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Safety Information

T0637

Sigma-Aldrich

Trypsin inhibitor

saline suspension

Synonym(s):

Trypsin Inhibitor Agarose

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About This Item

MDL number:
MFCD00165901
UNSPSC Code:
41106500
NACRES:
NA.56

Product Name

Trypsin inhibitor–Agarose, saline suspension, protein from Glycine max (soybean)

biological source

protein from Glycine max (soybean)

form

saline suspension

matrix

cross-linked 4% beaded agarose

matrix activation

cyanogen bromide

matrix attachment

amino

matrix spacer

1 atom

capacity

≥1 mg/mL binding capacity (trypsin)(with activity of 10,000 BAEE units per mg)

storage temp.

2-8°C

Application

Trypsin inhibitor-Agarose has been used in affinity chromatography for the purification:

  • of shrimp chymotrypsin
  • of protease from Trichoderma reesei
  • of Ras-interacting protein 1(Rasip 1)
Trypsin inhibitor-agarose is used in protein chromatography, affinity chromatography, and specialty resins.

Physical form

Suspension in 0.5 M NaCl containing preservative

Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

ISHL Indicated Name

Substances Subject to be Indicated Names

ISHL Notified Names

Substances Subject to be Notified Names

JAN Code

T0637-BULK:
T0637-VAR:
T0637-1ML:4548173212289
T0637-5ML:4548173212302
T0637-10ML:4548173212272
T0637-25ML:4548173212296

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Certificates of Analysis (COA)

Lot/Batch Number
SLCJ9939
SLCG2836
SLCF1898
SLCD1899
SLBZ2745

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Fabiana Cornejo Maciel et al.
Journal of molecular endocrinology, 34(3), 655-666 (2005-06-16)
We have described that, in adrenal and Leydig cells, the hormonal regulation of free arachidonic acid (AA) concentration is mediated by the concerted action of two enzymes: an acyl-CoA thioesterase (MTE-I or ARTISt) and an acyl-CoA synthetase (ACS4). In this
Y J Chuang et al.
The Journal of biological chemistry, 276(18), 14961-14971 (2001-03-30)
Heparin activates the primary serpin inhibitor of blood clotting proteinases, antithrombin, both by an allosteric conformational change mechanism that specifically enhances factor Xa inactivation and by a ternary complex bridging mechanism that promotes the inactivation of thrombin and other target
L J Marnett et al.
The Journal of biological chemistry, 263(32), 16532-16535 (1988-11-15)
Treatment of prostaglandin (PG)H synthase purified from ram seminal vesicle microsomes with trypsin cleaves the 70-kDa subunits into 33- and 38-kDa fragments (Chen, Y.-N. P., Bienkowski, M. J., and Marnett, L. J. (1987) J. Biol. Chem. 262, 16892-16899). In contrast
Liu-Ying Luo et al.
Clinical cancer research : an official journal of the American Association for Cancer Research, 12(3 Pt 1), 742-750 (2006-02-10)
Preliminary data suggest that hK11 is a novel serum biomarker for prostate and ovarian cancer. To examine the enzymatic characteristics of hK11, we purified and functionally characterized native hK11 from seminal plasma. hK11 was purified from seminal plasma by immunoaffinity
S Lawler et al.
Current biology : CB, 8(25), 1387-1390 (1999-01-16)
Mitogen-activated protein kinases (MAPKs) mediate many of the cellular effects of growth factors, cytokines and stress stimuli. Their activation requires the phosphorylation of a threonine and a tyrosine residue located in a Thr-X-Tyr motif (where X is any amino acid)
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