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nm 134268  (OriGene)


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    Structured Review

    OriGene nm 134268
    Nm 134268, supplied by OriGene, used in various techniques. Bioz Stars score: 90/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/sc321813/Cytoglobin+(CYGB)+(NM_134268)+Human+Untagged+Clone/pmc04821708-118-21-13
    Average 90 stars, based on 8 article reviews
    nm 134268 - by Bioz Stars, 2026-09
    90/100 stars

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    Related Articles

    Clone Assay:

    Article Title: Peroxidase Activation of Cytoglobin by Anionic phospholipids: Mechanisms and Consequences
    Article Snippet: LC-MS/MS analysis was performed using a Dionex Ultimate 3000 RSLC nano system coupled on-line to a Q-Exactive hybrid quadrupole-orbitrap mass spectrometer (ThermoFisher Scientific) using a C18 column (XTerra 2.5 μm, 125 Å, 50 × 2 mm (Waters)). .. In summary, the region encoding the human Cygb protein was cloned from the Origene (Rockville, MD) cDNA clone SC321813 ( {"type":"entrez-nucleotide","attrs":{"text":"NM_134268","term_id":"374253798","term_text":"NM_134268"}} NM_134268 ) and inserted into the Nco I/ Hin dIII restriction sites of the pET28a plasmid (Novagen) generating the pET28- Hsa Cygb plasmid. .. The plasmid was transformed into SoluBL21 E. coli cells (Genlantis).

    Plasmid Preparation:

    Article Title: Peroxidase Activation of Cytoglobin by Anionic phospholipids: Mechanisms and Consequences
    Article Snippet: LC-MS/MS analysis was performed using a Dionex Ultimate 3000 RSLC nano system coupled on-line to a Q-Exactive hybrid quadrupole-orbitrap mass spectrometer (ThermoFisher Scientific) using a C18 column (XTerra 2.5 μm, 125 Å, 50 × 2 mm (Waters)). .. In summary, the region encoding the human Cygb protein was cloned from the Origene (Rockville, MD) cDNA clone SC321813 ( {"type":"entrez-nucleotide","attrs":{"text":"NM_134268","term_id":"374253798","term_text":"NM_134268"}} NM_134268 ) and inserted into the Nco I/ Hin dIII restriction sites of the pET28a plasmid (Novagen) generating the pET28- Hsa Cygb plasmid. .. The plasmid was transformed into SoluBL21 E. coli cells (Genlantis).



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    Fig. 7. Formation of disulfide bond between Cys38 and Cys83 induces the bending of the E helix and an increase of the distance between E and F helices. The figure shows the overlay of the hexa-coordinated crystal structure of the C38S/C83S mutant of <t>human</t> <t>Cygb</t> (purple, PDB ID: 1UT0) with a model of the penta-coordinated, ferric wild-type structure (cyan). The yellow dashed line indicates the distance between the alpha carbons of Ala88 (E helix) and Val105 (F helix). Molecular dynamics simulations indicate that the formation of the disulfide bond causes an increase in this interhelical distance (8.04 ± 0.64 Å vs 7.2 Å, respectively), allowing for the binding of hydrophobic chains in the hydrophobic core of Cygb.
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    Fig. 7. Formation of disulfide bond between Cys38 and Cys83 induces the bending of the E helix and an increase of the distance between E and F helices. The figure shows the overlay of the hexa-coordinated crystal structure of the C38S/C83S mutant of <t>human</t> <t>Cygb</t> (purple, PDB ID: 1UT0) with a model of the penta-coordinated, ferric wild-type structure (cyan). The yellow dashed line indicates the distance between the alpha carbons of Ala88 (E helix) and Val105 (F helix). Molecular dynamics simulations indicate that the formation of the disulfide bond causes an increase in this interhelical distance (8.04 ± 0.64 Å vs 7.2 Å, respectively), allowing for the binding of hydrophobic chains in the hydrophobic core of Cygb.
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    Fig. 7. Formation of disulfide bond between Cys38 and Cys83 induces the bending of the E helix and an increase of the distance between E and F helices. The figure shows the overlay of the hexa-coordinated crystal structure of the C38S/C83S mutant of human Cygb (purple, PDB ID: 1UT0) with a model of the penta-coordinated, ferric wild-type structure (cyan). The yellow dashed line indicates the distance between the alpha carbons of Ala88 (E helix) and Val105 (F helix). Molecular dynamics simulations indicate that the formation of the disulfide bond causes an increase in this interhelical distance (8.04 ± 0.64 Å vs 7.2 Å, respectively), allowing for the binding of hydrophobic chains in the hydrophobic core of Cygb.

    Journal: Biochimica et biophysica acta

    Article Title: Peroxidase activation of cytoglobin by anionic phospholipids: Mechanisms and consequences.

    doi: 10.1016/j.bbalip.2016.02.022

    Figure Lengend Snippet: Fig. 7. Formation of disulfide bond between Cys38 and Cys83 induces the bending of the E helix and an increase of the distance between E and F helices. The figure shows the overlay of the hexa-coordinated crystal structure of the C38S/C83S mutant of human Cygb (purple, PDB ID: 1UT0) with a model of the penta-coordinated, ferric wild-type structure (cyan). The yellow dashed line indicates the distance between the alpha carbons of Ala88 (E helix) and Val105 (F helix). Molecular dynamics simulations indicate that the formation of the disulfide bond causes an increase in this interhelical distance (8.04 ± 0.64 Å vs 7.2 Å, respectively), allowing for the binding of hydrophobic chains in the hydrophobic core of Cygb.

    Article Snippet: In summary, the region encoding the human Cygb protein was cloned from the Origene (Rockville, MD) cDNA clone SC321813 (NM_134268) and inserted into the NcoI/HindIII restriction sites of the pET28a plasmid (Novagen) generating the pET28–HsaCygb plasmid.

    Techniques: Mutagenesis, Binding Assay