T6567
Porcine pancreas
BioReagent
1 mM HCl: soluble 1 mg/mL, clear, colorless
wet ice
2-8°C
Danger
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Respiratory system
11 - Combustible Solids
WGK 1
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
Documents related to the products that you have purchased in the past have been gathered in the Document Library for your convenience.
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Product numbers are combined with Pack Sizes/Quantity when displayed on the website (example: T1503-25G). Please make sure you enter ONLY the product number in the Product Number field (example: T1503).
Example:
Additional examples:
705578-5MG-PW
PL860-CGA/SHF-1EA
MMYOMAG-74K-13
1000309185
enter as 1.000309185)
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How to Find a Lot/Batch Number for COA
Lot and Batch Numbers can be found on a product's label following the words 'Lot' or 'Batch'.
For a lot number such as TO09019TO, enter it as 09019TO (without the first two letters 'TO').
For a lot number with a filling-code such as 05427ES-021, enter it as 05427ES (without the filling-code '-021').
For a lot number with a filling-code such as STBB0728K9, enter it as STBB0728 without the filling-code 'K9'.
In some cases, a COA may not be available online. If your search was unable to find the COA you can request one.
If available for a given product, the recommended re-test date or the expiration date can be found on the Certificate of Analysis.
The lot specific COA document can be found by entering the lot number above under the "Documents" section.
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This product is soluble in 1mM HCL.
Each vial content 20 ug of the product.
The product has been treated with TPCK to remove chymotryptic activity, further purified through affinity chromatography, and lyophilized, resulting in convenient use and highly specific cleavage. This information is on the product page under application.
If you are looking for trypsin sequence information, you have to go to the NCBI Protein Data Bank.
As per Sigma R and D the information is as follows: In order to efficiently digest a protein with trypsin, it must be denatured and the disulfide bonds modified by reduction and alkylation, or at least reduced. Many intact proteins are highly resistant to digestion with trypsin. If you do not want to reduce and alkylate, you can then just boil the protein with 5 mM DTT or 20 mM 2ME for 10 minutes, and then quickly cool on ice to denature the protein. This may result in a precipitate, but the trypsin will still digest the protein and it will clear within an hour or two. You can also dissolve the protein in 6 M guanidine-HCl or 8 M urea. Reduce and alkylate using the PROT-RA kit or other suitable method. Then they would have to dilute the solution to less than 2 M of either denaturant and then add the trypsin. This is the method that we use routinely in the lab.
Ask a Scientist here.
Evaluation of Recombinant, Chemically Treated Trypsin in Proteomics and Protein Characterization Assays
See how pretreatment with a mucin-selective protease, Mucinase StcE, for tryptic-digest sample preparation of mucins may increase the number of glycopeptides and glycoforms identified from your samples.
The field of proteomics is continually looking for new ways to investigate protein dynamics within complex biological samples. Recently, many researchers have begun to use RNA interference (RNAi) as a method of manipulating protein levels within their samples, but the ability to accurately determine these protein amounts remains a challenge. Fortunately, over the past decade, the field of proteomics has witnessed significant advances in the area of mass spectrometry. These advances, both in instrumentation and methodology, are providing researchers with sensitive assays for both identification and quantification of proteins within complex samples. This discussion will highlight some of these methodologies, namely the use of Multiple Reaction Monitoring (MRM) and Protein-AQUA.
This procedure is for products with a specification for Trypsin activity using Na-Benzoyl-L-arginine ethyl ester (BAEE) as a substrate. The procedure is a continuous spectrophotometric rate determination (A253, Light path = 1 cm).
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