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429700 Leptin, Human, Recombinant, E. coli

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429700
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概要

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429700-1MGCN
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      Description
      OverviewRecombinant, human leptin expressed in E. coli. Native leptin is a product of the obese (ob) gene that serves as a ligand for the OB receptor (OB-R). Mice with mutations of the ob gene have been found to be obese and diabetic and to have reduced activity, metabolism, and body temperature. Reported to reduce hepatic glucose production by blocking phosphoenolpyruvate synthesis. Note: Following complete dissolution in 15 mM HCl, add 7.5 mM sterile NaOH and bring the pH to approximately 5.2.
      Catalogue Number429700
      Brand Family Calbiochem®
      SynonymsrhOB
      References
      ReferencesAnderwald, C., et al. 2002. Mol. Endocrinol. 16, 1612.
      Ookuma, M., et al. 1998. Diabetes 47, 219.
      Campfield, L.A., et al. 1995. Science 269, 546.
      Halaas, J.L., et al. 1995. Science 269, 543.
      Pelleymounter, M.A., et al. 1995. Science 269, 540.
      Zhang, Y., et al. 1994. Nature 372, 425.
      Product Information
      CAS number177404-21-6
      FormLyophilized
      FormulationLyophilized from a sterile filtered solution in PBS.
      Quality LevelMQ100
      Applications
      Biological Information
      Biological activityED₅₀ = 0.4-2 ng/ml as measured by its ability to induce proliferation of leptin-dependent rOB-R transfected murine BAF3 cells
      Purity≥97% by SDS-PAGE
      Physicochemical Information
      ContaminantsEndotoxin: ≤1.0 EU/µg leptin
      Dimensions
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Storage and Shipping Information
      Ship Code Ambient Temperature Only
      Toxicity Standard Handling
      Storage ≤ -70°C
      Do not freeze Ok to freeze
      Special InstructionsTo reconstitute lyophilized leptin, add 15 mM sterile HCl (0.5 ml/1 mg vial or 2.5 ml/5 mg vial) to the vial. After the protein is completely dissolved, add 7.5 mM sterile NaOH (0.3 ml/1mg vial or 1.5 ml/5 mg vial) to bring the pH to ~5.2. Lyophilized samples are stable for at least six months at -70°C. Upon reconstitution, this cytokine can be stored under sterile conditions at 4°C for one month or at -70°C for three months without detectable loss of activity. Avoid repeated freeze/thaw cycles of reconstituted solutions.
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications
      Global Trade Item Number
      カタログ番号 GTIN
      429700-1MGCN 04055977210132

      Documentation

      Leptin, Human, Recombinant, E. coli (M)SDS

      タイトル

      英語版製品安全データシート((M)SDS) 

      Leptin, Human, Recombinant, E. coli 試験成績書(CoA)

      タイトルロット番号
      429700

      参考資料

      参考資料の概要
      Anderwald, C., et al. 2002. Mol. Endocrinol. 16, 1612.
      Ookuma, M., et al. 1998. Diabetes 47, 219.
      Campfield, L.A., et al. 1995. Science 269, 546.
      Halaas, J.L., et al. 1995. Science 269, 543.
      Pelleymounter, M.A., et al. 1995. Science 269, 540.
      Zhang, Y., et al. 1994. Nature 372, 425.
      データシート

      Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.

      Revision14-May-2008 RFH
      SynonymsrhOB
      DescriptionRecombinant, human leptin expressed in E. coli. Leptin was originally identified as a protein product of the mouse obese gene. Mice with mutations in the obese gene that block the synthesis of leptin have been found to be obese and diabetic and to have reduced activity, metabolism and body temperature. cDNA clones encoding leptin have been isolated from human, simian, mouse and rat cells. Human leptin shares approximately 84% sequence identity with the mouse protein. Human leptin cDNA encodes a 167 amino acid residue protein with a 21 amino acid signal sequence that is cleaved to yield the 146 amino acid mature protein. The expression of leptin mRNA has been shown to be restricted to adipose tissue.

      A high-affinity receptor for leptin (OB-R) with homology to gp130 and the G-CSF receptor was subsequently cloned. The OB-R cytoplasmic domain transduces the leptin signal through the JAK-STAT pathway. Although OB-R mRNA was initially shown to be expressed predominantly in the choroid plexus and in the hypothalamus, more recent data also revealed the expression of this receptor in endothelial cells (Ecs). Furthermore, the angiogenic activity of leptin has been demonstrated both in vitro and in vivo, suggesting a physical mechanism whereby leptin-induced angiogenesis may facilitate increased energy expenditure.
      FormLyophilized
      FormulationLyophilized from a sterile filtered solution in PBS.
      CAS number177404-21-6
      Purity≥97% by SDS-PAGE
      ContaminantsEndotoxin: ≤1.0 EU/µg leptin
      Biological activityED₅₀ = 0.4-2 ng/ml as measured by its ability to induce proliferation of leptin-dependent rOB-R transfected murine BAF3 cells
      Storage ≤ -70°C
      Do Not Freeze Ok to freeze
      Special InstructionsTo reconstitute lyophilized leptin, add 15 mM sterile HCl (0.5 ml/1 mg vial or 2.5 ml/5 mg vial) to the vial. After the protein is completely dissolved, add 7.5 mM sterile NaOH (0.3 ml/1mg vial or 1.5 ml/5 mg vial) to bring the pH to ~5.2. Lyophilized samples are stable for at least six months at -70°C. Upon reconstitution, this cytokine can be stored under sterile conditions at 4°C for one month or at -70°C for three months without detectable loss of activity. Avoid repeated freeze/thaw cycles of reconstituted solutions.
      Toxicity Standard Handling
      Merck USA index14, 5443
      ReferencesAnderwald, C., et al. 2002. Mol. Endocrinol. 16, 1612.
      Ookuma, M., et al. 1998. Diabetes 47, 219.
      Campfield, L.A., et al. 1995. Science 269, 546.
      Halaas, J.L., et al. 1995. Science 269, 543.
      Pelleymounter, M.A., et al. 1995. Science 269, 540.
      Zhang, Y., et al. 1994. Nature 372, 425.