CAS 9002-07-7 Trypsin Sterile-Filtered Bioreagent Suitable for Cell Culture

• Customization: Available
• CAS No.: 9002-07-7
• Formula: C35h47n7o10
• Model NO.: YB126
• EINECS: 232-650-8
• Environmental Protection: No
• Certification: ISO9001
• Color: White
• Classification: Coenzyme
• Function: Catalysis
• Appearance: Powder
• Type: Pharmaceutical Intermediates
• Quality: Refined
• Colour: White
• Samples: Available
• Certificates: ISO9001/SGS
• Package: 1kg/5kg/10kg/25kg
• Stocks: in Stock
• Lead Time: 5-7 Working Days
• Shelf Life: 2-3 Years
• Site Audit: Available
• Transport: Air/Express/Sea
• MOQ: 1 Unit
• Payment Method: LC/Tt/DAP/OA
• Form: Powder
• Purity: 99%
• Transport Package: Drum/Bottle/Bags
• Specification: 250USPu/mg
• Trademark: Yunbang OEM
• Origin: China

Product Description

CAS 9002-07-7 Trypsin sterile-filtered  BioReagent suitable for cell culture

 

Company Informations

Hunan Yunbang Pharmaceutical Co., Ltd. (Yunbangpharm) located in Changsha High-tech Industrial Park, Hunan. It is a high-tech enterprise specializing in the research and development, production and sales of Pharmaceutical raw materials, Pharmaceutical intermediates(API) and Fine chemicals. Based in China, Yunbangpharm has been providing suitable solutions for many domestic,foreign pharmaceutical companies and traders. Excellent quality, good reputation and authentic price have won the praise of the majority of customers.

The company adheres to the corporate tenet of "We do not produce medicines, but help pharmaceutical companies make good medicines".

We can provide customers with customized processing, research and development services;
We can develop high-end Pharmaceutical and chemical products with high technical difficulties,high barriers and unique production processes;
We can provide 100 grams Grade, kilograms, and hundred kilograms of raw material pharmaceutical intermediates and other products.
We can perform -100°C to 300°C reaction.

R&D strength is the company's core competitiveness.Yunbangpharm has maintains a good cooperation relationship with many Universities and Research institutes locally, which can quickly transform R&D results into industrial production.

Our goal : To achieve the integrated upgrade of Pharmaceutical intermediates, raw materials and high-end chemical products, adhere to "serving pharmaceutical companies, creating our brands" to provide customers with high-quality and low-cost pharmaceutical and chemical products, realizing Win-win cooperation and common development.
 

Product Description

Trypsin is a serine protease enzyme that plays a key role in the digestion of proteins. It is produced in the pancreas as an inactive zymogen called trypsinogen, which is then activated in the small intestine by the enzyme enterokinase. Once activated, trypsin is responsible for cleaving peptide bonds on the carboxyl side of the amino acids lysine and arginine. This enzyme is widely used in biochemical and biotechnology research, as well as in various industrial processes such as the production of protein hydrolysates and in cell culture applications. Trypsin is available in purified form for laboratory use and is an important tool for studying protein structure and function.

Application

For trypsin digestion of peptides, use a ratio of about 1:100 to 1:20 for trypsin:peptide. The typical use for this product is in removing adherent cells from a culture surface. The concentration of trypsin necessary to dislodge cells from their substrate is dependent primarily on the cell type and the age of the culture. Trypsins have also been used for the re-suspension of cells during cell culture, in proteomics research for digestion of proteins and in various in-gel digestions. Additional applications include assessing crystallization by membrane-based techniques and in a study to determine that protein folding rates and yields can be limited by the presence of kinetic traps.

Biochem/physiol Actions

Trypsin cleaves peptides on the C-terminal side of lysine and arginine residues. The rate of hydrolysis of this reaction is slowed if an acidic residue is on either side of the cleavage site and hydrolysis is stopped if a proline residue is on the carboxyl side of the cleavage site. The optimal pH for trypsin activity is 7-9. Trypsin can also act to cleave ester and amide linkages of synthetic derivatives of amino acids. EDTA is added to trypsin solutions as a chelating agent that neutralizes calcium and magnesium ions that obscure the peptide bonds on which trypsin acts. Removing these ions increases the enzymatic activity.

