Recombinant Human PCYT1B GST (N-Term) Protein Summary
| Description |
A recombinant protein with GST tag at N-terminal corresponding to the amino acids 1-369 of Human PCYT1B Source: Wheat Germ (in vitro) Amino Acid Sequence: MPVVTTDAESETGIPKSLSNEPPSETMEEIEHTCPQPRLTLTAPAPFADETNCQCQAPHEKLTIAQARLGTPADRPVRVYADGIFDLFHSGHARALMQAKTLFPNSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEVIRDAPWTLTPEFLEKHKIDFVAHDDIPYSSAGSDDVYKHIKEAGMFVPTQRTEGISTSDIITRIVRDYDVYARRNLQRGYTAKELNVSFINEKRYRFQNQVDKMKEKVKNVEERSKEFVNRVEEKSHDLIQKWEEKSREFIGNFLELFGPDGAWKQMFQERSSRMLQALSPKQSPVSSPTRSRSPSRSPSPTFSWLPLKTSPPSSPKAASASISSMSEGDEDEK |
Preparation Method |
in vitro wheat germ expression system |
| Details of Functionality |
This protein was produced in an in vitro wheat germ expression system that should preserve correct conformational folding that is necessary for biological function. While it is possible that this protein could display some level of activity, the functionality of this protein has not been explicitly measured or validated. |
| Source |
Wheat germ |
| Protein/Peptide Type |
Recombinant Protein |
| Gene |
PCYT1B |
| Purity |
>80% by SDS-PAGE and Coomassie blue staining |
Applications/Dilutions
| Dilutions |
- ELISA
- Immunoaffinity Purification
- Protein Array
- Western Blot
|
| Theoretical MW |
68.3 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
Packaging, Storage & Formulations
| Storage |
Store at -80C. Avoid freeze-thaw cycles. |
| Buffer |
50 mM Tris-HCl, 10 mM reduced Glutathione, pH 8.0 in the elution buffer. |
| Preservative |
No Preservative |
| Purity |
>80% by SDS-PAGE and Coomassie blue staining |
Notes
This product is produced by and distributed for Abnova, a company based in Taiwan.
Alternate Names for Recombinant Human PCYT1B GST (N-Term) Protein
Background
TCP1 beta is a subunit of a cytosolic hetero-oligomer chaperon that is known to be involved in the folding of actin and tubulin. This protein is a member of the chaperonin family, which includes Escherichia coli GroEL, the mitochondrial heat-shock protein Hsp60, the plastid Rubisco-subunit-binding protein and the archaebacterial protein TF55. These chaperonins assist the folding of proteins upon ATP hydrolysis. Nine different subunits of TCP-1 containing chaperonin complexes from mammalian testis and seven different subunits of mouse F9 cells have been identified. It has been suggested that each CCT subunit has a specific, independent function, as they are highly diverged from each other but conserved from mammals to yeast. The expansion in the number of types of CCT subunit, compared with other chaperonins, has allowed CCT to carry out more complex functions that are required for the folding and assembly of highly evolved eukaryotic proteins.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are
guaranteed for 3 months from date of receipt.
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