Chilled Seasoning Products is a food additive used for flavoring, just like wasabi/horseradish/mustard, ginger puree and garlic puree in Artisan Foods.
A chilled seasonging products is a dried seed, fruit, root, bark, or vegetable substance primarily used for flavoring, coloring or preserving food. Sometimes a chilled seasoning products is used to mask other flavors, and some spices have antimicrobial properties.
Weifang Artisan Foods specialized in fresh and Frozen Ginger, garlic, wasabi and spice for 16 years, and we corporate with many customers such as Metro(Japan), 7-eleven, SMZ products,etc. With BRC/ GAP/ TNC/ HACCP/ ISO9001/ JAS certificates, the market share of our products is No.1 in Japan, especially in the field of ginger, garlic,solo garlic and peeled garlic. We have been focusing on Japanese market before 2014, but now we decide to develop international market. In fact, we have already cooperated with many European and American customers since 2014.
Artisan Foods aims to provide safe, delicious, high-quality food at affordable price. In order to make sure that the quality of all products can be confirmed or tested immediately from the planting to processing and logistic, traceability system have been introduced by Artisan Foods.
Chilled Seasoning Products Seasoning Food,Seasoning Sauce,Seasoning Sushi Jar,Meat Seasoning WEIFANG ARTISAN FOODS CO.,LTD. , http://www.artisanfoods-wf.com
Although the company, Ablynx, has only 45 people, 33 of them are scientists and bioengineers. These people share the common ideal: to find the smallest segment of antibody protein that can replace the entire antibody and convert this minimal protein. Cheng can create billions of dollars in medicine, in other words, create the world's first new nano-antibody medicine for the treatment of cancer, rheumatoid arthritis, enteritis and other diseases, and even treat Alzheimer's disease.
Ablynx's success has benefited from the combined effects of three factors: rapid advances in antibody therapeutics, problems plaguing complex antibody drugs, and unique insights of the company's scientists about the related biological knowledge of the camel family.
Antibody drugs surged into the body, except for the brain, the most complicated part being the immune system. In a sense, we are actually living in a world where "bacteria can eat people." Various bacteria have never swiftly eroded us, treating us as the best place for their progeny to help us and serve us. Defenders are antibodies. Antibodies are Y-shaped proteins produced by fully armed B cells and live in blood and intercellular fluids. Each antibody model bears a mission to identify other molecules encountered through chemical tactile sensations. When the immune system is eroded by microorganisms, allergens, or toxins it emits a unique chemical signal that activates our own defense system.
Although our immune system has complex self-defense features, our bodies still suffer from different diseases. In the case of cancer or respiratory viral infections, the immune system often responds slowly; when rejection occurs during organ transplantation or when asthma occurs, the immune system often overreacts; and the immune system sometimes mistakenly attacks normal human cells. Causes rheumatoid arthritis and other autoimmune-diminished diseases.
For decades, drug researchers have been trying to find artificial antibodies to overcome or alleviate these immune system diseases. Since the invention of a technology for mass production of monoclonal antibodies in 1975, only two kinds of antibody drugs have been approved by the US Food and Drug Administration in 20 years. The stalemate in the development of antibody drugs was not broken until 1997. By the end of 2004, 17 therapeutic antibody drugs had been approved by the U.S. Food and Drug Administration. The scope of treatment covered various diseases mentioned above. These drugs were only available in 2004. Year after year, it has created a high income of 11.2 billion U.S. dollars for pharmaceutical companies. At present, monoclonal antibodies are still in a stage of rapid development. There are still dozens of monoclonal antibodies in the stage of research and development and clinical experiments. Some scientists predict that 16 kinds of monoclonal antibody drugs will be listed in the next three years. In 2008, the global sales of monoclonal antibodies will exceed the 17 billion US dollars mark.
