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Key Documents

T4019

Sigma-Aldrich

Trypsin−Agarose

buffered aqueous suspension, from bovine pancreas trypsin

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About This Item

MDL number:
UNSPSC Code:
12352204
eCl@ss:
42020142
NACRES:
NA.54

biological source

bovine pancreas (trypsin)

Quality Level

form

buffered aqueous suspension

concentration

≥15 units/mL (packed gel)

extent of labeling

≥15 units per mL (packed gel)

matrix

beaded agarose

storage temp.

2-8°C

Related Categories

General description

The trypsin molecule has two domains: one is related to the enzyme active site and the tryptophan residues; the other is related to the 8-anilinonaphthalene-1-sulfonate binding.

Application

An experimental approach using SDS-PAGE, in-gel trypsin digestion and proteomic analysis identified five endosomal proteins. Trypsin cleavage of the high-risk HPV-16 E5 protein (16E5) generates a unique four-amino acid C-terminal peptide that serves as a marker for E5 expression in transfected cells and epithelial cell lines containing integrated and episomal HPV-16 DNA.

Unit Definition

One unit will hydrolyze 1.0 μmole of BAEE per min at pH 8.0 at 30 °C (titrimetric assay).

Physical form

Suspension in approx. 10 mM acetic acid, pH 3.2, containing preservative

Preparation Note

TPCK-treated

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Botulinum neurotoxin serotypes A and B (BoNT/A & B) are highly effective medicines to treat hyperactive cholinergic neurons. Due to neutralizing antibody formation, some patients may become non-responders. In these cases, the serotypes BoNT/C-G might become treatment alternatives. BoNT/D is
Ziad Sahab et al.
Journal of virology, 86(17), 9465-9473 (2012-06-29)
The high-risk human papillomavirus type 16 (HPV-16) E5 protein (16E5) induces tumors in a transgenic mouse model and may contribute to early stages of cervical carcinogenesis. Although high-risk E5 expression is generally thought to be lost during the progression to
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It is well known that the activation of mast cells due to the binding of mastoparan to the G(α) subunit of trimeric G proteins involves exocytosis regulation. However, experimental evidence in the literature indicates that mastoparan can also activate certain

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