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B2188

Sigma-Aldrich

Anti-BPI (61-75) antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

Sinonimo/i:

Anti-Bactericidal permeability-increasing protein precursor

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About This Item

Codice UNSPSC:
12352203
NACRES:
NA.41

Origine biologica

rabbit

Livello qualitativo

Coniugato

unconjugated

Forma dell’anticorpo

IgG fraction of antiserum

Tipo di anticorpo

primary antibodies

Clone

polyclonal

Stato

buffered aqueous solution

PM

antigen ~54 kDa

Reattività contro le specie

human

tecniche

western blot: 1:500-1:1,000

N° accesso UniProt

Condizioni di spedizione

dry ice

Temperatura di conservazione

−20°C

modifica post-traduzionali bersaglio

unmodified

Informazioni sul gene

human ... BPI(671)

Descrizione generale

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.

Immunogeno

synthetic peptide corresponding to amino acids 61-75 of human BPI

Applicazioni

Anti-BPI (61-75) antibody produced in rabbit has been used in immunoprecipitation.

Azioni biochim/fisiol

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).

Descrizione del bersaglio

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.

Stato fisico

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Esclusione di responsabilità

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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Codice della classe di stoccaggio

10 - Combustible liquids

Classe di pericolosità dell'acqua (WGK)

nwg

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°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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