Recombinant Proteins

NKMAX has been developing and manufacturing recombinant proteins since 2004. Today, NKMAX produces over 3000 proteins for research use, all of which are produced in-house. Of these, NKMAX has validated the bioactivity of over 200 proteins. They are easily identified by indicating “(bioactivity validated)” in the product the name. The bioactivity details are included in their datasheet.


We produce recombinant proteins by using DNA cloning techniques



Interleukin series, GH, EGF, IGF, VEGF, TNFa, TNFB, BMP series


Aldose reductase, GPT, GST, GOT, GAPDH, G3PD, PP2CA


BID, Bcl2, 14-3-3 series, ADK, BAG2, p53, p53, p21, NKP46, KRAS


ApoA1, Alpha-enolase, CRADD, CA2, DLD, Hexokinase, APRT



Of the NKMAX’s proteins that have not been tested for biological activity, most have not been exposed to denaturing agents, so it is quite possible they’re bioactive. We recommend that clients who are doing function studies buy a sample size to test. Most of NKMAX’s proteins are expressed in E. Coli., and a few are produced in baculovirus.

NKMAX takes pride in its customer service and its involvement in the research community by providing good quality recombinant proteins at reasonable prices.


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What is a recombinant protein?

It’s a protein that is produced with the help of recombinant technology.

A recombinant protein is encoded by a recombinant DNA (rDNA), which is a DNA sequence or gene that is created using laboratory methods called molecular cloning to bring together genetic material from several sources, creating sequences that may or may not be found in biological organisms. This allows to extract a desired gene from a target organism and inserted into another organism’s plasmids, called vectors, to carry the gene of interest. In concrete terms, it allows a bacteria, such as E.coli, to host a plasmid that will force the bacteria to produce large quantities of a specific human gene or protein.

The host cells used for recombinant protein production can be derived from bacteria, mammalian cell, insect and yeast.

The advantage of a bacterial expression system is the cost and the yield, which allows NKMAX to give better prices. However, not all human proteins can be expressed in E.Coli. More complex proteins are normally produced in more sophisticated expression systems in organisms such as insect cells (baculovirus) or mammalian cells (CHO cells). Proteins coexpressed in bacteria will not possess post-translational modifications, e.g. phosphorylation or glycosylation. Eukaryotic expression systems are needed for post-translational modifications.