Rat Bactericidal Permeability-Increasing Protein (BPI) Protein

2574€ (1 mg)
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935106861
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name
Rat Bactericidal Permeability-Increasing Protein (BPI) Protein
category
Proteins and Peptides
provider
Abbexa
reference
abx065492
tested applications
WB, SDS-PAGE
Description
Recombinant Bactericidal/Permeability Increasing Protein (BPI) is a recombinant Rat protein produced in a Prokaryotic expression system (E. coli).
Documents del producto
Instrucciones
Data sheet
Product specifications
| Category | Proteins and Peptides |
| Immunogen Target | Bactericidal Permeability-Increasing Protein (BPI) |
| Host | E. coli |
| Origin | Rat |
| Conjugation | Unconjugated |
| Observed MW | Molecular Weight: Calculated MW: 16.4 kDa Concentration: Prior to lyophilization: 200 µg/ml Sequence Fragment: Asn320-Pro452 Tag: N-terminal His tag |
| Expression | Recombinant |
| Purity | > 95% |
| Size 1 | 1 mg |
| Size 2 | 5 mg |
| Form | Lyophilized To keep the original salt concentration, we recommend reconstituting to the original concentration prior to lyophilization (see Concentration) in ddH2O. If a lower concentration is required, dilute in PBS, pH 7.4. If a higher concentration is required, the product can be reconstituted directly in PBS, pH 7.4, though please note that this will change the overall salt concentration. The stock concentration should be between 0.1-1.0 mg/ml. Do not vortex. |
| Tested Applications | WB, SDS-PAGE |
| Buffer | Prior to lyophilization: PBS, pH 7.4, containing 0.01% Sarcosyl, 1 mM DTT, 5% Trehalose and Proclin-300. |
| Availability | Shipped within 1-2 months. |
| Storage | Store at 2-8 °C for up to one month. Store at -80 °C for up to one year. Avoid repeated freeze/thaw cycles. |
| Dry Ice | No |
| UniProt ID | Q6AXU0 |
| Background | Protein BPI |
| Status | RUO |
| Note | This product is for research use only. Not for human consumption, cosmetic, therapeutic or diagnostic use. |
Descripción
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BPI antibody
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-nagative bacterium P.aeruginosa, this activity is inhibited by LPS from P.aeruginosa.
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