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B6804

Sigma-Aldrich

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

MDL number:
MFCD02095875
UNSPSC Code:
12352203
NACRES:
NA.46

biological source

mouse

Quality Level

200

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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Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

B6804-BULK:
B6804-VAR:
B6804-.2ML:
B6804-100UL:

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Certificates of Analysis (COA)

Lot/Batch Number
027M4756
091M4771
010K4830

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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)
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
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

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