Luciferase Antibody - BSA Free

Dot Blot: Luciferase Antibody [NBP2-44165] - Dot Blot results of Rabbit anti-Luciferase Antibody. Dots are Luciferase (Photobacterium fischerii) at (1) 100ng, (2) 33.3ng, (3) 11.1ng, (4) 3.70ng, (5) 1.23ng. Primary Antibody: Rabbit anti-Luciferase. Secondary Antibody: Goat Anti-Rabbit IgG HRP.

• Reactivity: Ba
• Applications: WB, DB, ELISA, IHC, IP
• Clonality: Polyclonal
• Host: Rabbit
• Conjugate: Unconjugated
• Format: BSA Free

Luciferase Antibody - BSA Free Summary

• Description: This product was prepared from monospecific antiserum by a delipidation and defibrination. Assay by immunoelectrophoresis resulted in a single precipitin arc against anti-rabbit serum, purified and partially purified Luciferase [Photobacterium fischerii]
  
  Store vial at 4C prior to restoration. For extended storage aliquot contents and freeze at -20C or below. Avoid cycles of freezing and thawing. Centrifuge product if not completely clear after standing at room temperature. This product is stable for several weeks at 4C as an undiluted liquid. Dilute only prior to immediate use.
• Immunogen: Luciferase [Photobacterium fischerii] (Uniprot: P19907)
• Isotype: Serum
• Clonality: Polyclonal
• Host: Rabbit
• Purity: Delipidation and Defibrination

Applications/Dilutions

• Dilutions:
  • Dot Blot
  • ELISA 1:5000-1:25000
  • Immunohistochemistry 1:500-1:2500
  • Immunoprecipitation 1:100
  • Western Blot 1:1000-1:5000
• Application Notes: This product has been tested by dot blot and is suitable for western blotting, immunohistochemistry, immunoprecipitation, and ELISA. Researchers should determine optimal titers for applications that are not stated below.

Reactivity Notes

Aliivibrio fischeri (Vibrio) Photobacterium

Cross reactivity against Luciferase from other tissues and species may occur but have not been specifically determined

Packaging, Storage & Formulations

• Storage: Store at -20C. Avoid freeze-thaw cycles.
• Buffer: 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2
• Preservative: 0.01% Sodium Azide
• Purity: Delipidation and Defibrination

Alternate Names for Luciferase Antibody - BSA Free

• Alkanal monooxygenase alpha chain
• Alkanal monooxygenase beta chain
• Bacterial luciferase alpha chain
• Bacterial luciferase beta chain
• ec 1.13.12.7
• firefly luciferase
• Fluc
• LuC
• Luciferase
• luciferin 4 monooxygenase
• Luciferin 4-monooxygenase
• luxA
• luxB

Background

Luciferase is a generic term for a group of oxidative enzymes used in bioluminescence. Firefly (Photinus pyralis) and bacterial luciferase enzymes are commonly used in assay systems such as cell viability assays, reporter gene assays, and for in vivo imaging. Bacterial luciferases are flavoenzymes composed of two subunits each encoded by the luxA and luxB genes, while the firefly luciferase is a single polypeptide specified by the luc gene (1). Firefly luciferase (theoretical molecular weight: 61 kDa) oxidizes the substrate luciferin to oxyluciferin in a bioluminescent reaction requiring Mg2+ and ATP (2,3). This reaction produces a flash of yellow-green light with an emission peak around 560nm that can be detected by a luminometer (3). Firefly luciferase has become one of the more widely used reporter proteins and is an excellent tool for the study of gene expression, given that the amount of light emitted is directly proportional to luciferase activity (4).

The luciferase assay is fast and sensitive, differentiating itself from the CAT (chloramphenicol acetyltransferase) assay because it does not require a radioactive substrate.

References

1. Eun, H. (1996). Marker/Reporter enzymes. Enzymology Primer for Recombinant DNA Technology, 567-645. doi:10.1016/b978-012243740-3/50011-9

2. McNabb, D. S., Reed, R., & Marciniak, R. A. (2005). Dual luciferase assay system for rapid assessment of gene expression in Saccharomyces cerevisiae. Eukaryotic Cell, 4(9), 1539-1549. doi:10.1128/ec.4.9.1539-1549.2005

3. Fraga, H. (2008). Firefly luminescence: A historical perspective and recent developments. Photochemical & Photobiological Sciences, 7(2), 146-158. doi:10.1039/b719181b

4. Younes, A., Lukyanenko, Y. O., Lyashkov, A. E., Lakatta, E. G., & Sollott, S. J. (2011). A bioluminescence method for direct measurement of phosphodiesterase activity. Analytical Biochemistry, 417(1), 36-40. doi:10.1016/j.ab.2011.05.036

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

Bioinformatics

• Uniprot:
  • P19907(Bacteria)