China Largest Manufacturer factory sales BOVINE HEMOGLOBIN POWDER CAS 9008-02-0 CAS NO.9008-02-0

                                PRODUCT DETAILS       

HEMOGLOBIN Basic information Product Name: HEMOGLOBIN Synonyms: Hemoglobin from porcine blood;Hemoglobin from turkey ;Hemoglobin from rat,Hb;Hemoglobin porcine,Hb;Hemoglobin human,Hb;Hemoglobin (Bovine, 2*cryst);HEMOGLOBIN FROM BOVINE BLOOD, PGE. WITH 100 G*;HEMOGLOBIN DOG CAS: 9008-02-0 MF: C13H10N2O2 MW: 226.2307 EINECS: 293-254-9 Product Categories: Nitric Oxide Scavengers;Nitric Oxide ScavengersCell Signaling Enzymes;Nitric Oxide and Cell Stress;Nitric Oxide Metabolism Mol File: 9008-02-0.mol   HEMOGLOBIN Chemical Properties storage temp.  2-8°C solubility  0.6 M HCl: soluble20mg/mL form  substrate powder color  Dark brown powder Water Solubility  Soluble in water. EPA Substance Registry System Hemoglobins (9008-02-0)   Safety Information Hazard Codes  B Safety Statements  22-24/25 WGK Germany  3 F  1-10 TSCA  Yes HS Code  3002905150 MSDS Information Provider Language SigmaAldrich English   HEMOGLOBIN Usage And Synthesis Description Haemoglobin, the oxygen-transport protein in the red blood cells, is a tetramer and each of the four chains contains a haeme group. It is interesting to note that the four haeme groups in haemoglobin do not operate independently. The release (and binding) of oxygen is a cooperative process, which means that the loss (uptake) of the first oxygen molecule triggers the release of the remaining three. The current model for oxygen binding in haemoglobin and myoglobin can be explained in the following way. The deoxy form contains a high-spin Fe(II) centre, which, because of its size, does not form a plane with its four nitrogen donor atoms. Instead, it is located slightly above the plane, drawn towards the His residue. Once oxygen enters trans to the His residue, the iron centre is oxidised to a low-spin Fe3+ centre and O2 is reduced to [O2]-. Both species contain an unpaired electron. The low-spin Fe3+ moves into the plane and pulls the His residue down. This affects the remaining protein chain and triggers the uptake/release of oxygen in the other three haeme groups. Uses Hemoglobin is the most important respiratory protein of vertebrates by virtue of its ability to transport oxygen from the lungs to body tissues, and to facilitate the return transport of carbon dioxide. It is used as a coloring agent for pet foods, a natural source of iron for nutraceuticals, a protein source for non-ruminant animals, and as a raw material for pharmaceutical porphyrin derivative production. Uses Medicine, usually called hemoglobin. Uses Hemoglobin from bovine blood has been used in: standard curve generation for the quantification intraparenchymal hemorrhage and parenchymal hemorrhage in spinal cord homogenate using Drabkin′s assay, Quadrupole-Ion Mobility-Time-of-Flight mass spectrometery the generation of molecularly imprinted polymers (MIPs) to mimic high molecular-weight polyethylene glycol (PEG) in crystallization studies Definition The respiratory protein of the red blood cells, it transfers oxygen from the lungs to the tissues and carbon dioxide from the tissues to the lungs. Its affinity for carbon monoxide is >200 times that for oxygen. Hemoglobin is a conjugated protein of molec Definition The pigment of the red blood cells that is responsible for the transport of oxygen from the lungs to the tissues. It consists of a basic protein, globin, linked with four heme groups. Heme is a complex compound containing an iron atom. The most important property of hemoglobin is its ability to combine reversibly with one molecule of oxygen per iron atom to form oxyhemoglobin, which has a bright red color. The iron is present in the divalent state (iron(II)) and this remains unchanged with the binding of oxygen. There are variations in the polypeptide chains, giving rise to different types of hemoglobins in different species. The binding of oxygen depends on the oxygen partial pressure; high pressure favors formation of oxyhemoglobin and low pressure favors release of oxygen. Definition One of a group ofglobular proteins occurring widely inanimals as oxygen carriers in blood.Vertebrate haemoglobin comprisestwo pairs of polypeptide chains,known as α-chains and β-chains(forming the globin protein), witheach chain folded to provide a bindingsite for a haem group. Each ofthe four haem groups binds oneoxygen molecule to form oxyhaemoglobin.Dissociation occurs inoxygen-depleted tissues: oxygen is releasedand haemoglobin is reformed.The haem groups also bind other inorganicmolecules, including carbonmonoxide (to form carboxyhaemoglobin).In vertebrates, haemoglobinis contained in the red blood cells(erythrocytes). General Description Native hemoglobin from bovine erythrocytes. A major oxygen-transporting component of red blood cells that is also nitric oxide scavenger. Blocks carbachol-stimulated cGMP production. This preparation contains primarily Ferric-hemoglobin and must be reduced to the ferrous form to bind molecular oxygen. Note: this preparation contains primarily ferric-hemoglobin and must be reduced to the ferrous form to bind molecular oxygen. Biochem/physiol Actions The Fe2+/Fe3+ balance is a physiological indicator of blood oxygenation. Deoxygenated hemoglobin accessorizes a feedback loop by reducing nitrite to NO, a vasodilator which enhances blood flow to oxygen-deprived tissues. Purification Methods Purify it from blood using CM-32 cellulose column chromatography. [Matsukawa et al. J Am Chem Soc 107 1108 1985.] For the purification of the  and  chains see Hill et al. Biochemical Preparations 10 55 1963. Histones (from S4A mouse lymphoma). The purification of histones uses a macroprocess column, heptafluorobutyric acid as solubilising and ion-pairing agent and an acetonitrile gradient. [McCroskey et al. Anal Biochem 163 427 1987.]   HEMOGLOBIN Preparation Products And Raw materials Preparation Products L-Leucine-->Chorionic Gonadotropin-->L-Histidine hydrochloride monohydrate-->Superoxide dismutase-->Hematoprophyrin-->hemoglobin, Vitreoscilla-->L-Histidine hydrochloride

