B2188
Anti-BPI (61-75) antibody produced in rabbit
IgG fraction of antiserum, buffered aqueous solution
Synonyme(s) :
Anti-Bactericidal permeability-increasing protein precursor
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About This Item
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41
Source biologique
rabbit
Niveau de qualité
Conjugué
unconjugated
Forme d'anticorps
IgG fraction of antiserum
Type de produit anticorps
primary antibodies
Clone
polyclonal
Forme
buffered aqueous solution
Poids mol.
antigen ~54 kDa
Espèces réactives
human
Technique(s)
western blot: 1:500-1:1,000
Numéro d'accès UniProt
Conditions d'expédition
dry ice
Température de stockage
−20°C
Modification post-traductionnelle de la cible
unmodified
Informations sur le gène
human ... BPI(671)
Description générale
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.
Immunogène
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.
Actions biochimiques/physiologiques
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).
Description de la cible
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.
Forme physique
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Clause de non-responsabilité
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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Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
nwg
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
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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)
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.
P W Gray et al.
The Journal of biological chemistry, 264(16), 9505-9509 (1989-06-05)
The bactericidal permeability increasing protein (BPI) is a 50-60-kDa membrane-associated protein isolated from granules of polymorphonuclear leukocytes. A full-length cDNA clone encoding human BPI has been isolated and the derived amino acid sequence reveals a structure that is consistent with
Chiung-Zuei Chen et al.
COPD, 9(2), 197-202 (2012-03-14)
Bactericidal/permeability-increasing protein (BPI) is a member of the pattern recognition receptors of the innate immune system. Recently, an association between genetic polymorphism in the BPI gene and a risk of airflow decline after transplantation was demonstrated, but whether these findings
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