Zinc-Chelated Separopore® 4B-CL
€0.00
In stock
SKU
BW-20181049
Application:
Zn2+-chelated Separopore® 4B-CL is an imminodiacetate (IDA) immobilized metal affinity chromatography (IMAC) matrix that seperates proteins via their differences in affinity to Zn2+ ions. Zn2+-chelated Separopore® 4B-CL is ideal for purification of recombinant proteins containing (His)6 fusion tag.
Note: Separopore® is a cost-effective equivalent to Sepharose® in all of its physical properties and binding characteristics.
Technical Specifications:
Chelating group: Nickel
Matrix: Separopore® 4B-CL (crosslinked agarose beads, 4%)
Particle size range: 52 – 165 µm
Matrix activation: Epoxy
Metal ion capacity: >20 µmol Zn2+ / ml drained gel
pH stability: 3 – 12
Supplied as suspension in 20% ethanol
References:
Targeting of metallothionein by L-homocysteine: a novel mechanism for disruption of zinc and redox homeostasis. Arterioscler Thromb Vasc Biol. (2007) 27: 49-54.
Identification of serotonin-sensitive aryl acylamidase activity with cobra venom acetylcholinesterase. Indian J Biochem Biophys. (2003) 40: 92-7.
Selective inactivation of butyrylcholinesterase with metal chelators suggests there is more than one metal binding site. Int J Biochem Cell Biol. (1998) 30: 695-705.
Isolation and partial characterization of an endopeptidase from Enterolobium contortisiliquum seeds. Braz J Med Biol Res. (1994) 27: 1299-310.
Collagenases from human and rat skin fibroblasts purified on a zinc chelating column reveal marked differences in latency as a result of serum culture conditions. Int J Biochem. (1992) 24: 725-35.
Evidence for presence of Zn+2-binding site in acetylcholinesterase. Biochimie. (2009) 91: 526-32.
Construction and characterization of a recombinant chimeric plasminogen activator consisting of a fibrin peptide and a low molecular mass single-chain urokinase. Biochimie. (2001) 83: 1049-55.
Modification of surface histidine residues abolishes the cytotoxic activity of Clostridium difficile toxin A. Toxicon. (2001) 39: 325-33.
Expression of active human tissue-type plasminogen activator in Escherichia coli. Appl Environ Microbiol. (1998) 64: 4891-6.
Serum butyrylcholinesterase of non-human primate shows amine sensitive aryl acyl amidase and metallopeptidase activities and characteristics similar to those of the human serum enzyme. Indian J Biochem Biophys. (1998) 35: 148-56.
Human seminal plasma beta-microseminoprotein: its purification, characterization, and immunohistochemical localization. Int J Biochem Cell Biol. (1995) 27: 603-11.
Leukemic cells (HL-60) produce a novel extracellular matrix-degrading proteinase that is not inhibited by tissue inhibitors of matrix metalloproteinases (TIMPs). Exp Hematol. (1995) 23: 155-60.
Biochemical and molecular characterization of stromelysin synthesized by human osteoarthritic chondrocytes stimulated with recombinant human interleukin-1. Clin Exp Rheumatol. (1994) 12: 489-96.
Cerebral plasminogen activator activity in spontaneously hypertensive stroke-prone rats. Stroke. (1992) 23: 995-9.
Zinc chelates bind human hemopexin. Acta Chem Scand. (1991) 45: 537-8.
Purification of a procollagenase-activator present in medium of cultured guinea pig carrageenin granuloma. Connect Tissue Res. (1991) 26: 259-69.
Purification and properties of extracellular matrix-degrading metallo-proteinase overproduced by Rous sarcoma virus-transformed rat liver cell line, and its identification as transin. J Biochem. (1990) 108: 537-43.
Partial amino acid sequence of human PMN leukocyte procollagenase. Biol Chem Hoppe Seyler. (1990) 371: 295-304.
Characterization and activation of procollagenase from human polymorphonuclear leucocytes. N-terminal sequence determination of the proenzyme and various proteolytically activated forms. Eur J Biochem. (1990) 189: 295-300.
Purification and characterization of a plasma factor which cleaves single-chain form of t-PA and u-PA. Thromb Res Suppl. (1990) 10: 27-43.
Leukocyte tissue-type plasminogen activator activity in dialysis patients. Int J Artif Organs. (1989) 12: 91-5.
Gelatin-degrading type IV collagenase isolated from human small cell lung cancer. Invasion Metastasis. (1989) 9: 167-81.
The collagenase produced by neoplastic rat epithelial cells: modulation of secretion, molecular weight characteristics, and purification. Matrix. (1989) 9: 7-16.
Purification of a gelatin-degrading type IV collagenase secreted by ras oncogene-transformed fibroblasts. J Natl Cancer Inst. (1988) 80: 1416-20.
Purification and characterization of natural and recombinant human plasminogen activator inhibitor-1 (PAI-1). Eur J Biochem. (1988) 175: 531-40.
Related products:
Metal ion-chelating-Separopore® 4B-CL (Metal-free) (SKU # 20181020)
Co2+-chelated Separopore® 4B-CL (SKU # 20181047)
Cu2+-chelated Separopore® 4B-CL (SKU # 20181048)
Ni2+-chelated Separopore® 4B-CL (SKU # 20181046)
Usage: bioWORLD's products are supplied for LABORATORY RESEARCH USE ONLY. The product may not be used as a drug, agricultural or pesticidal product , food additive or as a household chemical.
