T4299
Trypsin-EDTA solution
1 ×, sterile-filtered, BioReagent, suitable for cell culture, 500 BAEE units porcine trypsin and 180 μg EDTA, 4Na per ml in Dulbecco′s PBS without calcium and magnesium
Szinonimák:
Cocoonase, Tryptar, Tryptase
Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez
Összes fotó(1)
About This Item
Javasolt termékek
biológiai forrás
Porcine pancreas
Minőségi szint
sterilitás
sterile-filtered
termékcsalád
BioReagent
Forma
solution
koncentráció
1 ×
technika/technikák
cell culture | mammalian: suitable
szennyeződések
Porcine parvovirus, none detected (9 CFR)
pH
7.0-7.6
kiszállítva
dry ice
tárolási hőmérséklet
−20°C
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Alkalmazás
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. It can be used with endothelial cell cultures.
Biokémiai/fiziológiai hatások
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.
Serine protease inhibitors, including DFP, TLCK, APMSF, AEBSEF, and aprotinin, amongst others, will inhibit Trypsin.
Komponensek
Trypsin consists of a single chain polypeptide of 223 amino acid residues, produced by the removal of the N-terminal hexapeptide from trypsinogen which is cleaved at the Lys - lle peptide bond. The sequence of amino acids is cross-linked by 6 disulfide bridges. This is the native form of trypsin, beta-trypsin. BETA-trypsin can be autolyzed, cleaving at the Lys - Ser residue, to produce alpha-trypsin. Trypsin is a member of the serine protease family.
Vigyázat
This product is stored frozen between -10 and -40°C. Repeated cycles of freezing and thawing should be avoided.
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kapcsolódó termék
Product No.
Leírás
Árazás
Tárolási osztály kódja
12 - Non Combustible Liquids
WGK
nwg
Lobbanási pont (F)
Not applicable
Lobbanási pont (C)
Not applicable
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Analitikai tanúsítványok (COA)
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Protocols
Trypsin is commonly used for dissociating adherent cells from surfaces. A wide variety of trypsin solutions are available to meet your specific cell line requirements.
Tudóscsoportunk valamennyi kutatási területen rendelkezik tapasztalattal, beleértve az élettudományt, az anyagtudományt, a kémiai szintézist, a kromatográfiát, az analitikát és még sok más területet.
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