GeneHarbor's pipeline includes novel enzymes and processes for the production of pharmaceutical products, neutraceutical products and high-value added food ingredients.


The Company also operates its own manufacture facility that industrially manufactures biochemicals of the highest standard. The products and product pipeline include: reduced glutathione; the derivative of glutathione, SAMe,



Main Products

    GSH white powder 3               SAG white powder 1             NAD 2       

L-Glutathione reduced(GSH)                S-Acetyl glutathione (SAG)                              NAD


NADH 1          Protein A 1              Protein G 1

NADH                                 Recombinant Protein A                       Recombinant Protein G

Products Description


Name: L-glutathione reduced, GSH

Formula: C10H17N3O6S

MW: 307.32

CAS: 70-18-8

Purity : ≥ 98.5% (HPLC)

Appearance: White crystalline powder

Storage: 2-8


Glutathione-The World’s Most Powerful Antioxidant in Your Body!

Every cell in your body requires an adequate supply to function and to stay healthy. It’s your body’s super defender against illness, infection, toxins, and disease. GSH is critical to optimum brain function, and is also your body’s first line of defense against diseases of aging and the harmful effects of stress and overexertion.

Glutathione is Essential to Health   Glutathione’s three major roles in the body are summarized by the letters A-B-C(Antioxidant, Blood Booster and Cell Detoxifier),these are the three critical processes driven by glutathione.

Why Should We Need GSH Supplement?

Research has shown that individuals who have low levels of glutathione are susceptible to chronic illness. Research shows that GSH levels decline by 8% to 12% per decade, beginning at the age of 20. Levels of glutathione are further reduced by continual stress upon the immune system such as illness, infection, and environmental toxins. As we now know, a lowered immune system can bring about illness and disease. This is a ferocious cycle. While you need glutathione for a productive immune system, a weakened immune system hampers the production of glutathione.


The Power of Glutathione

Glutathione has been shown to slow down the aging process, detoxify and improve liver function, strengthen the immune system, and reduce the chances of developing cancer. Glutathione also works to help improve mental functions, increase energy, improve concentration, permit increased exercise, and improve heart and lung function.


Glutathione is widely used in pharmaceuticals, health functional foods, dietary supplements, cosmetics etc.


NAD (Oxidized Coenzyme I):

Names: Nicotinamide adenine dinucleotide; Coenzyme; Co; NAD; NAD+.

Formula: C21H27N7O14P2

MW: 663.43
: 53-84-9
Purity: ≥95% (ADH); ≥98% (HPLC)

Appearance: White powder



Nicotinamide adenine dinucleotide, abbreviated NAD+, is a coenzyme found in all living cells.  The compound is a dinucleotide, since it consists of two nucleotides joined through their phosphate groups. One nucleotide contains an adenine base and the other nicotinamide



Nicotinamide adenine dinucleotide has several essential roles in metabolism. It acts as a coenzyme in redox reactions, as a donor of ADP-ribose moieties in ADP-ribosylation reactions, as a precursor of the second messenger molecule cyclic ADP-ribose, as well as acting as a substrate for bacterial DNA ligases and a group of enzymes called sirtuins that use NAD+ to remove acetyl groups from proteins. In addition to these metabolic functions, NAD+ emerges as an adenine nucleotide that can be released from cells spontaneously and by regulated mechanisms, and can therefore have important extracellular roles.

The enzymes that make and use NAD+ and NADH are important in both current pharmacology and the research into future treatments for disease. Drug design and drug development exploits NAD+ in three ways: as a direct target of drugs, by designing enzyme inhibitors or activators based on its structure that change the activity of NAD-dependent enzymes, and by trying to inhibit NAD+ biosynthesis.

The coenzyme NAD+ is not itself currently used as a treatment for any disease. However, it is potentially useful in the therapy of neurodegenerative diseases such as Alzheimer's and Parkinson disease.  NAD+ is also a direct target of the drug isoniazid, which is used in the treatment of tuberculosis, an infection caused by Mycobacterium tuberculosis. Isoniazid is a prodrug and once it has entered the bacteria, it is activated by a peroxidase, which oxidizes the compound into a free radical form. This radical then reacts with NADH, to produce adducts that are very potent inhibitors of the enzymes enoyl-acyl carrier protein reductase, and dihydrofolate reductase. In December 2013 a remarkable result concerning the ability of NAD to reverse mitochondrial aging was reported by a team led by David Sinclair. In an experiment with mice, Sinclair found that 2-year-old mice given NAD for just one week had significantly improved nuclear-mitochrondrial communication.


NAD is widely used in drugs, research, diagnostic, dietary supplement , synthesis etc.


Name: β-Nicotinamide adenine dinucleotide , reduced form (disodium salt)

Formula: C21H27N7O14P2Na2

MW: 709.4

CAS: 606-68-6

Purity: ≥95% (ADH); ≥98% (HPLC)

Appearance: White powder


What is NADH ? 

