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anti-BPI antibody :: Mouse anti-Human BACTERICIDAL PERMEABILITY INCREASING PROTEIN Monoclonal Antibody

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Catalog # MBS604935
Unit / Price
  0.1 mg  /  $780 +1 FREE 8GB USB
anti-BPI antibody
Product Name

BACTERICIDAL PERMEABILITY INCREASING PROTEIN (BPI), Monoclonal Antibody

Also Known As

BACTERICIDAL PERMEABILITY INCREASING PROTEIN (BPI, CAP57)

Product Synonym Names
Anti -BACTERICIDAL PERMEABILITY INCREASING PROTEIN (BPI, CAP57)
Product Gene Name
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
Clonality
Monoclonal
Isotype
IgG1
Clone Number
9G128
Host
Mouse
Species Reactivity
Human
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.
Immunogen
Human BPI.
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
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 GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Primary Accession #
UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
53,442 Da[Similar Products]
NCBI Official Full Name
bactericidal permeability-increasing protein
NCBI Official Symbol
NCBI Protein Information
bactericidal permeability-increasing protein
UniProt Protein Name
Bactericidal permeability-increasing protein
UniProt Gene Name
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.
Precautions
All of MyBioSource's Products are for scientific laboratory research purposes and are not for diagnostic, therapeutics, prophylactic or in vivo use. Through your purchase, you expressly represent and warrant to MyBioSource that you will properly test and use any Products purchased from MyBioSource in accordance with industry standards. MyBioSource and its authorized distributors reserve the right to refuse to process any order where we reasonably believe that the intended use will fall outside of our acceptable guidelines.
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.

It is the responsibility of the customer to report product performance issues to MyBioSource within 30 days of receipt of the product. Please visit our Terms & Conditions page for more information.
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