Native Soybean Trypsin Inhibitor protein (Agarose) (ab94845)
Key features and details
- Expression system: Native
- Purity: > 95% SDS-PAGE
- Suitable for: SDS-PAGE, Functional Studies
Description
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Product name
Native Soybean Trypsin Inhibitor protein (Agarose) -
Purity
> 95 % SDS-PAGE.
ab94845 is immobilized on an agarose resin via coupling to primary amines to create an affinity resin with specificity for a number of serine proteases. -
Expression system
Native -
Accession
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Protein length
Full length protein -
Animal free
No -
Nature
Native -
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Species
Soybean
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Conjugation
Agarose
Associated products
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Related Products
Specifications
Our Abpromise guarantee covers the use of ab94845 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Applications
SDS-PAGE
Functional Studies
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Form
Liquid -
Additional notes
Provided as 20 ml of 1:1 slurryab94845 binds free trypsin tighter with increasing pH from 4.5-8.0 that allows for a simple gradient to low pH (~2.5-3.0) for elution. Binding capacity: 1 ml resin binds > 2 mg Trypsin Inhibitor protein -
Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped at 4°C. Store at +4°C.
pH: 7.40
Preservative: 0.02% Sodium azide
Constituents: 1.58% Tris HCl, 0.87% Sodium chloride
General Info
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Alternative names
- CRISP8
- KTi
- KTi3
see all -
Relevance
The soybean trypsin inhibitor was first crystallized by Kunitz in 1945 and is one of several such inhibitors found in soybeans. It inhibits the proteolytic action approximately of an equal weight of crystalline trypsin by combining with trypsin to form a stable compound. Chymotrypsin is only slightly inhibited by soy inhibitor.
Protocols
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
Datasheets and documents
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SDS download
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Datasheet download
References (0)
ab94845 has not yet been referenced specifically in any publications.