Hazmat Shipping: Non-hazardous
Storage: 2-8°C
Brand Name: bioPLUS™, Separopore®
Zn2+-chelated Separopore® 4B-CL is an imminodiacetate (IDA) immobilized metal affinity chromatography (IMAC) matrix that seperates proteins via their differences in affinity to Zn2+ ions. Zn2+-chelated Separopore® 4B-CL is ideal for purification of recombinant proteins containing (His)6 fusion tag.
Note: Separopore® is a cost-effective equivalent to Sepharose® in all of its physical properties and binding characteristics.
Technical Specifications:
Chelating group: Nickel
Matrix: Separopore® 4B-CL (crosslinked agarose beads, 4%)
Particle size range: 52 – 165 µm
Matrix activation: Epoxy
Metal ion capacity: >20 µmol Zn2+ / ml drained gel
pH stability: 3 – 12
Supplied as suspension in 20% ethanol
References:
Targeting of metallothionein by L-homocysteine: a novel mechanism for disruption of zinc and redox homeostasis. Arterioscler Thromb Vasc Biol. (2007) 27: 49-54.
Identification of serotonin-sensitive aryl acylamidase activity with cobra venom acetylcholinesterase. Indian J Biochem Biophys. (2003) 40: 92-7.
Selective inactivation of butyrylcholinesterase with metal chelators suggests there is more than one metal binding site. Int J Biochem Cell Biol. (1998) 30: 695-705.
Isolation and partial characterization of an endopeptidase from Enterolobium contortisiliquum seeds. Braz J Med Biol Res. (1994) 27: 1299-310.
Collagenases from human and rat skin fibroblasts purified on a zinc chelating column reveal marked differences in latency as a result of serum culture conditions. Int J Biochem. (1992) 24: 725-35.
Evidence for presence of Zn+2-binding site in acetylcholinesterase. Biochimie. (2009) 91: 526-32.
Construction and characterization of a recombinant chimeric plasminogen activator consisting of a fibrin peptide and a low molecular mass single-chain urokinase. Biochimie. (2001) 83: 1049-55.
Modification of surface histidine residues abolishes the cytotoxic activity of Clostridium difficile toxin A. Toxicon. (2001) 39: 325-33.
Expression of active human tissue-type plasminogen activator in Escherichia coli. Appl Environ Microbiol. (1998) 64: 4891-6.
Serum butyrylcholinesterase of non-human primate shows amine sensitive aryl acyl amidase and metallopeptidase activities and characteristics similar to those of the human serum enzyme. Indian J Biochem Biophys. (1998) 35: 148-56.
Human seminal plasma beta-microseminoprotein: its purification, characterization, and immunohistochemical localization. Int J Biochem Cell Biol. (1995) 27: 603-11.
Leukemic cells (HL-60) produce a novel extracellular matrix-degrading proteinase that is not inhibited by tissue inhibitors of matrix metalloproteinases (TIMPs). Exp Hematol. (1995) 23: 155-60.
Biochemical and molecular characterization of stromelysin synthesized by human osteoarthritic chondrocytes stimulated with recombinant human interleukin-1. Clin Exp Rheumatol. (1994) 12: 489-96.
Cerebral plasminogen activator activity in spontaneously hypertensive stroke-prone rats. Stroke. (1992) 23: 995-9.
Zinc chelates bind human hemopexin. Acta Chem Scand. (1991) 45: 537-8.
Purification of a procollagenase-activator present in medium of cultured guinea pig carrageenin granuloma. Connect Tissue Res. (1991) 26: 259-69.
Purification and properties of extracellular matrix-degrading metallo-proteinase overproduced by Rous sarcoma virus-transformed rat liver cell line, and its identification as transin. J Biochem. (1990) 108: 537-43.
Partial amino acid sequence of human PMN leukocyte procollagenase. Biol Chem Hoppe Seyler. (1990) 371: 295-304.
Characterization and activation of procollagenase from human polymorphonuclear leucocytes. N-terminal sequence determination of the proenzyme and various proteolytically activated forms. Eur J Biochem. (1990) 189: 295-300.
Purification and characterization of a plasma factor which cleaves single-chain form of t-PA and u-PA. Thromb Res Suppl. (1990) 10: 27-43.
Leukocyte tissue-type plasminogen activator activity in dialysis patients. Int J Artif Organs. (1989) 12: 91-5.
Gelatin-degrading type IV collagenase isolated from human small cell lung cancer. Invasion Metastasis. (1989) 9: 167-81.
The collagenase produced by neoplastic rat epithelial cells: modulation of secretion, molecular weight characteristics, and purification. Matrix. (1989) 9: 7-16.
Purification of a gelatin-degrading type IV collagenase secreted by ras oncogene-transformed fibroblasts. J Natl Cancer Inst. (1988) 80: 1416-20.
Purification and characterization of natural and recombinant human plasminogen activator inhibitor-1 (PAI-1). Eur J Biochem. (1988) 175: 531-40.
Related products:
Metal ion-chelating-Separopore® 4B-CL (Metal-free) (SKU # 20181020)
Co2+-chelated Separopore® 4B-CL (SKU # 20181047)
Cu2+-chelated Separopore® 4B-CL (SKU # 20181048)
Ni2+-chelated Separopore® 4B-CL (SKU # 20181046)
Usage: bioWORLD's products are supplied for LABORATORY RESEARCH USE ONLY. The product may not be used as a drug, agricultural or pesticidal product , food additive or as a household chemical.
Hazmat Shipping: Non-hazardous
Storage: 2-8°C
Brand Name: bioPLUS™, Separopore®
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