Ablynx said that by the end of next year, they will also start a phase 1 clinical trial of nanobody drugs, with a view to dividing the antibody drug from a large cake to a cup. Nanomolecules with a molecular weight of only 1/10 of the antibody and a few nanometers in length are likely to surpass current antibody drugs and produce new drugs in Alzheimer's disease and other disease areas, but Ablynx's current goal is to create a The best-selling antibodies in the market and superior nano-antibodies in terms of efficacy.
Antibody Drugs Face Difficult Problems Although monoclonal antibodies still have huge room for development, their high prices have brought a lot of trouble. According to reports, asthma patients spend $11,000 per year on asthma antibody drug Xolair; Remicade injections of eight doses of antibody antibody to rheumatoid arthritis require $4,600; and each cancer patient is in the antibody drug Heré„„ceptin every year. The cost was as high as 38,000 US dollars.
The main reason why monoclonal antibodies are so expensive is that their structure is too complex. According to the molecular weight standard, the antibody is a supermolecular substance, and each molecule contains two sets of heavy and light chains and overlaps with the sugar molecules. Prior to the synthesis of monoclonal antibodies, it is usually necessary to isolate the antibodies from the mice and then humanize them. The process of humanization is very complicated. Human genes need to be embedded in mouse-derived antibodies, and protein fragments with the same amino acid sequence as human antibodies are compiled, partially or completely replacing the proteins in the mouse-derived antibodies. In addition, there are companies that have adapted transgenic mice to produce antibodies that are close to humanized. The purpose of humanization of antibodies is to reduce the side effects such as exclusivity in antibody treatment, but it needs to generate macromolecular proteins that cannot be synthesized by chemical methods like conventional drugs, and can only be used in bioreactors with synthetic monoclonal antibodies. A variety of mammalian cells are required for the cultivation of the gene. This process usually takes several months.
This method of cell culture makes it difficult for monoclonal antibodies to be produced on a large scale. Compared to chemical plants or microbial biosynthesis plants of the same scale, monoclonal antibody drugs consume much more capital in the construction and production process. In addition, drug companies must also ensure that the bioreactors are pure and protected against viruses that destroy valuable cells or contaminate the antibodies produced. Recent studies have shown that the combined production in the coming years is also far less than the market demand for monoclonal antibody drugs. All these factors have stimulated the rising prices of cloned drugs.
The macromolecular properties of antibody drugs also hamper their extensive use and efficacy. Monoclonal antibodies degrade under conditions of high temperatures and strong acids and bases and must be stored at absolute zero, otherwise they will lose their activity completely within a few weeks. Antibodies can be rapidly degraded by the digestive system, preventing them from entering the brain or the periphery of some tumors. Many diseases cannot be treated with monoclonal antibodies, and monoclonal antibodies are only administered by injection.
In some cases, the use of simpler, smaller protein molecules would be better under some circumstances where the monoclonal antibody drug does not work properly, even if it works properly, and at synthesis, manipulation, absorption, and price The aspect will have more advantages. This concept predicted the birth of nanobodies many years ago. If the three segments of the Y-antibody molecule are considered to be a trunk and two branches, in the 1980s, protein engineers obtained antibody fragments by removing the trunk or trunk and a branch to study antibody fragments instead of the entire antibody. Its function. These antibody fragments can also be therapeutically effective as whole antibodies by binding to toxins, pathogens, abnormal cell signals, or binding to cellular receptors of undesirable molecules. However, because some protein fragments in the Y-type structure are removed, antibody fragments cannot restore the function of other immune system components such as T cells.
The advantage of antibody fragments is that they can be synthesized by bacteria, yeast or fungi. This method is much cheaper than using mice to synthesize antibodies. Antibody fragments can also secretly enter the center of the tumor, which can be used as a carrier of radioactive isotopes or chemotherapy drugs. These drugs can be brought into the tumor cells to directly attack the tumor cells. In addition, antibody fragments can be broken down more rapidly or filtered from the blood. Compared with whole antibody drugs that last for several weeks in vivo, the half-life is only a few hours. This feature is advantageous when used as a carrier, but it is used as a drug. However, it is a major drawback. The duration of efficacy in the body is too short. This is why only one antibody fragment has been marketed in the United States so far.
