B2188
Anti-BPI (61-75) antibody produced in rabbit
IgG fraction of antiserum, buffered aqueous solution
Sinônimo(s):
Anti-Bactericidal permeability-increasing protein precursor
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About This Item
Código UNSPSC:
12352203
NACRES:
NA.41
fonte biológica
rabbit
Nível de qualidade
conjugado
unconjugated
forma do anticorpo
IgG fraction of antiserum
tipo de produto de anticorpo
primary antibodies
clone
polyclonal
Formulário
buffered aqueous solution
peso molecular
antigen ~54 kDa
reatividade de espécies
human
técnica(s)
western blot: 1:500-1:1,000
nº de adesão UniProt
Condições de expedição
dry ice
temperatura de armazenamento
−20°C
modificação pós-traducional do alvo
unmodified
Informações sobre genes
human ... BPI(671)
Descrição geral
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.
Imunogênio
synthetic peptide corresponding to amino acids 61-75 of human BPI
Aplicação
Anti-BPI (61-75) antibody produced in rabbit has been used in immunoprecipitation.
Ações bioquímicas/fisiológicas
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).
Descrição-alvo
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.
forma física
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Exoneração de responsabilidade
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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Código de classe de armazenamento
10 - Combustible liquids
Classe de risco de água (WGK)
nwg
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°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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