Skip to Content
Merck
CN

SRP6308

Alpha Defensins

≥95% (SDS-PAGE)

Synonym(s):

Defensin, HNP-4, Neutrophil defensin 4, alpha 4

Sign In to View Organizational & Contract Pricing.

Select a Size


About This Item

NACRES:
NA.32
UNSPSC Code:
12352202
Biological source:
human
Assay:
≥95% (SDS-PAGE)
Form:
frozen liquid
Mol wt:
<3.5 kDa
Technical Service
Need help? Our team of experienced scientists is here for you.
Let Us Assist
Technical Service
Need help? Our team of experienced scientists is here for you.
Let Us Assist

biological source

human

assay

≥95% (SDS-PAGE)

form

frozen liquid

mol wt

<3.5 kDa

packaging

pkg of 25 μg

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... HNP-4(1669)

General description

α defensins are a family of mammalian defensin peptides. In general, defensins are small cysteine-rich cationic proteins found in both vertebrates and invertebrates. These mixed α defensins are purified from human neutrophils. These peptides are active in killing bacteria, fungi, and enveloped viruses, and therefore, enable the neutrophils to inactivate and destroy potential pathogens. Defensins damage or kill ingested microbes by penetrating the microbial′ s cell membrane by way of electrical attraction, and consequently forming pores in the membrane. Human neutrophil-derived α-defensins (HNPs) are capable of enhancing phagocytosis by mouse macrophages. HNP1-3 have been reported to increase the production of tumor necrosis factor (TNF) and IL-1, while decreasing the production of IL-10 by monocytes. Increased levels of proinflammatory factors (e.g., IL-1, TNF, histamine and prostaglandin D2) and suppressed levels of IL-10 at the site of microbial infection are likely to amplify local inflammatory responses. This might be further reinforced by the capacity of some human and rabbit α-defensins to inhibit the production of immunosuppressive glucocorticoids by competing for the binding of adrenocorticotropic hormone to its receptor. Moreover, human α-defensins can enhance or suppress the activation of the classical pathway of complement in vitro by binding to solid-phase or fluid-phase complement C1q, respectively. The capacity of defensins to enhance phagocytosis, promote neutrophil recruitment, enhance the production of proinflammatory cytokines, suppress anti-inflammatory mediators and regulate complement activation argues that defensins upregulate innate host inflammatory defenses against microbial invasion.
HNP-4 (defensin alpha 4)/DEFA4 (neutrophil defensin 4) is a cationic, arginine-rich, non glycosylated peptide that has six cysteine residues. It is located in azurophilic granules of neutrophil granulocytes. HNP-4 has a molecular weight of 3.5-4.5 kDa. The gene that codes for α-defensins is mapped to human chromosome 8p23.

Biochem/physiol Actions

Expression of HNP-4 (defensin alpha 4)/DEFA4 (neutrophil defensin 4) helps to determine benign and malignant salivary gland tumors. It participates in the oxygen-independent killing of phagocytized microorganisms. HNP-4 is powerful against E. coli, S. faecalis and C. albicans.

Physical form

Frozen in 1 M acetic acid.

Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

Regulatory Information

新产品
This item has

Choose from one of the most recent versions:

Certificates of Analysis (COA)

Lot/Batch Number

Don't see the Right Version?

If you require a particular version, you can look up a specific certificate by the Lot or Batch number.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Purification and characterization of human neutrophil peptide 4, a novel member of the defensin family.
Wilde CG, et al.
The Journal of Biological Chemistry, 264(19), 11200-11203 (1989)
Human α-defensin (DEFA) gene expression helps to characterise benign and malignant salivary gland tumours.
Winter J, et al.
BMC Cancer, 12(1), 465-465 (2012)
Epithelial antimicrobial peptides in host defense against infection.
Bals R.
Respiratory Research, 1(3), 5-5 (2000)

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service