B2188
Anti-BPI (61-75) antibody produced in rabbit
IgG fraction of antiserum, buffered aqueous solution
Synonym(s):
Anti-Bactericidal permeability-increasing protein precursor
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About This Item
UNSPSC Code:
12352203
NACRES:
NA.41
biological source
rabbit
conjugate
unconjugated
antibody form
IgG fraction of antiserum
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen ~54 kDa
species reactivity
human
technique(s)
western blot: 1:500-1:1,000
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... BPI(671)
General description
BPI (Bactericidal permeability-increasing protein) gene is mapped on to human chromosome 20q11.23. It belongs to the family of lipid-transfer proteins. BPI is mainly present in the granules of neutrophils and on the surface of neutrophils and monocytes.
Immunogen
synthetic peptide corresponding to amino acids 61-75 of human BPI
Application
Anti-BPI (61-75) antibody produced in rabbit has been used in immunoprecipitation.
Biochem/physiol Actions
BPI gene encodes a membrane associated bactericidal permeability increasing protein. BPI possesses high affinity for lipopolysaccharide. It has antimicrobial activity against gram-negative organisms and is essential constituent of the innate immune system for destroying the microbes as well as modulates subsequent adaptive immune responses. The amino-terminal of BPI is responsible for antimicrobial cytotoxicity and endotoxin-neutralization. The carboxyl-terminal is mainly for BPI-dependent transfer of Gram-negative bacteria and cell free endotoxin-rich particles to specific host cells. Mutation in BPI gene or a decrease of plasma BPI level may lead to chronic obstructive pulmonary disease (acute pneumonia and cystic fibrosis).
Target description
BPI (61-75), bactericidal/permeability-increasing protein, encodes a lipopolysaccharide binding protein. It is associated with human neutrophil granules and has bactericidal activity on gram-negative organisms.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Storage Class Code
10 - Combustible liquids
WGK
nwg
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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A myeloperoxidase-containing complex regulates neutrophil elastase release and actin dynamics during NETosis
Metzler KD, et al.
Testing, 8(3), 883-896 (2014)
Karen McQuillan et al.
Frontiers in pharmacology, 11, 1098-1098 (2020-08-09)
In people with cystic fibrosis (PWCF), inflammation with concurrent infection occurs from a young age and significantly influences lung disease progression. Studies indicate that neutrophils are important effector cells in the pathogenesis of CF and in the development of anti-neutrophil
Kathleen D Metzler et al.
Cell reports, 8(3), 883-896 (2014-07-30)
Neutrophils contain granules loaded with antimicrobial proteins and are regarded as impermeable organelles that deliver cargo via membrane fusion. However, during the formation of neutrophil extracellular traps (NETs), neutrophil elastase (NE) translocates from the granules to the nucleus via an
Hendrik Schultz et al.
Clinica chimica acta; international journal of clinical chemistry, 384(1-2), 12-23 (2007-08-07)
Gram-negative bacteria (GNB) and their endotoxin present a constant environmental challenge. Endotoxins can potently signal mobilization of host defenses against invading GNB but also potentially induce severe pathophysiology, necessitating controlled initiation and resolution of endotoxin-induced inflammation to maintain host integrity.
Alexander Holweg et al.
Biochemical Society transactions, 39(4), 1045-1050 (2011-07-27)
The human BPI (bactericidal/permeability-increasing protein), stored in primary azurophilic granula of neutrophil granulocytes and produced by mucosal epithelia, has been known for decades to bind LPS (lipopolysaccharide) with very high affinity and to efficiently kill Gram-negative bacteria. Thus BPI potentially
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