B6804
Monoclonal Anti-Bacterial Alkaline Phosphatase (BAP, PhoA) antibody produced in mouse
clone BAP-77, ascites fluid
Synonym(s):
Monoclonal Anti-Phosphatase, Alkaline, bacterial
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About This Item
Conjugate:
alkaline phosphatase conjugate
Clone:
BAP-77, monoclonal
Application:
ELISA (i), WB
Citations:
3
To inquire about this product B6804, please contact your local Merck office or dealer. Contact Technical Service
biological source
mouse
conjugate
alkaline phosphatase conjugate
antibody form
ascites fluid
antibody product type
primary antibodies
clone
BAP-77, monoclonal
mol wt
antigen ~50 kDa
species reactivity
bacteria
technique(s)
indirect ELISA: suitable, western blot: 1:20,000 using purified Escherichia coli BAP
isotype
IgG1
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
General description
Bacterial alkaline phosphatase (BAP) is a periplasmic enzyme that is encoded by the phoA gene. The use of a BAP tag to the target gene yields a stable fusion product that does not affect the bioactivity and biodistribution of the target gene in recombinant expression vector systems. Hence, anti-BAP antibodies can be useful tools for the detection and analysis of target biomolecules fused to BAP tags.Monoclonal Anti-Bacterial Alkaline Phosphatase (BAP, PhoA) (mouse IgG1 isotype) is derived from the BAP-77 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from a BALB/c mouse immunized with a BAP tagged fusion protein. Bacterial alkaline phosphatase (BAP) also known as PhoA, EC 3.1.3.1 is an 50 kDa protein, derived from E. coli.
Immunogen
A bacterial alkaline phosphatase (BAP) tagged fusion protein.
Application
Monoclonal Anti-Bacterial Alkaline Phosphatase (BAP, PhoA) antibody is suitable for use in western blot (at 1:20,000 dilutions using purified Escherichia coli BAP) and indirect ELISA.
Biochem/physiol Actions
Bacterial alkaline phosphatase (BAP) enzyme regulates the catabolism of phosphate esters. Alkaline phosphatase appears to require export to the periplasm to show enzymatic activity. Fusions of the secreted alkaline phosphatase to an integral cytoplasmic membrane protein of E. coli shows different activities depending on where with the membrane protein the alkaline phosphatase is fused. Fusions to positions in or near the periplasmic (extracellular) domain lead to high alkaline phosphatase activity, whereas those to positions in the cytoplasmic domain give low activity.
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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This Item | |||
|---|---|---|---|
| conjugate alkaline phosphatase conjugate | conjugate unconjugated | conjugate agarose conjugate | conjugate unconjugated |
| species reactivity bacteria | species reactivity human | species reactivity human | species reactivity bacteria |
| clone BAP-77, monoclonal | clone PAP-12, monoclonal | clone 8B6, monoclonal | clone GAL-13, monoclonal |
| antibody form ascites fluid | antibody form ascites fluid | antibody form purified immunoglobulin | antibody form ascites fluid |
| biological source mouse | biological source mouse | biological source mouse | biological source mouse |
| mol wt antigen ~50 kDa | mol wt - | mol wt - | mol wt - |
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Storage Class
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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Enhancing the detection of Toxoplasma gondii via an anti-SAG1 scFv-alkaline phosphatase immunoconjugate
<BIG>Hannachi E, et al.</BIG>
Biotechnology reports (Amsterdam, Netherlands), 2019, e00360-e00360 null
Design and characterization of a recombinant colorimetric SAG1-alkaline phosphatase conjugate to detect specific antibody responses against Toxoplasma gondii
<BIG>Bel-Ochi, N C, et al</BIG>
Journal of Immunological Methods, 394, 107-114 (2013)
D K Agrawal et al.
Journal of bacteriology, 172(6), 3180-3190 (1990-06-01)
The phoA503 mutant was identified as a mutant that shows a novel phoA regulatory phenotype. The phoA503 allele dramatically reduces the synthesis of bacterial alkaline phosphatase activity during Pi starvation in an otherwise wild-type host and during the logarithmic growth
Global Trade Item Number
| SKU | GTIN |
|---|---|
| B6804-.2ML | 04061837856341 |
| B6804-100UL | 04061837856358 |