pFLAG-MAC Expression Vector

Bacterial vector for cytoplasmic expression of N-terminal Met-FLAG fusion proteins

Pricing and availability is not currently available.


for molecular biology


buffered aqueous solution


FLAG® tagged

shipped in

dry ice

storage temp.


General description

The pFLAG-MAC Expression Vector is a 5.0 kb E. coli expression vector used for cloning and cytoplasmic expression of properly inserted open reading frame as an N-terminal Met-FLAG® fusion protein. The Met-FLAG fusion protein may be detected using Monoclonal ANTI-FLAG M2 (F3165), Monoclonal ANTI-FLAG M5 (F4042), and can be purified using the ANTI-FLAG M2 Affinity Gel (A2220).

The pFLAG-ATS-BAP Control Plasmid is a 6.8 kb E. coli plasmid used for efficient and controlled periplasmic expression of N-terminal FLAG-BAP fusion protein. The FLAG-BAP fusion protein may be detected using Monoclonal ANTI-FLAG M1 (F3040), or Monoclonal ANTI-FLAG M2 (F3165), or purified using ANTI-FLAG M1 Agarose Affinity Gel (A4596), or ANTI-FLAG M2 Affinity Gel (A2220).

Vector Maps and Sequences


  • pFLAG-MAC Expression Vector 10 μg (E5644) is supplied as 0.5 mg/ml in 10 mM Tris-HCl (pH 8.0) with 1 mM EDTA.
  • pFLAG-ATS-BAP Control Plasmid 1 μg (C9079) is supplied as 0.5 mg/ml in 10 mM Tris-HCl (pH 8.0) with 1 mM EDTA.

Legal Information

FLAG is a registered trademark of Sigma-Aldrich Co. LLC
pFLAG-MAC is a trademark of Sigma-Aldrich Co. LLC


NONH for all modes of transport

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Huang, et al.
Gene, 766, 145156-145156 (2020)
Vikramjit S Bajwa et al.
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Brassinosteroids (BRs) are plant hormones that are perceived at the cell surface by a membrane-bound receptor kinase, BRASSINOSTEROID INSENSITIVE1 (BRI1). BRI1 interacts with BRI1-ASSOCIATED RECEPTOR KINASE1 (BAK1) to initiate a signal transduction pathway in which autophosphorylation and transphosphorylation of BRI1...
Julia A Ross et al.
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YscD is an essential component of the plasmid pCD1-encoded type III secretion system (T3SS) of Yersinia pestis. YscD has a single transmembrane (TM) domain that connects a small N-terminal cytoplasmic region (residues 1 to 121) to a larger periplasmic region...
Sandra Lobo et al.
The Journal of biological chemistry, 277(43), 41268-41273 (2002-08-24)
Most Ras proteins are posttranslationally modified by a palmitoyl lipid moiety through a thioester linkage. However, the mechanism by which this occurs is not known. Here, evidence is presented that the Ras2 protein of Saccharomyces cerevisiae is palmitoylated by a...

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