Human Recombinant BPI protein, His Tag (V2LY-0526-LY2384)

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Basic Information

Expressed Host
HEK293 Cells
Protein Species
Human
Tag
His Tag
Protein Construction
This product is Human Recombinant BPI protein, His Tag consist of Amino Acid: 1-487 and predicts a molecular mass of 52.1 kDa.
Molecule Mass
52.1 kDa
Verified
HPLC
Sequence
Amino Acid: 1-487
Species
Human

Formulations & Storage [For reference only, actual COA shall prevail!]

Purity
≥85% as determined by SDS-PAGE. ≥95% as determined by SEC-HPLC.
Endotoxin
Please contact us for more information.
Format
Lyophilized
Reconstitution
Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.
Buffer
Lyophilized from sterile Please contact us for any concerns or special requirements.

Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA.
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
More Infomation

Target

Full Name
Bactericidal/Permeability-Increasing Protein
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. Has antibacterial activity against the Gram-negative bacterium P.aeruginosa, this activity is inhibited by LPS from P.aeruginosa.
Biological Process
Antibacterial humoral response Source: UniProtKB
Antimicrobial humoral immune response mediated by antimicrobial peptide Source: UniProtKB
Antimicrobial humoral response Source: Reactome
Cellular response to lipopolysaccharide Source: UniProtKB
Defense response to Gram-negative bacterium Source: UniProtKB
Innate immune response Source: GO_Central
Lipopolysaccharide-mediated signaling pathway Source: GO_Central
Negative regulation of interleukin-6 production Source: BHF-UCL
Negative regulation of interleukin-8 production Source: BHF-UCL
Negative regulation of macrophage activation Source: BHF-UCL
Negative regulation of tumor necrosis factor production Source: BHF-UCL
Neutrophil degranulation Source: Reactome
Cellular Location
Secreted; Cytoplasmic granule membrane. Membrane-associated in polymorphonuclear Leukocytes (PMN) granules.

Theprungsirikul, J., Skopelja-Gardner, S., Burns, A. S., Wierzbicki, R. M., & Rigby, W. F. (2021). Bactericidal/Permeability-Increasing Protein Preeminently Mediates Clearance of Pseudomonas aeruginosa In Vivo via CD18-Dependent Phagocytosis. Frontiers in immunology, 12, 1407.

Theprungsirikul, J., Skopelja-Gardner, S., Wierzbicki, R. M., Sessions, K. J., & Rigby, W. F. (2021). Differential Enhancement of Neutrophil Phagocytosis by Anti–Bactericidal/Permeability-Increasing Protein Antibodies. The Journal of Immunology, 207(3), 777-783.

Liu, Y., Zha, H., Han, X., Yu, S., Chai, Y., Zhong, J., & Zhu, Q. (2021). Molecular characterization and functional analysis of the bactericidal permeability-increasing protein/LPS-binding protein (BPI/LBP) from roughskin sculpin (Trachidermus fasciatus). Developmental & Comparative Immunology, 123, 104133.

Kong, Q., Lv, Z., Kang, Y., An, Y., Liu, Z., & Zhang, J. (2021). Bactericidal Permeability Increasing Protein Deficiency Aggravates Acute Colitis in Mice by Increasing the Serum Levels of Lipopolysaccharide. Frontiers in Immunology, 11, 3543.

Theprungsirikul, J., Thaden, J. T., Wierzbicki, R. M., Burns, A. S., Skopelja-Gardner, S., Fowler Jr, V. G., ... & Rigby, W. F. C. (2020). Low-avidity autoantibodies against bactericidal/permeability-increasing protein occur in gram-negative and gram-positive bacteremia. Infection and immunity, 88(10), e00444-20.

McQuillan, K., Gargoum, F., Murphy, M. P., McElvaney, O. J., McElvaney, N. G., & Reeves, E. P. (2020). Targeting IgG Autoantibodies for Improved Cytotoxicity of Bactericidal Permeability Increasing Protein in Cystic Fibrosis. Frontiers in Pharmacology, 11, 1098.

Yang, D., Han, Y., Chen, L., Cao, R., Wang, Q., Dong, Z., ... & Zhao, J. (2019). A bactericidal permeability-increasing protein (BPI) from manila clam Ruditapes philippinarum: Investigation on the antibacterial activities and antibacterial action mode. Fish & shellfish immunology, 93, 841-850.

Skopelja-Gardner, S., Theprungsirikul, J., Meagher, R. E., Beliveau, C. M., Bradley, K. E., Avery, M., ... & Rigby, W. F. (2019). Autoimmunity to bactericidal/permeability-increasing protein in bronchiectasis exhibits a requirement for Pseudomonas aeruginosa IgG response. European Respiratory Journal, 53(2).

Bülow, S., Zeller, L., Werner, M., Toelge, M., Holzinger, J., Entzian, C., ... & Gessner, A. (2018). Bactericidal/permeability-increasing protein is an enhancer of bacterial lipoprotein recognition. Frontiers in immunology, 9, 2768.

Balakrishnan, A., & Chakravortty, D. (2017). Epithelial cell damage activates bactericidal/permeability increasing-protein (BPI) expression in intestinal epithelium. Frontiers in microbiology, 8, 1567.

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For research use only. Not intended for any clinical use.

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