Anti-Pbp2B

Anti-Pbp2B, Cat. No. ABS2199, is a rabbit polyclonal antibody that detects Penicillin-binding protein 2B (Pbp2B) and has been tested for use in Immunofluorescence and Western Blotting.

Immunofluorescence Western Blotting

Western Blotting Analysis: A 1:10,000 dilution from a representative lot detected Pbp2B in WT Bacillus Subtilis and GFP-Pbp2B (Courtesy of Dr. Richard Daniel at Newcastle University, UK).

Western Blotting Analysis: A 1:10,000 dilution from a representative lot detected His-PbpB recombinant protein (Courtesy of Dr. Richard Daniel at Newcastle University, UK).

Immunofluorescence Analysis: A representative lot detected Pbp2B in Immunofluorescence applications (Daniel, R.A., et. al. (2000). Mol Microbiol. 35(2):299-311).

Western Blotting Analysis: A representative lot detected Pbp2B in Western Blotting applications (Bisson-Filho, A.W., et. al. (2017). Science. 355(6326):739-743; Adams, D.W., et. al. (2016). Mol Microbiol. 99(6):1028-42).

This rabbit polyclonal antibody specifically detects Penicillin-binding protein 2B (Pbp2B) in Bacillus subtilis.

His-tagged full-length recombinant Penicillin-binding protein 2B from Bacillus subtilis, strain 168CA.

Stable for 1 year at -20°C from date of receipt. Handling Recommendations: Upon receipt and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.

Rabbit polyclonal antiserum with 0.05% sodium azide.

Evaluated by Western Blotting with His-PbpB recombinant protein.

Western Blotting Analysis: A 1:10,000 dilution of this antibody detected His-PbpB recombinant protein.

Penicillin-binding protein 2B (UniProt: Q07868; also known as PBP-2B, Penicillin-binding protein B) is encoded by the PbpB gene (Gene ID: 939847) in Bacillus subtilis. Analysis of the Bacillus subtilis genome shows 16 PBP-encoding genes that are identified based on their sequence similarities and include four class A, six class B, and six low-molecular-weight PBP-encoding genes. PBPs contain a conserved C-terminal penicillin-binding domain that possesses d,d-carboxypeptidase or endopeptidase activity in low-molecular-weight PBPs and transpeptidase activity in most high-molecular-weight PBPs. PBPs are the main targets of beta-lactam antibiotics. PBP-2B is a single-pass membrane protein that is a member of the transpeptidase family. It is involved in the synthesis of septal peptidoglycan and functions with FtsW that facilitates the transport of cytosolically synthesized Lipid II into the existing cell wall. It is synthesized throughout vegetative growth and its synthesis is enhanced during stage II of sporulation, but it is undetectable in the mature spore. PBP-2B is shown to be essential for vegetative cell division and sporulation septation. PBP-2B consists of a cytoplasmic domain (aa 1-13), a transmembrane domain (aa 14-31), and an extracellular domain (aa 32-312). PBP-2B also has two penicillin-binding protein and serine/threonine kinase-associated (PASTA) domains (aa 598-657 and 658-714) PASTA:), which are believed to bind beta-lactam antibiotics and are involved in peptidoglycan metabolism. (Ref.: Daniel, RA., et al. (2000). Mol. Microbiol. 35(2); 299-311; Ogawara, H. (2016). J. Antibiotics. 69; 660 685; Wei, Y., et al. (2003). J. Bacteriol. 185(16); 4717 4726).

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.