{"product_id":"ulp1-sumo-protease-ulp1-peptidase-bhp13700001","title":"Ulp1 (SUMO Protease \/Ulp1 peptidase)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eUlp1\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 Ulp1 peptidase; SUMO Protease.\u003c\/p\u003e\u003cp\u003eRecombinant Yeast Ulp1 protein expressed in E.coli.\u003c\/p\u003e\u003cp\u003eSUMO (Small Ubiquitin-like MOdifiers) Protease 1 (Ulp1, Ubl-specific protease 1 from Saccharomyces cerevisiae) is a highly active cysteine protease. It is highly specific as it recognizes the tertiary structure of the ubiquitin-like (UBL) protein, SUMO (Smt3), rather than its amino acid sequence. SUMO fusion tag, as an N-terminal fusion partner, has been shown to enhance functional protein production in prokaryotic and eukaryotic expression systems with significantly improved protein stability and solubility.\u003c\/p\u003e\u003ch2\u003eBiological significance and function\u003c\/h2\u003e\u003cp\u003eFunctionally, \u003cstrong\u003eUlp1\u003c\/strong\u003e is connected to ubiquitin\/SUMO-dependent regulation of protein stability, localization, and signaling duration. These modification pathways act as reversible molecular switches that help tune pathway outputs during stress, cell-cycle control, and quality-control processes. This target is frequently investigated in research themes such as \u003cstrong\u003eMetabolism \u0026amp; Enzymology\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\u003eMolecular weight:\u003c\/strong\u003e 28.7 KD\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eProtein length:\u003c\/strong\u003e The recombinant yeast ULP1 consists of 219 amino acids and has a predicted molecular mass of 28.7 KD. The apparent molecular mass of the ULP1 is approximately 28 KD in SDS-PAGE under reducing conditions due to glycosylation.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression region:\u003c\/strong\u003e Amino acid sequence derived from ULP1 isoform (Q02724) (403-621 aa + N-terminal Poly-6*His tag C-terminal Poly-6*His tag) was expressed.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePurity:\u003c\/strong\u003e \u0026gt;95% as determined by SDS-PAGE.\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. For ubiquitin\/SUMO pathway enzymes, catalytic activity often depends on correct folding and active-site integrity rather than glycosylation.\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 Many recombinant proteins incorporate affinity tags (e.g., His, GST, Fc) to aid purification and capture in binding assays. Where relevant, tag status can be considered when comparing activity or interaction data.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eFormulation:\u003c\/strong\u003e Lyophilized from sterile 20 mM Tris , 500 mM NaCl pH8.0.. 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 Ubiquitin\/SUMO pathway measurements can reflect changes in protein turnover, signaling dwell time, and stress-adaptation programs. Mechanistic interpretation is often strengthened by pairing modification-state readouts with measurements of substrate abundance, localization, and interaction partners.\u003c\/p\u003e","brand":"Abbkine Scientific Co., Ltd.","offers":[{"title":"500 U","offer_id":52997734433133,"sku":"PRP3001-500U","price":69.0,"currency_code":"USD","in_stock":true},{"title":"1000 U","offer_id":52997734465901,"sku":"PRP3001-1000U","price":129.0,"currency_code":"USD","in_stock":true},{"title":"5000 U","offer_id":52997734498669,"sku":"PRP3001-5000U","price":499.0,"currency_code":"USD","in_stock":true}],"url":"https:\/\/www.ebiohippo.com\/products\/ulp1-sumo-protease-ulp1-peptidase-bhp13700001","provider":"BioHippo","version":"1.0","type":"link"}