Mouse Anti-Ampicillin Recombinant Antibody (clone aL2) (CAT#: PABW-008)

Recombinant Mouse Antibody (aL2) is capable of binding to Ampicillin. This antiody binds to intact ampicillin and shows no detectable cross-reactivity with hydrolyzed ampicillin.


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Figure 1 Phage-ELISA analysis of aL2, aL4, Al5 and aL6 on transferrin-ampicillin-coated plates.

Figure 1 Phage-ELISA analysis of aL2, aL4, Al5 and aL6 on transferrin-ampicillin-coated plates.

The signals correspond to 1011 phage particles (in 100 ml). Black bars re¯ect speci®c binding. Competitive inhibition was studied by pre-incubation with 1 mM ampicillin (grey bars) and 1 mM 6-APA (white bars).

Burmester, J., Spinelli, S., Pugliese, L., Krebber, A., Honegger, A., Jung, S., ... & PluÈckthun, A. (2001). Selection, characterization and x-ray structure of anti-ampicillin single-chain Fv fragments from phage-displayed murine antibody libraries. Journal of molecular biology, 309(3), 671-685.

Figure 2 Recombinant AL2 and L2 Proteins Inhibit ADK Activity in Vitro.

Figure 2 Recombinant AL2 and L2 Proteins Inhibit ADK Activity in Vitro.

(A) Autoradiograph of a chromatogram showing AMP generated in ADK reactions preincubated with the indicated proteins before ATP addition, as described in the text.
(B) ADK activity is reduced proportionally by preincubation with increasing amounts of AL2. Reactions contained 10 ng of ADK and varying amounts of His-AL2.
(C) Stoichiometry of inhibition. The graph shows relative ADK activity plotted against increasing His-AL2:ADK ratio. ADK activity (AMP/AMP+ATP) in each reaction was calculated after phosphorimager quantitation of radioactivity in individual spots.

Wang, H., Hao, L., Shung, C. Y., Sunter, G., & Bisaro, D. M. (2003). Adenosine kinase is inactivated by geminivirus AL2 and L2 proteins. The Plant Cell, 15(12), 3020-3032.

Figure 3 AL2 Is in the Nucleus and the Cytoplasm of TGMV-Infected Cells.

Figure 3 AL2 Is in the Nucleus and the Cytoplasm of TGMV-Infected Cells.

Epidermal cells from TGMV-infected plants (top three rows) and mock-inoculated plants (bottom row) were examined under bright-field illumination using differential interference contrast optics. Nuclei were located by DAPI staining (blue; left column), and AL2 protein was detected using AL2 primary antiserum followed by FITC-conjugated secondary antiserum (green; middle column). DAPI + FITC merge images are shown in the right column. The irregular cells shown in the top row were originally positioned over mesophyll, whereas the elongated cells shown in the lower rows were associated with veins.

Wang, H., Hao, L., Shung, C. Y., Sunter, G., & Bisaro, D. M. (2003). Adenosine kinase is inactivated by geminivirus AL2 and L2 proteins. The Plant Cell, 15(12), 3020-3032.

Figure 4 ADK Levels Are Reduced in Transgenic Plants Expressing AL2 and L2 and Also during Geminivirus Infection.

Figure 4 ADK Levels Are Reduced in Transgenic Plants Expressing AL2 and L2 and Also during Geminivirus Infection.

(A) ADK activity is reduced in transgenic N. benthamiana plants expressing AL21-100 and L2. Crude extracts obtained from comparable stem samples from just below the shoot apex were analyzed for ADK activity as described in the text using equal amounts of protein extract from each sample (150 to 400 ng in different experiments). Labeled AMP produced was quantitated using a phosphorimager. The observed differences between nontransgenic and transgenic plants were statistically significant, as determined by Student's t test (P < 0.05). Graph values represent means ± se.
(B) ADK activity is reduced in TGMV- and BCTV-infected plants. Comparable stem samples from just below the shoot apex were obtained from mock-inoculated N. benthamiana plants and plants infected with wild-type BCTV, a BCTV L2 mutant, TGMV, PVX, or CMV and analyzed as described above and in the text. In all cases, the observed differences between virus-infected and control plants proved statistically significant, as determined by Student's t test (P < 0.05). Graph values represent means ± se.

Wang, H., Hao, L., Shung, C. Y., Sunter, G., & Bisaro, D. M. (2003). Adenosine kinase is inactivated by geminivirus AL2 and L2 proteins. The Plant Cell, 15(12), 3020-3032.


Specifications

  • Immunogen
  • Ampicillin
  • Host Species
  • Mouse
  • Derivation
  • Mouse
  • Type
  • Mouse IgG
  • Specificity
  • Tested positive against synthetic Ampicillin
  • Clone
  • aL2
  • Applications
  • ELISA, Block

Product Property

  • Purity
  • >95% as determined by analysis by SDS-PAGE
  • Concentration
  • Please refer to the vial label for the specific concentration.
  • Buffer
  • PBS
  • Preservative
  • No preservatives
  • Storage
  • Centrifuge briefly prior to opening vial. Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

  • Alternative Names
  • Ampicillin; (2S,5R,6R)-6-([(2R)-2-amino-2-phenylacetyl]amino)-3,3-dimethyl-7-oxo-4-thia-1-azabicyclo[3.2.0]heptane-2-carboxylic acid; Principen; amcap; amcill; aminobenzylpenicillintrihydrate; amperil; ampichel

Product Notes

This is a product of Creative Biolabs' Hi-Affi™ recombinant antibody portfolio, which has several benefits including:

• Increased sensitivity
• Confirmed specificity
• High repeatability
• Excellent batch-to-batch consistency
• Sustainable supply
• Animal-free production

See more details about Hi-Affi™ recombinant antibody benefits.

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Recombinant Antibody

CAT Product Name Application Type
MOB-61 Recombinant Anti-Ampicillin Antibody WB, Neut, FuncS IgG
MHH-61 Recombinant Human Anti-Ampicillin Antibody WB, Dot, FuncS IgG

Human Antibody

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For research use only. Not intended for any clinical use. No products from Creative Biolabs may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative Biolabs.

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