Recombinant human alpha Defensin 1 protein (ab54409)

Overview

Description

  • NatureRecombinant
  • SourceEscherichia coli
  • Amino Acid Sequence
    • SpeciesHuman

Specifications

Our Abpromise guarantee covers the use of ab54409 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications

    SDS-PAGE

    Functional Studies

  • Purity> 95 % SDS-PAGE.

  • FormLyophilised
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. The lyophilized protein is stable for a few weeks at room temperature. Store at -20°C long term.

    Preservative: None
    Buffer: None
    Endotoxin level: < 0.1 ng per ug of alpha defensin 1.

    This product is an active protein and may elicit a biological response in vivo, handle with caution.

  • ReconstitutionThis protein should be reconstituted in water to a concentration of 0.1-1.0 mg/ml. This solution can be diluted into other buffer solutions. The reconstituted protein should be stored in working aliquots at -20°C.

General Info

  • Alternative names
    • alpha 1
    • DEF1
    • DEF1_HUMAN
    • DEFA1
    • DEFA1B
    • DEFA2
    • Defensin
    • Defensin 1
    • Defensin, alpha 1
    • Defensin, alpha 1, myeloid related sequence
    • Defensin, alpha 2
    • HNP-1
    • HNP-2
    • HNP1
    • HP-1
    • HP-2
    • HP1
    • HP2
    • MRS
    • Myeloid related sequence
    • Neutrophil defensin 1
    • Neutrophil defensin 2
    see all
  • FunctionDefensin 1 and defensin 2 have antibacterial, fungicide and antiviral activities. Has antimicrobial activity against Gram-negative and Gram-positive bacteria. Defensins are thought to kill microbes by permeabilizing their plasma membrane.
  • Sequence similaritiesBelongs to the alpha-defensin family.
  • Cellular localizationSecreted.
  • Information by UniProt

References for Recombinant human alpha Defensin 1 protein (ab54409)

ab54409 has not yet been referenced specifically in any publications.

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