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pGAPZα C
| 型號(hào) | 載體名稱(chēng) | 出品公司 | 載體用途 |
| VJI0295 | pGAPZα C | Invitrogen | 酵母表達(dá)載體 |
The glyceraldehyde-3-phosphate dehydrogenase （GAPDH） enzyme is constitutively
expressed at high levels in many organisms, including Pichia pastoris. The promoter of
the gene （GAP） encoding the GAPDH protein has recently been characterized and shown
to express recombinant proteins to high levels in Pichia pastoris, depending on the
carbon source used （Waterham et al., 1997）. The level of expression seen with the GAP
promoter （PGAP） can be slightly higher than that obtained with the AOX1 promoter.
The pGAPZ A, B, and C vectors （2.9 kb） and pGAPZα A, B, and C （3.1 kb） vectors use
the GAP promoter to constitutively express recombinant proteins in Pichia pastoris.
Proteins can be expressed as fusions to a C-terminal peptide containing the myc epitope
for detection and a polyhistidine tag for purification on metal-chelating resin （i.e.
ProBondô）. In addition, pGAPZα produces proteins fused to an N-terminal peptide
encoding the Saccharomyces cerevisiae α-factor secretion signal. Both vectors are
supplied in three reading frames to facilitate in frame cloning with the C-terminal tag
and/or the N-terminal secretion signal. Selection of these vectors is based on the dominant
selectable marker, Zeocinô, which is bifunctional in both Pichia and E. coli.
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