Horseradish Peroxidase (HRP) C1A

£200.00£1,500.00

Clear
SKU: N/A Category:

Description

Product name: Horseradish Peroxidase (HRP) C1A

Product description: Recombinant Armoracia rusticana (Horseradish) Peroxidase C1A produced in Nicotiana benthamiana by Agrobacterium-mediated transient expression.

Description

Host species: Nicotiana benthamiana

Molecular weight: 35.5 kDa + Glycosylation

Tag: N-terminal His-tag

Uses: For in vitro research use only. Not for human in vivo or therapeutic use.

Relevance: Horseradish Peroxidase C1A is a heme-binding glycoprotein which catalyses the following reaction: ROOR’ + electron donor (2 e−) + 2H+ → ROH + R’OH1. It has a variety of roles in nature; including the removal of H2O2, oxidation of toxic reductants, and response to environmental stresses such as wounding and pathogen attack2. HRP is frequently used for a variety of biochemical applications due to its ability to be readily conjugated to a variety of molecules and to produce coloured3, fluorimetric4, or luminescent signals when in the presence of the relevant substrate.

Specification

Purity: 98 % as shown by SDS-PAGE

Figure 1: reducing 4-20% SDS-PAGE analysis of 5 µg HRP.

Biological activity: Active.

Endotoxin: Not tested.

Storage

Formulation: Lyophilized from 25 mM Tris pH8, 50 mM NaCl.

Shipping: Recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.

Stability & Storage: See COA for detailed storage instructions. Lyophilized materials are stable for up to twelve months from date of receipt at -70℃.

It is recommended that reconstituted protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Reconstitution: A hardcopy of COA with reconstitution instructions is included with the product.

References

  1. Veitch NC. Horseradish peroxidase: a modern view of a classic enzyme. Phytochemistry. Feb;65(3):249-59. Review. (2004).
  2. https://www.uniprot.org/uniprot/P00433
  3. Conyers SM, Kidwell DA. Chromogenic substrates for horseradish peroxidase. Anal Biochem. 192(1):207-11. (1991).
  4. Acharya AP, Nafisi PM, Gardner A, MacKay JL, Kundu K, Kumar S, Murthy N. A fluorescent peroxidase probe increases the sensitivity of commercial ELISAs by two orders of magnitude. Chem Commun. 49 (88): 10379–10381. (2013).