To overcome this problem, many companies continue to modify antibody fragments, even leaving only one of the chain ends. Such an antibody terminal contains an important chemical component such as a complementarity determining region. The complementarity determining region determines the degree of closeness of binding of the target or antigen to be recognized by the antibody and the antibody antigen. The molecular weight of this single-chain antibody is already very close to that of Ablynx Nanobody. . However, since it is obtained from a macromolecular diabodies, the single-chain antibody has the same stickiness as the diabodies, and is easily aggregated in the body of the antibody-synthesizing bacteria and the patient using the antibody drug, thereby reducing the single-chain antibody. The efficiency of its synthesis and its efficacy.
Find Nanobodies on Camels
Ablynx obtained nanobodies from camels when biochemists reorganized antibody fragments to solve problems in antibody development. In 1989 when a founder of Ablynx Company participated in a wild surgery examination on how camels and buffaloes resisted parasitic diseases, after detecting antibodies isolated from camel blood, a special case was discovered: In addition to normal tetra-chain antibodies In addition, there are antibodies that contain only two heavy chains and are naturally occurring antibodies that are structurally simple. Ablynx published many years of research in its 1993 issue of Nature: Half of the antibodies in camel's blood have no light chains, and what is even more surprising is that these "heavy-chain antibodies" are like normal antibodies. It binds tightly to targets such as antigens, and it does not stick to each other like single-chain antibodies and even aggregate into blocks.
Camel is different from the secrets of other mammals in this feature. Although it is not known, the evolution of nature has provided a good solution for scientists to solve the difficult problems faced by antibodies and antibody fragments. Nanobodies are not only one-tenth the molecular weight of antibodies, but they are also more flexible in chemistry and can mesh with active sites of enzymes and cracks in cell membranes. Because nano-antibodies are much smaller than antibodies and do not have chemical hydrophobicity, they are more resistant to heat and acid and alkali. Rat experiments have shown that they can maintain stability and activity when they pass through the mouse's digestive system, enhance the possibility of oral administration of antibody drugs to treat diseases, and nanobodies can maintain stable efficacy at room temperature.
Nanobodies are much simpler in chemical composition and shape than antibodies. They can be encoded by a single gene and are more easily synthesized by microorganisms. In 2002, Dutch biologists brewed 1000 grams of sodium antibody in a 15,000-liter yeast reactor, and Ablynx said in a recent report that they have greatly increased the production of nanobodies produced by yeast reactors. One liter of litre is produced, so that a 15,000-liter reactor can brewed 15,000 grams of nanobody. Nanobody production is much easier, faster, and cheaper than the production of normal antibodies.
The greatest advantage of Nanobodies is that they are easier to bind to each other or to other compounds. Ablynx has combined antiserum nanoproteins with targeting proteins to extend its half-life in blood to weeks, increasing drug efficacy duration. The company also binds four nanobodies so that each molecule can bind to more antigens or bind to two different targets, increasing drug efficacy. Ablynx has also recently published their exciting research results. The nanobody they designed can bind to receptors on cancer cells and then bind to any tumor cells it encounters. Nanobodies of this type can also act as dual functions by binding each enzyme to an enzyme, converting the prodrug into a chemotherapeutic agent and killing the tumor cells. They divided the cancerous mice into two groups. One group was given chemotherapeutic drugs. As a result, the tumors only shrank a little; the other group was given dual-function nanobodies, and other nanobodies excluded rats and injected them with prodrugs. The result was chemotherapy. The more targeted, both to maintain normal cells, tumor cells can also be completely removed.
Small nanobody potential
In the current hotspot of the pharmaceutical industry, the development of therapeutic antibody drugs known as “biological missiles†is extremely active, but its common features are that its molecular structure is too large, its structure is too complex, and its price is too expensive, which limits its production and its clinical application. Promotion. In this regard, a Belgian biotechnology company said that their "nano-antibodies" extracted from camels will overcome these deficiencies, making them smaller and more effective, and are expected to cure more diseases, at a much lower price.