{"product_id":"recombinant-helicobacter-pylori-hp-1019-periplasmic-serine-endoprotease-degp-like-protein-c-his-bhp21406329","title":"Recombinant Helicobacter pylori HP_1019\/Periplasmic serine endoprotease DegP-like Protein, C-His","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTarget identity:\u003c\/strong\u003e\u003cstrong\u003eHELICOBACTER\u003c\/strong\u003e is a enzyme. It is typically cytosolic, nuclear, or organelle-localized (depends on isoform).\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eHELICOBACTER\u003c\/strong\u003e is provided as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. Recombinant proteins are commonly used as defined molecular inputs in biochemical and cell-free systems, enabling controlled interrogation of binding, activity, and pathway-relevant interactions.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eProtein identity context:\u003c\/strong\u003e HELICOBACTER (expression region Ser2-Lys443; approx. molecular weight 49.10 kDa).\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eHELICOBACTER\u003c\/strong\u003e supports biochemical transformations that can be read out as changes in substrate\/product balance or signaling intermediates. Recombinant enzymes enable controlled reconstitution experiments and mechanistic interrogation with defined inputs. This target is frequently explored in \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e research contexts.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003eKey molecular attributes can influence binding behavior, stability, and assay background—especially for multimeric, disulfide-rich, or PTM-dependent targets.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Ser2-Lys443\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 49.10 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;90%\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eForm:\u003c\/strong\u003e Lyophilized\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1 mM EDTA, 4% Trehalose, 1% Mannitol.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e Prokaryotic expression typically yields a non-glycosylated recombinant form. This is often appropriate for many intracellular proteins and binding studies, while disulfide-rich or PTM-dependent extracellular targets may behave differently when native PTMs are required. For enzymes, cofactor binding state and oligomerization can also shape apparent activity in reconstituted assays.\u003c\/p\u003e\u003ch2\u003eStructural and biochemical features\u003c\/h2\u003e\u003cp\u003eEnzyme behavior can be influenced by oligomerization, cofactor state, and local microenvironment, which may change apparent kinetics in simplified assay formats.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression host selection can influence folding and PTM state, which may affect activity or binding in different assay formats.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003ePurification:\u003c\/strong\u003e Affinity-chromatography. Purification approach and formulation influence sample homogeneity and background signal in downstream biochemical measurements.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eEndotoxin consideration:\u003c\/strong\u003e Reported endotoxin level is Please contact with the lab for this information.; this parameter can matter when recombinant proteins are used in cell-based systems sensitive to innate immune activation.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eReconstitution:\u003c\/strong\u003e Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details..\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Enzymatic readouts can reflect both abundance and catalytic state. Orthogonal measurements (substrate levels, product formation, and pathway markers) help clarify whether changes arise from expression, inhibition, or cofactor availability.\u003c\/p\u003e","brand":"Biohippo Inc","offers":[{"title":"100 ug","offer_id":53001204662637,"sku":"JN944012-100UG","price":311.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53001204695405,"sku":"JN944012-1MG","price":1627.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/JN944012-SDSPAGE-1.jpg?v=1770275287","url":"https:\/\/www.ebiohippo.com\/products\/recombinant-helicobacter-pylori-hp-1019-periplasmic-serine-endoprotease-degp-like-protein-c-his-bhp21406329","provider":"BioHippo","version":"1.0","type":"link"}