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Merck

B2188

Sigma-Aldrich

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

IgG fraction of antiserum, buffered aqueous solution

Sinónimos:

Anti-Bactericidal permeability-increasing protein precursor

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

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

10 - Combustible liquids

wgk_germany

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (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)
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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