{"product_id":"mouse-oncostatin-m-osm-protein-bhp13700355","title":"Mouse Oncostatin M (OSM) Protein","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eOSM\u003c\/strong\u003e is supplied as a recombinant protein reagent for \u003cstrong\u003eresearch use only\u003c\/strong\u003e. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e OSM; OS-M; Oncostatin M.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eSpecies origin:\u003c\/strong\u003e Mouse.\u003c\/p\u003e\u003cp\u003eMouse Oncostatin M (OSM) Protein, expressed in E. coli\u003c\/p\u003e\u003cp\u003eEndotoxin : \u0026lt; 1.0 EU per μg of the protein as determined by the LAL method\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eFunctionally, \u003cstrong\u003eOSM\u003c\/strong\u003e integrates upstream signaling cues into gene-expression programs. Regulation often depends on localization, partner interactions, and regulatory modifications that determine DNA binding and cofactor recruitment. This target is frequently investigated in research themes such as \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e.\u003c\/p\u003e\u003ch2\u003eMolecular characteristics\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eMolecular characteristics:\u003c\/strong\u003e Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.\u003c\/p\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource species:\u003c\/strong\u003e Mouse\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMolecular weight:\u003c\/strong\u003e 20.39 kDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The Recombinant Mouse Oncostatin M (OSM) Protein consists of 183 amino acids and predicts a molecular mass of 20.39KDa\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from Mouse Oncostatin M (OSM) Protein (P53347)(Ala24-Arg206)was expressed.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt; 99 % as determined by SDS-PAGE\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiological activity:\u003c\/strong\u003e Testing in progress\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003e\u003cstrong\u003ePost-translational considerations:\u003c\/strong\u003e E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required.\u003c\/p\u003e\u003ch2\u003eExpression and purification strategy\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eExpression system:\u003c\/strong\u003e E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eTagging:\u003c\/strong\u003e No tag tags are commonly used to streamline purification and enable capture\/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile 20 mM Tris with 150 mM NaCl, pH 7.4. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.\u003c\/p\u003e\u003ch2\u003eResearch interpretation\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eResearch interpretation:\u003c\/strong\u003e Recombinant protein reagents enable controlled experiments such as interaction reconstitution, quantitative calibration, and mechanistic perturbation with defined inputs. Interpretation is strengthened by pairing the primary readout with orthogonal markers that report on pathway state, localization, and complex assembly.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"5 ug","offer_id":52997769462125,"sku":"PRP1307-5UG","price":69.0,"currency_code":"USD","in_stock":true},{"title":"50 ug","offer_id":52997769494893,"sku":"PRP1307-50UG","price":189.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":52997769527661,"sku":"PRP1307-100UG","price":469.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":52997769560429,"sku":"PRP1307-1MG","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/PRP1307.png?v=1770191287","url":"https:\/\/www.ebiohippo.com\/products\/mouse-oncostatin-m-osm-protein-bhp13700355","provider":"BioHippo","version":"1.0","type":"link"}