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Home > Products >  China Largest factory Manufacturer Supply Kallikrein CAS 9001-01-8

China Largest factory Manufacturer Supply Kallikrein CAS 9001-01-8 CAS NO.9001-01-8

  • FOB Price: USD: 1.00-3.00 /Kilogram Get Latest Price
  • Min.Order: 1 Kilogram
  • Payment Terms: L/C,D/A,D/P,T/T,MoneyGram,Other
  • Available Specifications:

    AAAAA(1-100)KilogramAAAAA(100-500)KilogramAAAAA(1000-5000)Kilogram

  • Product Details

Keywords

  • Kallikrein
  • Kallikrein
  • 9001-01-8

Quick Details

  • ProName: China Largest factory Manufacturer Sup...
  • CasNo: 9001-01-8
  • Molecular Formula: 9001-01-8
  • Appearance: POWDER
  • Application: Pharm chemicals industry
  • DeliveryTime: 3-5 days
  • PackAge: 25KG/Drum
  • Port: Shanghai Guangzhou Qingdao Shenzhen
  • ProductionCapacity: 1000 Kilogram/Day
  • Purity: 99.9%
  • Storage: 2-8°C
  • Transportation: By air /Sea/ coruier
  • LimitNum: 1 Kilogram
  • Heavy metal: 10PPM
  • Grade: Industrial Grade
  • Color: white
  • Melting point: ≥350°C
  • Boiling point: 363.24°C (rough estimate)
  • density: 1.667
  • solubility: 1 M NaOH: 10 mg/mL, dark green
  • Water Solubility: <0.1 g/100 mL at 21 oC
  • Stability: Stable. Combustible. Incompatible with...

Superiority

                          About Product Technical Details 

Product Name: Kallikrein
Synonyms: KININOGEN HIGH MOLECULAR WEIGHT, TWO CHAIN;KININOGEN, HIGH MOLECULAR WEIGHT, TWO CHAIN, HUMAN;KININOGEN, HIGH MOLECULAR WEIGHT, TWO CHAIN, HUMAN PLASMA;KININOGEN, HUMAN, HIGH MW, DOUBLE CHAIN;KININOGENIN;KININOGEN, LOW MOLECULAR WEIGHT;2HK;bradykini
CAS: 9001-01-8
MF:  
MW: 0
EINECS: 232-574-5
Product Categories:  
Mol File: Mol File
Kallikrein Structure
 
Kallikrein Chemical Properties
storage temp.  2-8°C
form  lyophilized powder
 
Safety Information
Hazard Codes  B
WGK Germany  3
RTECS  NZ2017050
MSDS Information
Provider Language
SigmaAldrich English
 
Kallikrein Usage And Synthesis
Structure Plasma kallikrein possesses a unique structure in vertebrates and is composed of four apple domains followed by a trypsin domain. The apple domain is a conserved protein folding with three disulfide bridges, and is often found on diverse proteins for protein-protein or protein-carbohydrate interactions. The apple domains on KLKB1 interact with the D6 domain of molecular weight kininogen (HMW-KNG), which is highly glycosylated. In teleost genomes, the KLKB1-like gene is absent and only lectins with four apple domains but no trypsin domain were found. These lectins were not found in other vertebrates, suggesting that the two genes could share the same origin but the trypsin domain was lost in the teleost lineage during evolution. Tissue kallikreins possess a single trypsin domain and are closely related to other serine proteases. It is not clear what enzyme is involved in the cleavage of KNG to form bradykinin (BK) in the fish and lamprey, given that KLKB1 and KLK are not identified.

                                  About Our Group

Since 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 Factories Production Lines

                                                   Our Factories R&D ability

                        Our Factories warehouse 

                

Details

                                                       More Product Information

Product Name: Kallikrein
Synonyms: KININOGEN HIGH MOLECULAR WEIGHT, TWO CHAIN;KININOGEN, HIGH MOLECULAR WEIGHT, TWO CHAIN, HUMAN;KININOGEN, HIGH MOLECULAR WEIGHT, TWO CHAIN, HUMAN PLASMA;KININOGEN, HUMAN, HIGH MW, DOUBLE CHAIN;KININOGENIN;KININOGEN, LOW MOLECULAR WEIGHT;2HK;bradykini
CAS: 9001-01-8
MF:  
MW: 0
EINECS: 232-574-5
Product Categories:  
Mol File: Mol File
Kallikrein Structure
 
Kallikrein Chemical Properties
storage temp.  2-8°C
form  lyophilized powder
 
Safety Information
Hazard Codes  B
WGK Germany  3
RTECS  NZ2017050
MSDS Information
Provider Language
SigmaAldrich English
 
Kallikrein Usage And Synthesis
Structure Plasma kallikrein possesses a unique structure in vertebrates and is composed of four apple domains followed by a trypsin domain. The apple domain is a conserved protein folding with three disulfide bridges, and is often found on diverse proteins for protein-protein or protein-carbohydrate interactions. The apple domains on KLKB1 interact with the D6 domain of molecular weight kininogen (HMW-KNG), which is highly glycosylated. In teleost genomes, the KLKB1-like gene is absent and only lectins with four apple domains but no trypsin domain were found. These lectins were not found in other vertebrates, suggesting that the two genes could share the same origin but the trypsin domain was lost in the teleost lineage during evolution. Tissue kallikreins possess a single trypsin domain and are closely related to other serine proteases. It is not clear what enzyme is involved in the cleavage of KNG to form bradykinin (BK) in the fish and lamprey, given that KLKB1 and KLK are not identified.

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