T2610

StableCell™ Trypsin Solution

10X, sterile-filtered, BioReagent, suitable for cell culture, 5.0 g porcine trypsin and 2 g EDTA, 4Na per liter of 0.9% sodium chloride

Manufacturer: Sigma Aldrich

Synonym(S): Trypsin-EDTA solution

Select a Size

Pack Size SKU Availability Price
100 ML T2610-100-ML In Stock ₹ 5,316.90
500 ML T2610-500-ML In Stock ₹ 13,197.90

T2610 - 100 ML

₹ 5,316.90

In Stock

Quantity

1

Base Price: ₹ 5,316.90

GST (18%): ₹ 957.042

Total Price: ₹ 6,273.942

Quality Level

500

sterility

sterile-filtered

product line

BioReagent

concentration

10X

technique(s)

cell culture | mammalian: suitable

shipped in

wet ice

storage temp.

2-8°C

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Description

  • Application: 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.
  • 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.
  • Features and Benefits: StableCell™ trypsin is formulated as a gentle solution for cell detachment. Enzyme activity is retained when stored at 2-8°C, and our studies even show >90% activity is retained when left at room temperatures for up to 7 weeks!Save Time - no more freeze or thaw cyclesSave Space - store at 2-8°C and free up your freezerDoes not need to be aliquotedOnly the best for your cells - manufactured in GMP environment
  • Components: 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.
  • Preparation Note: Incubating cells with too high a trypsin concentration for a long period can damage cell membranes and kill the cells. Solubilizing trypsin or diluting it from a concentrated solution should be done with a buffered salt solution containing no Ca2+ or Mg2+.
  • Storage and Stability: Recommended storage is 2-8°C upon arrival. During stability studies, data showed that this product retains ≥90% of its activity when stored at 37°C for up to 8 weeks.
  • Legal Information: StableCell is a trademark of Sigma-Aldrich Co. LLC

SAFETY INFORMATION

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

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