{"product_id":"recombinant-pbp2a-protein-c-his-bhp21400002","title":"Recombinant PBP2a Protein, C-His","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\n\n\u003cp\u003e\u003cstrong\u003eWhat is PBP2a?\u003c\/strong\u003e PBP2a (penicillin-binding protein 2a; often referred to as the \u003cstrong\u003eMecA\u003c\/strong\u003e protein) is a \u003cstrong\u003ebacterial cell-wall enzyme\u003c\/strong\u003e in \u003cem\u003eStaphylococcus aureus\u003c\/em\u003e that belongs to the \u003cstrong\u003epenicillin-binding protein (PBP) \/ DD-transpeptidase family\u003c\/strong\u003e. PBPs catalyze late-stage reactions in \u003cstrong\u003epeptidoglycan assembly\u003c\/strong\u003e, where peptide crosslinks are formed to strengthen the cell wall.\u003c\/p\u003e\n\n\u003cp\u003e\u003cstrong\u003eLocalization (research context):\u003c\/strong\u003e PBP2a is typically associated with the \u003cstrong\u003ecytoplasmic membrane\u003c\/strong\u003e in bacteria, positioning its catalytic region where peptidoglycan synthesis occurs. In many PBPs, an N-terminal membrane anchor helps localize the enzyme while the catalytic domains operate outside the cytosol on peptidoglycan precursors.\u003c\/p\u003e\n\n\u003cp\u003e\u003cstrong\u003eDomain \/ architecture (why fragments matter):\u003c\/strong\u003e High-molecular-weight PBPs, including PBP2a, are commonly described as having an N-terminal region important for membrane association and folding, and a \u003cstrong\u003eC-terminal transpeptidase domain\u003c\/strong\u003e that contains the catalytic machinery. In research discussions, this catalytic domain is the key unit for studying \u003cstrong\u003esubstrate recognition\u003c\/strong\u003e and \u003cstrong\u003eβ-lactam interaction\/inhibition logic\u003c\/strong\u003e.\u003c\/p\u003e\n\n\u003cp\u003e\u003cstrong\u003eWhat this recombinant protein represents:\u003c\/strong\u003e This product is a \u003cstrong\u003erecombinant PBP2a (MecA) protein fragment\u003c\/strong\u003e corresponding to \u003cstrong\u003eSer14–Glu657\u003c\/strong\u003e, expressed in \u003cstrong\u003eE. coli\u003c\/strong\u003e and supplied as a purified reagent with a \u003cstrong\u003eC-terminal His tag\u003c\/strong\u003e. Recombinant fragments are commonly used as \u003cstrong\u003edefined RUO inputs\u003c\/strong\u003e when researchers want a traceable, reproducible protein material for mechanistic studies, inhibitor-binding investigations, or assay system construction without relying on variable endogenous expression.\u003c\/p\u003e\n\n\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\n\n\u003cp\u003e\u003cstrong\u003eCore role in cell-wall biology:\u003c\/strong\u003e PBPs are central to \u003cstrong\u003epeptidoglycan crosslinking\u003c\/strong\u003e, a defining process in bacterial growth, morphology, and survival. PBP2a is frequently studied because it can function as a transpeptidase under conditions where other PBPs are compromised.\u003c\/p\u003e\n\n\u003cp\u003e\u003cstrong\u003eWhy PBP2a is a major research target:\u003c\/strong\u003e PBP2a is widely discussed in antimicrobial-resistance research because it is associated with \u003cstrong\u003ereduced susceptibility to many β-lactam antibiotics\u003c\/strong\u003e. This makes it a key experimental handle for studying how altered enzyme–inhibitor interactions can preserve peptidoglycan synthesis and maintain growth under β-lactam challenge.\u003c\/p\u003e\n\n\u003cp\u003e\u003cstrong\u003eResearch framing:\u003c\/strong\u003e In lab settings, PBP2a is used to support mechanistic questions such as how enzyme architecture influences inhibitor access, how substrate-mimetic probes engage the catalytic site, and how specific structural features contribute to “low-affinity” β-lactam behavior compared with more easily inhibited PBPs.\u003c\/p\u003e\n\n\u003ch2\u003eMolecular characteristics relevant to experimental design\u003c\/h2\u003e\n\n\u003cul\u003e\n  \u003cli\u003e\n\u003cstrong\u003eProtein class:\u003c\/strong\u003e Penicillin-binding protein \/ DD-transpeptidase (peptidoglycan crosslinking enzyme).