                                                                         About US 

Leader Biochemical Group is a large leader incorporated industry manufacturers and suppliers of advanced refined raw materials From the year of 1996 when our factory was put into production to year of 2020, our group has successively invested in more than 52 factories with shares and subordinates.We focus on manufacture Pharm & chemicals, functional active ingredients, nutritional Ingredients, health care products, cosmetics, pharmaceutical and refined feed, oil, natural plant ingredients industries to provide top quality of GMP standards products.All the invested factories' product lines cover API and intermediates, vitamins, amino acids, plant extracts, daily chemical products, cosmetics raw materials, nutrition and health care products, food additives, feed additives, essential oil products, fine chemical products and agricultural chemical raw materials And flavors and fragrances. Especially in the field of vitamins, amino acids, pharmaceutical raw materials and cosmetic raw materials, we have more than 20 years of production and sales experience. All products meet the requirements of high international export standards and have been recognized by customers all over the world. Our manufacture basement & R&D center located in National Aerospace Economic & Technical Development Zone Xi`an Shaanxi China. Now not only relying on self-cultivation and development as well as maintains good cooperative relations with many famous research institutes and universities in China. Now, we have closely cooperation with Shanghai Institute of Organic Chemistry of Chinese Academy of Science, Beijing Institute of Material Medical of Chinese Academy of Medical Science, China Pharmaceutical University, Zhejiang University. Closely cooperation with them not only integrating Science and technology resources, but also increasing the R&D speed and improving our R&D power. Offering Powerful Tech supporting Platform for group development. Keep serve the manufacture and the market as the R&D central task, focus on the technical research.  Now there are 3 technology R & D platforms including biological extract, microorganism fermentation and chemical synthesis, and can independently research and develop kinds of difficult APIs and pharmaceutical intermediates. With the strong support of China State Institute of Pharmaceutical Industry (hereinafter short for CSIPI), earlier known as Shanghai Institute of Pharmaceutical Industry (SIPI), we have unique advantages in the R & D and industrialization of high-grade, precision and advanced products.  Now our Group technical force is abundant, existing staff more that 1000 people, senior professional and technical staff accounted for more than 50% of the total number of employees, including 15 PhD research and development personnel, 5 master′ S degree in technical and management personnel 9 people. We have advanced equipment like fermentation equipment and technology also extraction, isolation, purification, synthesis with rich production experience and strict quality control system, According to the GMP required, quickly transforming the R&D results to industrial production in time, it is our advantages and our products are exported to North and South America, Europe, Middle East, Africa, and other five continents and scale the forefront in the nation, won good international reputation.  We believe only good quality can bring good cooperation, quality is our key spirit during our production, we are warmly welcome clients and partner from all over the world contact us for everlasting cooperation, Leader will be your strong, sincere and reliable partner in China.

