Product Name
BACTERICIDAL PERMEABILITY INCREASING PROTEIN (BPI), Monoclonal Antibody
Full Product Name
BACTERICIDAL PERMEABILITY INCREASING PROTEIN (BPI, CAP57)
Product Synonym Names
Anti -BACTERICIDAL PERMEABILITY INCREASING PROTEIN (BPI, CAP57)
Product Gene Name
anti-BPI antibody
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Research Use Only
For Research Use Only. Not for use in diagnostic procedures.
Chromosome Location
Chromosome: 13; NC_007311.4 (67778730..67805090)
3D Structure
ModBase 3D Structure for P17453
Specificity
Recognizes full length human natural and recombinant Bactericidal Permeability Increasing protein (BPI). 3F9 recognizes only free BPI and does not interact with BPI that has formed a complex with LPS.
Purity/Purification
Affinity Purified
Purified by Protein G affinity chromatography.
Form/Format
Supplied as a liquid in PBS, 0.1% BSA, 0.02% sodium azide.
Preparation and Storage
-20 degree C
Other Notes
Small volumes of anti-BPI antibody vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.
Related Product Information for
anti-BPI antibody
The antimicrobial protein BPI is a 55kD protein found in the primary (azurophilic) granules of human neutrophils and has also been detected on surface of neutrophils, small intestinal and oral epithelial cells. BPI is a bactericidal compound that is present in polymorphonuclear cells (PMN) and in lower levels in the specific granules of eosinophils. BPI possesses high affinity toward the lipid A region of lipopolysaccharides (LPS) that comprise the outer leaflet of the gram-negative bacterial outer membrane. Binding of BPI to the lipid A moiety of LPS exerts multiple anti-infective activities against gram-negative bacteria: 1) cytotoxicity via sequential damage to bacterial outer and inner lipid membranes, 2) neutralization of gram-negative bacterial LPS, 3) opsonization of bacteria to enhance phagocytosis by neutrophils. Airway epithelial cells constitutively express the BPI gene and produce the BPI protein and, therefore, BPI may be a critical determinant in the development of LPS-triggered airways disease. Inflammation induced by LPS possibly contributes to the development of rapid airflow decline, a serious and often fatal complication of hematopoietic cell transplantation. Furthermore, a 21kD bioactive recombinant fragment of BPI, rBPI21, was shown to confer a survival advantage
Product Categories/Family for anti-BPI antibody
Antibodies; Abs to Proteins
Application Notes for anti-BPI antibody
Suitable for use in immunoassays both as coating and as detector.
NCBI/Uniprot data below describe general gene information for BPI. It may not necessarily be applicable to this product.
NCBI Accession #
NP_776320.1
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NCBI GenBank Nucleotide #
NM_173895.2
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UniProt Primary Accession #
P17453
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UniProt Secondary Accession #
Q3T0P4[Other Products]
UniProt Related Accession #
P17453[Other Products]
Molecular Weight
53,442 Da[Similar Products]
NCBI Official Full Name
bactericidal permeability-increasing protein
NCBI Official Symbol
BPI??[Similar Products]
NCBI Protein Information
bactericidal permeability-increasing protein
UniProt Protein Name
Bactericidal permeability-increasing protein
Protein Family
Bactericidal permeability-increasing protein
UniProt Gene Name
BPI??[Similar Products]
UniProt Entry Name
BPI_BOVIN
UniProt Comments for BPI
Function: The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope.
Subunit structure: Monomer. Homodimer; disulfide-linked
Subcellular location: Secreted
By similarity. Cytoplasmic granule membrane
By similarity. Note: Membrane-associated in polymorphonuclear Leukocytes (PMN) granules
Tissue specificity: Restricted to cells of the myeloid series.
Domain: The N-terminal region may be exposed to the interior of the granule, whereas the C-terminal portion may be embedded in the membrane. During phagocytosis and degranulation, proteases may be released and activated and cleave BPI at the junction of the N- and C-terminal portions of the molecule, providing controlled release of the N-terminal antibacterial fragment when bacteria are ingested
Sequence similarities: Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.
Research Articles on BPI
1. Polymorphism in BPI has no effect on daughter yield deviation for somatic cell score in Holstein cattle.
Precautions
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Disclaimer
While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.
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