Other Proteins

Recombinant Human BD-2

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Product Details

Catalogue Number: 300-49

Defensins (alpha and beta) are cationic peptides with a broad spectrum of antimicrobial activity that comprise an important arm of the innate immune system.  The α-defensins are distinguished from the β-defensins by the pairing of their three disulfide bonds.  To date, six human β-defensins have been identified; BD-1, BD-2, BD-3, BD-4, BD-5 and BD-6.  β-defensins are expressed on some leukocytes and at epithelial surfaces.  In addition to their direct antimicrobial activities, they can act as chemoattractants towards immature dendritic cells and memory T cells.  The β-defensin proteins are expressed as the C-terminal portion of precursors, and are released by proteolytic cleavage of a signal sequence and, in some cases, a propeptide sequence.  β-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds.  Recombinant Human BD-2 is a 4.3 kDa protein containing 41 amino acid residues.

Source: E.coli

Synonyms: DEFB2, DEFB4A, Beta-Defensin 2, Skin-antimicrobial peptide 1, SAP1


Purity: ≥ 98% by SDS-PAGE gel and HPLC analyses.

Biological Activity: Determined by its ability to chemoattract immature human dendritic cells using a concentration of 10.0-100.0 ng/ml.

Calculated Molecular Weight: 4.3 kDa

Accession Number: O15263

Gene ID: 1673

Country Of Origin: USA

Not for human use.

Research Interest


First Author
Schibli, D J
The solution structures of the human beta-defensins lead to a better understanding of the potent bactericidal activity of HBD3 against Staphylococcus aureus.
The Journal of Biological Chemistry; 277(10) pg8279-89
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First Author
Abou Alaiwa, M H
pH modulates the activity and synergism of the airway surface liquid antimicrobials β-defensin-3 and LL-37.
Proceedings of the National Academy of Sciences of the United States of America; 111(52) pg18703-8
PubMed Id
First Author
Hoover, D M
The structure of human beta-defensin-2 shows evidence of higher order oligomerization.
The Journal of Biological Chemistry; 275(42) pg32911-8
PubMed Id