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3745 Hemoglobin, Bovine Erythrocytes

Hemoglobin, Bovine Erythrocytes, CAS 9008-02-0, is an iron-containing oxygen-transport metalloprotein. Suitable as a substrate for proteases, such as papain, pepsin, and trypsin.

Hemoglobin, Bovine Erythrocytes: Ficha de datos de seguridad (MSDS o SDS), certificado de análisis y de calidad (CoA y CoQ), expedientes, folletos y otros documentos disponibles.
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3745
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Descripción

Replacement Information

Precios y disponibilidad

Número de referencia DisponiblidadEmbalaje Cant./Env. Precio Cantidad
3745-5GM
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      Description
      OverviewNative hemoglobin from bovine erythrocytes. A major oxygen-transporting component of red blood cells that is also nitric oxide scavenger. Blocks carbachol-stimulated cGMP production. This preparation contains primarily Ferric-hemoglobin and must be reduced to the ferrous form to bind molecular oxygen. Note: this preparation contains primarily ferric-hemoglobin and must be reduced to the ferrous form to bind molecular oxygen.
      Catalogue Number3745
      Brand Family Calbiochem®
      References
      ReferencesGow, A.J., et al. 1999. Proc. Natl. Acad. Sci. USA 96, 9027.
      Castoldi, A.F., et al. 1993. Brain Res. 610, 57.
      Bredt, D.S., and Snyder, S.H. 1989. Proc. Natl. Acad. Sci. USA 86, 9030.
      Product Information
      CAS number9008-02-0
      FormLyophilized
      Quality LevelMQ100
      Applications
      ApplicationHemoglobin, Bovine Erythrocytes, CAS 9008-02-0, is an iron-containing oxygen-transport metalloprotein. Suitable as a substrate for proteases, such as papain, pepsin, and trypsin.
      Biological Information
      Purity≥95% by SDS-PAGE
      Physicochemical Information
      Dimensions
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Storage and Shipping Information
      Ship Code Blue Ice Only
      Toxicity Standard Handling
      Storage -20°C
      Do not freeze Ok to freeze
      Special InstructionsFollowing recosntitution aliquot and freeze (-20°C). Stock solutions are stable for up to 3 months at -20°C.
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications
      Global Trade Item Number
      Número de referencia GTIN
      3745-5GM 04055977191219

      Documentation

      Hemoglobin, Bovine Erythrocytes Ficha datos de seguridad (MSDS)

      Título

      Ficha técnica de seguridad del material (MSDS) 

      Hemoglobin, Bovine Erythrocytes Certificados de análisis

      CargoNúmero de lote
      3745

      Referencias bibliográficas

      Visión general referencias
      Gow, A.J., et al. 1999. Proc. Natl. Acad. Sci. USA 96, 9027.
      Castoldi, A.F., et al. 1993. Brain Res. 610, 57.
      Bredt, D.S., and Snyder, S.H. 1989. Proc. Natl. Acad. Sci. USA 86, 9030.
      Ficha técnica

      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.

      Revision12-May-2008 RFH
      DescriptionNative hemoglobin from bovine erythrocytes. A major oxygen-transporting component of red blood cells. A nitric oxide scavenger that complexes with nitric oxide. Blocks carbachol-stimulated cGMP production. This preparation contains primarily ferric-hemoglobin and must be reduced to the ferrous form to bind molecular oxygen.
      FormLyophilized
      CAS number9008-02-0
      Purity≥95% by SDS-PAGE
      SolubilityAqueous buffers (1 mg/ml) or H₂O (1 mg/ml)
      Storage -20°C
      Do Not Freeze Ok to freeze
      Special InstructionsFollowing recosntitution aliquot and freeze (-20°C). Stock solutions are stable for up to 3 months at -20°C.
      Toxicity Standard Handling
      Merck USA index14, 4648
      ReferencesGow, A.J., et al. 1999. Proc. Natl. Acad. Sci. USA 96, 9027.
      Castoldi, A.F., et al. 1993. Brain Res. 610, 57.
      Bredt, D.S., and Snyder, S.H. 1989. Proc. Natl. Acad. Sci. USA 86, 9030.