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BirA Protein, E. coli, Recombinant (His & MBP)

Catalog No. TMPY-03650
Synonyms: BirA, dhbB, bioR

The enzyme BirA is a key reagent because of its ability to biotinylate proteins at a specific residue in a recognition sequence. This enzyme is used to biotinylate the C termini of membrane proteins, allowing these proteins to be tetramerized by binding to streptavidin. Because of the specificity of the biotinylation at the C terminus, the orientation of the membrane proteins on the streptavidin is equivalent to that of the native protein on the cell surface. These tetrameric proteins can be used to study protein receptor-ligand interactions at the cell surface, and site-specific biotinylation can be used to study proteins in vitro using a defined orientation. The biotinylation of histones by BirA ligase is consistent with the proposed role of human HCS in chromatin. The N-terminal BirA domain is required for both transcriptional regulation of biotin synthesis and biotin protein ligase activity.

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BirA Protein, E. coli, Recombinant (His & MBP)
Pack Size Availability Price/USD Quantity
100 μg In stock $ 386.00
200 μg 5 days $ 660.00
500 μg 5 days $ 1,340.00
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Biological Description
Technical Params
Product Properties
Biological Information Testing in progress
Description The enzyme BirA is a key reagent because of its ability to biotinylate proteins at a specific residue in a recognition sequence. This enzyme is used to biotinylate the C termini of membrane proteins, allowing these proteins to be tetramerized by binding to streptavidin. Because of the specificity of the biotinylation at the C terminus, the orientation of the membrane proteins on the streptavidin is equivalent to that of the native protein on the cell surface. These tetrameric proteins can be used to study protein receptor-ligand interactions at the cell surface, and site-specific biotinylation can be used to study proteins in vitro using a defined orientation. The biotinylation of histones by BirA ligase is consistent with the proposed role of human HCS in chromatin. The N-terminal BirA domain is required for both transcriptional regulation of biotin synthesis and biotin protein ligase activity.
Species E. coli
Expression System E. coli
Tag His,MBP
Accession Number P06709
Synonyms BirA, dhbB, bioR
Construction A DNA sequence encoding the E.coil BirA (P06709) (Met1–Lys321) was fused with an N-terminal polyhistidine-tagged MBP tag at the N-terminus.
Protein Purity > 95 % as determined by SDS-PAGE

Molecular Weight Approxiamtely 36.9 kDa
Endotoxin Please contact us for more information.
Formulation Lyophilized from sterile 50mM Tris, 100mM NaCl, 10% Glycerol, pH 8.0. Please contact us for any concerns or special requirements. Normally 5 % - 8 % trehalose, mannitol and 0. 01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA.
Reconstitution A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information.
Stability & Storage

Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Shipping

In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.

Research Background The enzyme BirA is a key reagent because of its ability to biotinylate proteins at a specific residue in a recognition sequence. This enzyme is used to biotinylate the C termini of membrane proteins, allowing these proteins to be tetramerized by binding to streptavidin. Because of the specificity of the biotinylation at the C terminus, the orientation of the membrane proteins on the streptavidin is equivalent to that of the native protein on the cell surface. These tetrameric proteins can be used to study protein receptor-ligand interactions at the cell surface, and site-specific biotinylation can be used to study proteins in vitro using a defined orientation. The biotinylation of histones by BirA ligase is consistent with the proposed role of human HCS in chromatin. The N-terminal BirA domain is required for both transcriptional regulation of biotin synthesis and biotin protein ligase activity.

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Keywords

BirA Protein, E. coli, Recombinant (His & MBP) BirA dhbB bioR recombinant recombinant-proteins proteins protein

 

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