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CUSABIO

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CUSABIO is a National High-Tech Enterprise which combines research, production and sales in one. They are dedicated to providing 60,000+ validated antibodies, 8,000+ recombinant proteins, 660+ cytokines and thousands of ELISA kits to global customers in the research fields of cancer, cell biology, immunology, neuroscience, epigenetics, etc. 

What CUSABIO Does:

As a manufacturer of ELISA kits, Exosome isolation kits, antibodies, proteins and related reagents, their only mission is to provide the best products and related custom service to researchers so that they can have a good start for the next breakthrough. CUSABIO's high quality has been guaranteed by many published literatures in all kinds of famous journals, such as Science, Nature, Cell, Developmental Biology, Molecular Cell, Genes & Development, and so on. Now, the publications citing CUSABIO products has reached more than 4,800, with hundreds of publications updating every year.

Kits

CUSABIO has a sound platform for the development of assay kits, mature antigen-antibody research and development systems. Assay kits offered by CASABIO are mainly two types, including ELISA kits and exosome isolation kits. They are proficient in a variety of ELISA technologies such as the double antibody sandwich method, double antigen sandwich method, direct competition ELISA method, indirect competition ELISA blocking method, indirect ELISA method, and other methods. And fine affinity purification technology for the production of Exosome Isolation Kits is also adopted.

Combined with their diagnostic kits development team, CUSABIO is able to develop ELISA kits with clinical diagnostic levels and make the quality in the leading place worldwide. Exosomes have been one of the research hotspots in recent years, and the separation technology of exosomes has been constantly updated and improved. After continuous improvement and repeated testing, CUSABIO has also developed high purity, high yield, and high-efficiency exosome isolation kits. CUSABIO now offers a broad range of ELISA kits covering over 6,000 different assay targets and two Cell Supernatant Exosome Isolation Kits.

Antibodies

CUSABIO offers 60,000+ antibodies that are specific to a variety of species and can be used in multiple applications. Furthermore, the number of CUSABIO antibodies is continuing to grow at a rate of 1000 per year.

As an original manufacturer, CUSABIO designs, produces and validates every antibody in-house. Besides advanced experimental apparatus, CUSABIO antibody line also has a professional technical team, so CUSABIO has succeeded in setting up many technology platforms. At present CUSABIO antibodies can be applied in ELISA, WB, IHC/ICC, IF, IP/Co-IP, ChIP and FC. 

Proteins

CUSABIO Protein Expression Platform has established four recombinant expression systems from prokaryotic (E.coli) to eukaryotic (Yeast, mammalian cell and insect baculovirus), and has also built unique in-vitro E.coil expression system, which enables them to express transmembrane proteins that are usually difficult to express.

CUSABIO currently has 70 native proteins, 100 small molecule antigens, 320 active proteins, 1000+ recombinant proteins in stock, 5700+ developed recombinant proteins, 10,000+ cDNA clones, 36,000+ transmembrane proteins, 500,000+ semi-customized recombinant proteins. 

Custom Service

Given the specificity of each experiment, CUSABIO provides the latest and comprehensive custom services to meet their customers request, including phage display service, antibody service, protein service, gene synthesis service and oligo synthesis service. CUSABIO is very pleased to assist their customers worldwide with all passions and great efforts.

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Recombinant Feline coronavirus Spike glycoprotein(S),partial CSB-EP319859FEJ



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Specifications

20ug / 100ug / 1mg price = 100ug

Alternative Name(s):

(S glycoprotein)(E2)(Peplomer protein)

Species: (Organism)

Feline coronavirus (strain FIPV WSU-79/1146) (FCoV)

Gene Names:

S

Tag info:

C-terminal 6xHis-tagged

Target Protein AA Sequence:

PMQDNNTDVYCIRSNQFSVYVHSTCKSSLWDNIFNQDCTDVLEATAVIKTGTCPFSFDKLNNYLTFNKFCLSLSPVGANCKFDVAARTRTNEQVVRSLYVIYEEGDNIVGVPSDNSGLHDLSVLHLDSCTDYNIYGRTGVGIIRRTNSTLLSG

Expression Region:

561-713aa

Subcellular Location:

Tissue Specificity:

Protein Length:

Partial

Pathway:

Mol. Weight:

18.0 kDa

Purity:

Greater than 85% as determined by SDS-PAGE.

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.

Research Areas:

Microbiology

Function:

Involvement in disease:

Relevance:

S1 region attaches the virion to the cell membrane by interacting with host ANPEP/aminopeptidase N, initiating the infection. Binding to the receptor probably induces conformational changes in the S glycoprotein unmasking the fusion peptide of S2 region and activating membranes fusion. S2 region belongs to the 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) 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 target cell membranes.

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.

Protein Families:

Reference:

"Assembly of spikes into coronavirus particles is mediated by the carboxy-terminal domain of the spike protein." Godeke G.J., de Haan C.A., Rossen J.W., Vennema H., Rottier P.J. J. Virol. 74:1566-1571(2000)