NADH, biologically known as Coenzyme 1, is the reduced form of nicotinamide adenine dinucleotide (NAD) with the addition of high energy hydrogen (H), which provides energy to the cell. NADH is necessary for thousands of biochemical reactions within the body and is found naturally in every living cell. NADH plays a key role in the energy production of cells, particularly in the brain and central nervous system. The more NADH a cell has available, the more energy it can produce to perform its process efficiently. NADH stimulates cellular production of the eurotransmitters Dopamine, Noradrenaline, and Serotonin, thereby improving mental clarity, alertness and concentration.NADH is directly involved in the body’s cellular immune defense system and the more NADH in your body, the better the DNA repair system functions.

NADH in Food and Dietary Sources

NADH is present in every living cell, animal or plant.

It should be noted that most NADH we take in from foods is destroyed during the cooking process. Even if our diets consisted mostly of raw meat or fish, the greater part of the NADH present in these foods would be degraded by the stomach gastric acid system in our bodies.

Dietary supplement

NADH (nicotinamide adenine dinucleotide) is an amazing dietary supplement that has an abundance of beneficial effects on a cellular level. Many individuals take NADH as an energy supplement because it can effectively increase ATP production. ATP, or adenosine triphosphate, is the primary energy carrier of the body. NADH plays a key role in cellular energy production, particularly in the brain and central nervous system.

NADH is widely used to help supplement many cases involving Chronic Fatigue Syndrome (CFS), Fibromyalgia, Parkinsons, Alzheimers, Depression, Jet Lag, ADHD (Attention Deficit Hyperactivity Disorder), and more. What was commonly used to help relieve symptoms of conditions resulting in lack of energy, is now used by executives, athletes, and everyday people to increase energy, improve mental clarity, and improve physical performance. NADH also is a vital part in making the popular supplement CoQ10 effective into an antioxidant. NADH is taken regularly by hundreds of thousands of people worldwide who experience positive results from its natural benefits.







Appearance: r




Protein A:

Name: Recombinant Protein A

MW:  22kD (SDS-PAGE;  see Fig.1)

pH range: 2.0-11.0

Purity: ≥98% SDS-PAGEHPLC

Activity: ≥95% (human IgG binding activity)

Appearance: White powder

Storage: 2-8


Figure 1 Protein A (SDS-PAGE)


Recombinant Protein A is a type I membrane protein covalently linked to the cell wall of most strains of the Gram-positive bacterium Staphylococcus aureus. It has high affinity to IgG from various species, for instance human, rabbit and guinea pig, but only weak interaction with bovine and mouse. Protein A interacts with antibodies through two distinct binding events: the “classical” binding site on the Fc portion of human IgG1, IgG2, and IgG4, and the “alternate” binding site found on the Fab portion of human IgG, IgM, IgA, and IgE that contain heavy chains of the VH3 subfamily.


The properties of protein A enables it as a powerful affinity ligand for several immunological and purification applications. High selectivity and good physiochemical stability have made protein A the preferred generic ligand for affinity purification of antibodies and molecules tagged with an antibody Fc-region. Protein A can also be used in various immunochemical assays including Western blotting, immunohistochemistry, and ELISA applications by conjugation with different reporter molecules, such as fluorescent dyes (FITC), enzyme markers (peroxidase, β-galactosidase, alkaline phosphatase), biotin, and colloidal gold. Immunoprecipitation studies with protein A conjugated to beads are also commonly used to purify proteins or protein complexes indirectly through antibodies against the protein or protein complex of interest.

                                  Figure 2Protein G (SDS-PAGE)

Protein G

Name : Recombinant Protein G

FW : 25kd (SDS-PAGE, see Fig.2)

pH range : 2.0-11.0

Purity : ≥98% (HPLC)

Appearance : White powder

Storage : 2-8


Protein G is a bacterial cell wall protein expressed at the cell surface of certain group C and group G Streptococcal strains.

It has affinity for both Fab- and Fc-fragments of human IgG by independent and separate binding sites. Binding to the Fc region of immunoglobulins from several species by a non-immune mechanism exhibits great affinity for almost all mammalian immunoglobulin G (IgG) classes, including all human IgG subclasses (IgG1, IgG2, IgG3 and IgG4) and also rabbit, mouse, and goat IgG. Protein G bound all tested monoclonal IgG from mouse IgG1, IgG2a, and IgG3, and rat IgG2a, IgG2b, and IgG2c. In addition, polyclonal IgG from man, cow, rabbit, goat, rat, and mouse bound to protein G, whereas chicken IgG did not. Protein G has also been shown to bind human serum albumin but at a site that is structurally separated from the IgG-binding region. Protein G shows a broader range of binding to IgG subclasses than staphylococcal protein A. This applies to polyclonal IgG from cow, rat, goat, human and rabbit sources as well as several of rat and mouse monoclonal antibodies.


Protein G was found to be a powerful reagent for the detection of IgG, and consequently the antigen against which these antibodies are directed. It was used in Western blot analyses to detect various antigen-antibody complexes on nitrocellulose membranes. Moreover, protein G is widely used as a ligand coupled to resins in affinity chromatography for antibody purification.