Mouse anti TrpE Tag

Nordic MuBio
Product Code: EXA-X1556M
Product Group: Primary Antibodies
Supplier: Nordic MuBio
CodeSizePrice
EXA-X1556M100 ug£316.00
Quantity:
Prices exclude any Taxes / VAT

Overview

Host Type: Mouse
Antibody Isotype: IgG
Antibody Clonality: Monoclonal
Antibody Clone: 17
Regulatory Status: RUO
Target Species: Species Independent
Application: Western Blot (WB)
Shipping:
Ship at ambient temperature freeze upon arrival
Storage:
Product should be stored at -20°C. Aliquot to avoid freeze/thaw cycles

Further Information

Applications Description:
Antibody can be used for Western blotting of TrpE conjugated proteins (1-5 ?g/ml). Optimal concentration should be evaluated by serial dilutions.
Background:
Specific for 37 kDaTrpE protein. TrpE is a commonly used tag in some protein expression systems. This antibody can be used for analysis of expression of proteins alone or in conjunction with protein specific antibodies. Can also be used as a negative control antibody as it does not react with any known mammalian protein.
Caution:
This product is intended FOR RESEARCH USE ONLY, and FOR TESTS IN VITRO, not for use in diagnostic or therapeutic procedures involving humans or animals.
Concentration:
See vial for concentration
Field of Interest:
Molecular Biology
Formulation:
Provided as solution in phosphate buffered saline with 0.08% sodium azide
Functional Analysis:
Western Blotting
Immunogen:
Hybridoma produced by the fusion of splenocytes from mice immunized with full length recombinant TrpE protein and mouse myeloma cells.
Positive Control:
Not Available
Product Form:
Unconjugated
Product Stability:
Products are stable for one year from purchase when stored properly
Purification Method:
Protein A/G Chromatography

References

1. Chen, P., et al. 'Use of TrpE fusion protein to identify antigenic domains within the BIV envelope protein.' J. Virol. Methods 1994: 47, 331-343

2. Mercy, M.R., et al. 'A new series of trpE vectors that enable high expression of nonfusion proteins in bacteria.' Protein Expr. Purif. 1992: 3, 57-64