Tryptophan Synthase beta Chain/Trp B protein (His tag)
-
- Target
- Tryptophan Synthase beta Chain/Trp B
- Protein Type
- Recombinant
- Origin
- E. coli
- Source
- Escherichia coli (E. coli)
- Purification tag / Conjugate
- His tag
- Purpose
- Recombinant E.coli Tryptophan Synthase β Chain/Trp B Protein (His Tag)
- Sequence
- Thr2-Ile397
- Characteristics
- Recombinant E.coli Tryptophan synthase beta chain is produced by our E.coli expression system and the target gene encoding Thr2-Ile397 is expressed with a 6His tag at the N-terminus.
- Purity
- > 95 % as determined by reducing SDS-PAGE.
- Endotoxin Level
- < 1.0 EU per μg as determined by the LAL method.
-
- Comment
-
40-50 kDa
- Restrictions
- For Research Use only
-
- Format
- Frozen, Liquid
- Buffer
- Supplied as a 0.2 μm filtered solution of PBS, pH 7.4.
- Storage
- -20 °C
- Storage Comment
- Store at < -20°C, stable for 6 months. Please minimize freeze-thaw cycles.
-
- Target
- Tryptophan Synthase beta Chain/Trp B
- Background
-
Background: Tryptophan synthase is an enzyme that catalyzes the final two steps in the biosynthesis of tryptophan. It is commonly found in Eubacteria, Archaebacteria, Protista, Fungi, and Plantae, but is absent from animals such as humans. Tryptophan synthase typically exists as an α-ββ-α complex.The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate: L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O.The beta subunits catalyze the irreversible condensation of indole and serine to form tryptophan in a pyridoxal phosphate (PLP) dependent reaction. Their assembly into a complex leads to structural changes in both subunits resulting in reciprocal activation.
Synonym: Tryptophan synthase beta chain, trpB
- Molecular Weight
- 43.8 kDa
- UniProt
- P0A879
-