Serine protease inhibitors, including DFP, TLCK, APMSF, AEBSEF, and aprotinin, amongst others, will inhibit Trypsin.
 

FAQ

1:Can I get some samples before bulk order?
A: Most products provide free samples, but the shipping cost be paid by customers.

2: What's your MOQ?
A: We can have a discussion.

3: Which kind of payment terms do you accept?
A: PI will be sent first after confirmation of order,enclosed our bank information.Payment by T/T, Western Union,D/P, ETC.

4.How to place an order?
A: You can contact me through Trademanager, WhatsApp, Email and other contact methods, tell me the product and quantity you need, and then we will give you a quote.

5:How about your delivery time?
A: Generally, it will take 3 to 5 days after receiving your advance payment.

6:How do you treat quality complaint?
A: First of all, our quality control will reduce the quality problem to near zero. If there is a real quality problem caused by us, we will send you free goods for replacement or refund your loss.

Our Advantages

1. 90days quality guarantee for exchange.

2. For each batch order extracts, we will attach a factory Inspection Report with the goods delivery , including the BatchNo/ Date/ Test index ects; also will keep the archived extracts to ensure received by customers are the same each time.

3. Our team of experienced professionals are available online 24 hours a day to answer any questions and provide guidance on product usage and maintenance.
 

Product analysis

 

 

 

Product Name:	Trypsin
Synonyms:	Trypsin-EDTA Solution 1X;α-and β-trypsin;Tryprar;Trypsevas;Trypsin Powder, Porcine 1:250;TRYPSIN TYPE V-S: ACETYLATED FROM*BOVINE PANCREAS;TRYPSIN, PROTEOMICS SEQUENCING GRADE;TRYPSIN-EDTA SOLUTION FOR ENDOTHELIAL*CE LL CULTURES
CAS:	9002-07-7
MF:	C35H47N7O10
MW:	725.78858
EINECS:	232-650-8
Mol File:	9002-07-7.mol

Melting point	115°C
density	1.37[at 20ºC]
vapor pressure	0Pa at 25ºC
storage temp.	-20°C
solubility	Reconstitute in aqueous buffer
form	lyophilized powder
pka	pK1:6.25 (25°C,μ=0.1)
color	White powder
Odor	Odorless
Water Solubility	Soluble in water (10 mg/ml), phosphate buffers (10 mg/ml), and balanced salt solutions (1 mg/ml).
Merck	13,9865
Stability:	Stable. Incompatible with strong oxidizing agents.
LogP	-1.3 at 20ºC
CAS DataBase Reference	9002-07-7
EPA Substance Registry System	Trypsin (9002-07-7)

Hazard Codes	Xn,B
Risk Statements	36/37/38-42-42/43
Safety Statements	22-24-26-36/37-45-23
WGK Germany	2
RTECS	GC3050000
F	1-3-10
TSCA	Yes
HS Code	35079090
Hazardous Substances Data	9002-07-7(Hazardous Substances Data)

 

Chemical Properties	White or almost white, crystalline or amorphous powder, hygroscopic if amorphous.
Uses	Proteolytic enzyme.
Uses	Trypsin is a digestive enzyme found in the digestive system. The enzyme catalyzes the hydrolysis of peptide bonds breaking down proteins into smaller peptides.
Uses	Trypsin-EDTA Solution 10X has been used to release adherent cells from tissue culture plates for passaging.
Brand name	Parenzyme;Trypsillin.
General Description	Trypsin is applicable for tissue disaggregation, due to its effective action and tolerance towards different cell type and serum-induced neutralization.
Biochem/physiol Actions	Trypsin cleaves peptides on the C-terminal side of lysine and arginine residues. The rate of hydrolysis of this reaction is slowed if an acidic residue is on either side of the cleavage site and hydrolysis is stopped if a proline residue is on the carboxyl side of the cleavage site. The optimal pH for trypsin activity is 7-9. Trypsin can also act to cleave ester and amide linkages of synthetic derivatives of amino acids. EDTA is added to trypsin solutions as a chelating agent that neutralizes calcium and magnesium ions that obscure the peptide bonds on which trypsin acts. Removing these ions increases the enzymatic activity. Serine protease inhibitors, including DFP, TLCK, APMSF, AEBSEF, and aprotinin, amongst others, will inhibit Trypsin.

 

Detailed Photos