\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eBiological source:\u003c\/strong\u003e Bacterial enzyme from \u003cem\u003eStaphylococcus aureus\u003c\/em\u003e (PBP2a family, MecA).\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003eFragment logic:\u003c\/strong\u003e Ser14–Glu657 represents a large portion of the protein commonly used to capture the catalytic behavior in a soluble recombinant format, while removing or minimizing dependence on full membrane context.\u003c\/li\u003e\n  \u003cli\u003e\n\u003cstrong\u003ePTM considerations:\u003c\/strong\u003e PBP2a is a bacterial protein and is not expected to require eukaryotic PTMs (e.g., glycosylation) for core catalytic identity. Expression in \u003cstrong\u003eE. coli\u003c\/strong\u003e is therefore a typical choice for producing a non-glycosylated recombinant form suitable for many biochemical research questions.\u003c\/li\u003e\n\u003c\/ul\u003e\n\n\u003cp\u003e\u003cstrong\u003eConformation and activity interpretation:\u003c\/strong\u003e For enzymes that are membrane-associated in vivo, recombinant soluble preparations are best interpreted as \u003cstrong\u003edefined molecular inputs\u003c\/strong\u003e for controlled experiments. Depending on the specific research question, full in-membrane behavior (local concentration, partner proteins, or spatial organization) may add layers of regulation that are intentionally simplified in recombinant formats.\u003c\/p\u003e\n\n\u003ch2\u003eExpression and purification context (quality transparency for RUO)\u003c\/h2\u003e\n\n\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli.\u003c\/p\u003e\n\n\u003cp\u003e\u003cstrong\u003eRegion expressed:\u003c\/strong\u003e Ser14–Glu657, with \u003cstrong\u003eC-His\u003c\/strong\u003e tag.\u003c\/p\u003e\n\n\u003cp\u003e\u003cstrong\u003ePurification:\u003c\/strong\u003e Affinity chromatography; reported purity \u0026gt;90% (per your product data).\u003c\/p\u003e\n\n\u003cp\u003e\u003cstrong\u003eFormat and formulation:\u003c\/strong\u003e Supplied as a lyophilized preparation. Stabilizing excipients and buffered formats are commonly used to maintain solubility and functional integrity for recombinant enzymes during storage and transport. (Operational storage\/shipping instructions should remain in your dedicated fields, not here.)\u003c\/p\u003e\n\n\u003ch2\u003eHow to think about PBP2a reagents in research\u003c\/h2\u003e\n\n\u003cp\u003ePBP2a is often investigated as a \u003cstrong\u003emechanistic model enzyme\u003c\/strong\u003e linking cell-wall biochemistry to β-lactam interaction logic. A recombinant PBP2a fragment provides a \u003cstrong\u003etraceable reference material\u003c\/strong\u003e for comparing binding behaviors across probes or inhibitors, benchmarking reagent performance, and supporting reproducible assay systems where endogenous expression varies by strain, growth condition, or genetic background.\u003c\/p\u003e\n\n\u003cp\u003eBecause PBP2a sits at the intersection of \u003cstrong\u003epeptidoglycan synthesis\u003c\/strong\u003e and \u003cstrong\u003eantibiotic-resistance biology\u003c\/strong\u003e, well-defined recombinant preparations help researchers cleanly separate questions about \u003cstrong\u003eenzyme-intrinsic properties\u003c\/strong\u003e (binding, active-site accessibility, structural control) from broader cellular variables (transport, cell-wall architecture, stress responses, and pathway redundancy).\u003c\/p\u003e","brand":"Biohippo Inc","offers":[{"title":"100 ug","offer_id":53000605499757,"sku":"JN117012-100UG","price":311.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53000605532525,"sku":"JN117012-1MG","price":1627.0,"currency_code":"USD","in_stock":true}],"url":"https:\/\/www.ebiohippo.com\/products\/recombinant-pbp2a-protein-c-his-bhp21400002","provider":"BioHippo","version":"1.0","type":"link"}