                                                                      Our Group profiles

Our Factories production lines

                                                   Our Factories R&D ability

                        Our Factories warehouse 

                                                       Product information

HEMOGLOBIN Basic information Product Name: HEMOGLOBIN Synonyms: Hemoglobin from porcine blood;Hemoglobin from turkey ;Hemoglobin from rat,Hb;Hemoglobin porcine,Hb;Hemoglobin human,Hb;Hemoglobin (Bovine, 2*cryst);HEMOGLOBIN FROM BOVINE BLOOD, PGE. WITH 100 G*;HEMOGLOBIN DOG CAS: 9008-02-0 MF: C13H10N2O2 MW: 226.2307 EINECS: 293-254-9 Product Categories: Nitric Oxide Scavengers;Nitric Oxide ScavengersCell Signaling Enzymes;Nitric Oxide and Cell Stress;Nitric Oxide Metabolism Mol File: 9008-02-0.mol   HEMOGLOBIN Chemical Properties storage temp.  2-8°C solubility  0.6 M HCl: soluble20mg/mL form  substrate powder color  Dark brown powder Water Solubility  Soluble in water. EPA Substance Registry System Hemoglobins (9008-02-0)   Safety Information Hazard Codes  B Safety Statements  22-24/25 WGK Germany  3 F  1-10 TSCA  Yes HS Code  3002905150 MSDS Information Provider Language SigmaAldrich English   HEMOGLOBIN Usage And Synthesis Description Haemoglobin, the oxygen-transport protein in the red blood cells, is a tetramer and each of the four chains contains a haeme group. It is interesting to note that the four haeme groups in haemoglobin do not operate independently. The release (and binding) of oxygen is a cooperative process, which means that the loss (uptake) of the first oxygen molecule triggers the release of the remaining three. The current model for oxygen binding in haemoglobin and myoglobin can be explained in the following way. The deoxy form contains a high-spin Fe(II) centre, which, because of its size, does not form a plane with its four nitrogen donor atoms. Instead, it is located slightly above the plane, drawn towards the His residue. Once oxygen enters trans to the His residue, the iron centre is oxidised to a low-spin Fe3+ centre and O2 is reduced to [O2]-. Both species contain an unpaired electron. The low-spin Fe3+ moves into the plane and pulls the His residue down. This affects the remaining protein chain and triggers the uptake/release of oxygen in the other three haeme groups. Uses Hemoglobin is the most important respiratory protein of vertebrates by virtue of its ability to transport oxygen from the lungs to body tissues, and to facilitate the return transport of carbon dioxide. It is used as a coloring agent for pet foods, a natural source of iron for nutraceuticals, a protein source for non-ruminant animals, and as a raw material for pharmaceutical porphyrin derivative production. Uses Medicine, usually called hemoglobin. Uses Hemoglobin from bovine blood has been used in: standard curve generation for the quantification intraparenchymal hemorrhage and parenchymal hemorrhage in spinal cord homogenate using Drabkin′s assay, Quadrupole-Ion Mobility-Time-of-Flight mass spectrometery the generation of molecularly imprinted polymers (MIPs) to mimic high molecular-weight polyethylene glycol (PEG) in crystallization studies Definition The respiratory protein of the red blood cells, it transfers oxygen from the lungs to the tissues and carbon dioxide from the tissues to the lungs. Its affinity for carbon monoxide is >200 times that for oxygen. Hemoglobin is a conjugated protein of molec Definition The pigment of the red blood cells that is responsible for the transport of oxygen from the lungs to the tissues. It consists of a basic protein, globin, linked with four heme groups. Heme is a complex compound containing an iron atom. The most important property of hemoglobin is its ability to combine reversibly with one molecule of oxygen per iron atom to form oxyhemoglobin, which has a bright red color. The iron is present in the divalent state (iron(II)) and this remains unchanged with the binding of oxygen. There are variations in the polypeptide chains, giving rise to different types of hemoglobins in different species. The binding of oxygen depends on the oxygen partial pressure; high pressure favors formation of oxyhemoglobin and low pressure favors release of oxygen. Definition One of a group ofglobular proteins occurring widely inanimals as oxygen carriers in blood.Vertebrate haemoglobin comprisestwo pairs of polypeptide chains,known as α-chains and β-chains(forming the globin protein), witheach chain folded to provide a bindingsite for a haem group. Each ofthe four haem groups binds oneoxygen molecule to form oxyhaemoglobin.Dissociation occurs inoxygen-depleted tissues: oxygen is releasedand haemoglobin is reformed.The haem groups also bind other inorganicmolecules, including carbonmonoxide (to form carboxyhaemoglobin).In vertebrates, haemoglobinis contained in the red blood cells(erythrocytes). General Description Native hemoglobin from bovine erythrocytes. A major oxygen-transporting component of red blood cells that is also nitric oxide scavenger. Blocks carbachol-stimulated cGMP production. This preparation contains primarily Ferric-hemoglobin and must be reduced to the ferrous form to bind molecular oxygen. Note: this preparation contains primarily ferric-hemoglobin and must be reduced to the ferrous form to bind molecular oxygen. Biochem/physiol Actions The Fe2+/Fe3+ balance is a physiological indicator of blood oxygenation. Deoxygenated hemoglobin accessorizes a feedback loop by reducing nitrite to NO, a vasodilator which enhances blood flow to oxygen-deprived tissues. Purification Methods Purify it from blood using CM-32 cellulose column chromatography. [Matsukawa et al. J Am Chem Soc 107 1108 1985.] For the purification of the  and  chains see Hill et al. Biochemical Preparations 10 55 1963. Histones (from S4A mouse lymphoma). The purification of histones uses a macroprocess column, heptafluorobutyric acid as solubilising and ion-pairing agent and an acetonitrile gradient. [McCroskey et al. Anal Biochem 163 427 1987.]   HEMOGLOBIN Preparation Products And Raw materials Preparation Products L-Leucine-->Chorionic Gonadotropin-->L-Histidine hydrochloride monohydrate-->Superoxide dismutase-->Hematoprophyrin-->hemoglobin, Vitreoscilla-->L-Histidine hydrochloride