein forms an icosahedral capsid (T=4 symmetry) comprised of 240 copies of the capsid protein. This capsid is enveloped by a lipid membrane containing 80 spikes, each composed of E1-E2 heterodimer trimers. The capsid protein binds viral RNA near its ribosome binding site, facilitating translation post-genome release. It possesses autocatalytic protease activity, cleaving itself from the nascent structural protein. Following self-cleavage, transient ribosome association precedes viral RNA binding and rapid icosahedral core particle assembly. The resulting nucleocapsid interacts with the cytoplasmic domain of the spike glycoprotein E2 at the cell membrane, leading to budding and virion maturation. During infection, virions attach to target cells and undergo clathrin-mediated endocytosis, fusing with the host endosomal membrane. This releases the nucleocapsid into the cytoplasm, initiating uncoating (potentially triggered by capsid-ribosome interaction) to make the genomic RNA accessible. The protein specifically inhibits interleukin-1 receptor-associated kinase 1 (IRAK1)-dependent signaling during viral entry, evading innate immune detection before gene expression. The polyprotein provides the signal sequence for E3/E2 precursor translocation to the host endoplasmic reticulum. Furin-cleaved E3 remains associated with E1, maintaining E1's pH protection during secretory pathway transport. Following virion release, E3 is gradually released extracellularly. E2 participates in viral attachment by binding to the cell receptor, originating as a p62 precursor. Furin processing at the cell membrane before budding yields the E2-E1 heterodimer (unstable at low pH); p62 processing is a later step, preventing premature E1 fusion activation. E2's C-terminus, initially transmembrane, undergoes palmitoylation-induced reorientation from lumenal to cytoplasmic, crucial for budding via capsid protein interaction. The 6K protein, a constitutive membrane protein, is involved in glycoprotein processing, cell permeabilization, and virion budding. It disrupts calcium homeostasis (likely at the endoplasmic reticulum), causing cytoplasmic calcium elevation. Its lipophilic nature suggests a role in lipid selection for interaction with glycoprotein transmembrane domains, influencing bilayer deformability for budding. E1, a class II viral fusion protein, remains fusion-inactive while bound to E2 in mature virions. Endosomal acidification post-cell attachment and endocytosis dissociates the E1/E2 heterodimer, triggering E1 trimerization and fusion activity, leading to nucleocapsid release into the cytoplasm. Efficient fusion necessitates cholesterol and sphingolipids in the target membrane, optimally around one cholesterol molecule per two phospholipids, and specifically requires sterols with a 3-beta-hydroxyl group.

KEGG: vg:2193532

[Capsid protein]: Virion. Host cytoplasm. Host cell membrane. Host nucleus.; [Spike glycoprotein E2]: Virion membrane; Single-pass type I membrane protein. Host cell membrane; Single-pass type I membrane protein.; [6K protein]: Host cell membrane; Multi-pass membrane protein. Virion membrane; Multi-pass membrane protein.; [Spike glycoprotein E1]: Virion membrane; Single-pass type I membrane protein. Host cell membrane; Single-pass type I membrane protein.