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인용 및 참조 문헌 (40)
Invitrogen™
BOCILLIN™ FL Penicillin, Sodium Salt
Penicillin-binding proteins, present on the cytoplasmic membranes of eubacteria, can be detected with BOCILLIN FL penicillin and BOCILLIN 650/665 penicillin.Dissolve자세히 알아보기
| 카탈로그 번호 | 수량 |
|---|---|
| B13233 | 1 mg |
카탈로그 번호 B13233
제품 가격(KRW)
521,000
온라인 행사
Ends: 31-Mar-2026
612,000할인액 91,000 (15%)
Each
수량:
1 mg
제품 가격(KRW)
521,000
온라인 행사
Ends: 31-Mar-2026
612,000할인액 91,000 (15%)
Each
Penicillin-binding proteins, present on the cytoplasmic membranes of eubacteria, can be detected with BOCILLIN FL penicillin and BOCILLIN 650/665 penicillin.
Dissolve in high-quality anhydrous DMSO or water for a stock concentration of 1 to 10 mM.
For Research Use Only. Not for use in diagnostic procedures.
사양
여기/방출504/511 nm
라벨 유형Other Label(s) or Dye(s)
분자식C30H31BF2N5NaO6S
분자량661.46
제품라인BOCILLIN
수량1 mg
권장 스토리지Store in freezer (-5°C to -30°C) and protect from light.
배송 조건Room Temperature
물리적 형태Solid
제품 유형Antibiotic
Unit SizeEach
인용 및 참조 문헌 (40)
인용 및 참조 문헌
Abstract
In vitro activities of piperacillin against beta-lactamase-negative ampicillin-resistant Haemophilus influenzae.
Journal:Antimicrob Agents Chemother
PubMed ID:15047524
'The in vitro activities of piperacillin (PIP) against beta-lactamase-negative ampicillin (AMP)-resistant (BLNAR) Haemophilus influenzae were compared with those of cefotaxime (CTX) and ceftriaxone (CRO), and the potency of PIP as therapy for meningitis caused by BLNAR is also discussed. PIP showed good activity (MIC at which 90% of strains are
Characterization of HMW-PBPs from the rod-shaped actinomycete Corynebacterium glutamicum: peptidoglycan synthesis in cells lacking actin-like cytoskeletal structures.
Journal:Mol Microbiol
PubMed ID:17877698
'Analysis of the complete genome sequence of Corynebacterium glutamicum indicated that, in addition to ftsI, there are eight proteins with sequence motifs that are strongly conserved in penicillin binding proteins (PBPs): four genes that code for high-molecular-weight (HMW)-PBPs (PBP1a, PBP1b, PBP2a and PBP2b), two genes encoding low-molecular-weight PBPs (PBP4 and
Penicillin-binding protein 2a of Streptococcus pneumoniae: expression in Escherichia coli and purification and refolding of inclusion bodies into a soluble and enzymatically active enzyme.
Journal:Protein Expr Purif
PubMed ID:10419829
'Penicillin-binding proteins (PBPs), targets of beta-lactam antibiotics, are membrane-bound enzymes essential for the biosynthesis of the bacterial cell wall. PBPs possess transpeptidase and transglycosylase activities responsible for the final steps of the bacterial cell wall cross-linking and polymerization, respectively. To facilitate our structural studies of PBPs, we constructed a 5''-truncated
The basis for resistance to beta-lactam antibiotics by penicillin-binding protein 2a of methicillin-resistant Staphylococcus aureus.
Journal:J Biol Chem
PubMed ID:15226303
'Penicillin-binding protein 2a (PBP2a) of Staphylococcus aureus is refractory to inhibition by available beta-lactam antibiotics, resulting in resistance to these antibiotics. The strains of S. aureus that have acquired the mecA gene for PBP2a are designated as methicillin-resistant S. aureus (MRSA). The mecA gene was cloned and expressed in Escherichia
The cysteine-rich protein A from Helicobacter pylori is a beta-lactamase.
Journal:J Biol Chem
PubMed ID:10748053
'Among the large number of hypothetical proteins within the genomes of Helicobacter pylori, there is a family of unique and highly disulfide-bridged proteins, designated family 12, for which no function could originally be assigned. Sequence analysis revealed that members of this family possess a modular architecture of alpha/beta-units and a