GoldBio growth factors are manufactured for RESEARCH USE ONLY and cannot be sold for human consumption!
RecombinantHumanDefensin,Beta 104ADefensin,Beta 4, DEFB4, HBD4
Human beta-defensin 104A (DEFB104A) is an antimicrobial peptide that contributes to both the innate and the adaptive immune systems and is active against gram-negative and gram-positive bacteria, fungi, and viruses. Like the other β-defensins, DEFB104A is a small protein that contains a motif consisting of six cysteine residues which form three intramolecular disulfide bridges. It is expressed at highest levels in the testis and stomach, and at lower levels in the uterus, neutrophils, thyroid, lung, and kidney. Expression of DEFB104A is upregulated by phorbol 12-myristate 13-acetate (PMA), as well as in response to infection with gram-positive and gram-negative bacteria. DEFB104A is a cationic peptide and interacts with the membranes of invading microbes, which are negatively charged due to the presence of lipopolysaccharides (LPS) or lipoteichoic acid (LTA). LTA and LPS have higher affinity for DEFB103A than for Ca+2 and Mg+2 ions. The larger defensin molecule displaces the smaller ion, changing the membrane structure and affecting the stability of the membrane; this can lead to the formation of pores and subsequent depolarization or lysis. DEFB104A has been shown to be more active against Pseudomonas aeruginosa than DEFB1, DEFB4A, or DEFB103A. Inhibition of DEFB104A by high salt concentration may play a role in the pathogenesis of cystic fibrosis.
Sterile Filtered White lyophilized powder. Purified and tested for use in cell culture.
Source: Escherichia coli
MW: ~6.0 kDa (50 aminoacids)
Purity: >98% by SDS-PAGEand HPLC analyses.
Biological Activity: Fully biologically active when compared to standard. The biological activity determined by a chemotaxis bioassay using human monocytes is in a concentration range of 0.1-100.0 ng/ml.
Storage/Handling: Store desiccated at-20°C.
HGNC: 18115
NOT FOR HUMAN USE!
Additional resources for this protein may be found at:UniProt
