sc 28348 Search Results


jmjd6  (Santa Cruz Biotechnology)
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Santa Cruz Biotechnology jmjd6
Figure 2. Protein homology and structural features. (A) Schematic representation of the <t>JMJD6</t> protein. Eight mutations located at the JmjC domain (174-288 aa). (B) Multiple sequence alignment of the JMJD6 protein. Different colors represent different amino acids. Highly conserved mutation sites (consensus score > 90) are labeled in red (P129, F156, H187, K204, F266, and P268). (C) Crystal structure of JMJD6. H187 and K204 are located in the JMJD6 enzyme activity region, and H187 is the nearest site to the enzyme activity center. The purple ball represents Fe(II).
Jmjd6, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Figure 2. Protein homology and structural features. (A) Schematic representation of the JMJD6 protein. Eight mutations located at the JmjC domain (174-288 aa). (B) Multiple sequence alignment of the JMJD6 protein. Different colors represent different amino acids. Highly conserved mutation sites (consensus score > 90) are labeled in red (P129, F156, H187, K204, F266, and P268). (C) Crystal structure of JMJD6. H187 and K204 are located in the JMJD6 enzyme activity region, and H187 is the nearest site to the enzyme activity center. The purple ball represents Fe(II).

Journal: Molecules

Article Title: Computational and Mass Spectrometry-Based Approach Identify Deleterious Non-Synonymous Single Nucleotide Polymorphisms (nsSNPs) in JMJD6

doi: 10.3390/molecules26154653

Figure Lengend Snippet: Figure 2. Protein homology and structural features. (A) Schematic representation of the JMJD6 protein. Eight mutations located at the JmjC domain (174-288 aa). (B) Multiple sequence alignment of the JMJD6 protein. Different colors represent different amino acids. Highly conserved mutation sites (consensus score > 90) are labeled in red (P129, F156, H187, K204, F266, and P268). (C) Crystal structure of JMJD6. H187 and K204 are located in the JMJD6 enzyme activity region, and H187 is the nearest site to the enzyme activity center. The purple ball represents Fe(II).

Article Snippet: The sources of antibodies against the following proteins were as follows: β-actin (SAB3500350) from Sigma (Sigma-Aldrich, Inc., St. Louis, MO, USA), JMJD6 (sc-28348) from Santa Cruz (Santa Cruz Biotechnology, Inc., Santa Cruz, CA, USA), p53 monoclonal antibody (K0181-3), and p21 (K0081-3) from MBL (Medical & Biological Laboratories Co., Ltd, Tokyo, Japan).

Techniques: Sequencing, Mutagenesis, Labeling, Activity Assay

Figure 3. JMJD6 (H187R) abolishes the lysyl-hydroxylation of U2AF65 and influences mRNA splicing. (A,B) MS/MS analysis of recombinant U2AF65 reveals the hydroxylation of Lys-276 (A) by JMJD6 (WT) and no hydroxylation of Lys-276

Journal: Molecules

Article Title: Computational and Mass Spectrometry-Based Approach Identify Deleterious Non-Synonymous Single Nucleotide Polymorphisms (nsSNPs) in JMJD6

doi: 10.3390/molecules26154653

Figure Lengend Snippet: Figure 3. JMJD6 (H187R) abolishes the lysyl-hydroxylation of U2AF65 and influences mRNA splicing. (A,B) MS/MS analysis of recombinant U2AF65 reveals the hydroxylation of Lys-276 (A) by JMJD6 (WT) and no hydroxylation of Lys-276

Article Snippet: The sources of antibodies against the following proteins were as follows: β-actin (SAB3500350) from Sigma (Sigma-Aldrich, Inc., St. Louis, MO, USA), JMJD6 (sc-28348) from Santa Cruz (Santa Cruz Biotechnology, Inc., Santa Cruz, CA, USA), p53 monoclonal antibody (K0181-3), and p21 (K0081-3) from MBL (Medical & Biological Laboratories Co., Ltd, Tokyo, Japan).

Techniques: Tandem Mass Spectroscopy, Recombinant

Figure 4. JMJD6 (H187R) abolishes the lysyl-hydroxylation of p53 and cannot inhibit p21 expression. (A,B) MS/MS analysis of recombinant p53 reveals the hydroxylation of Lys-382 (A) by JMJD6 (WT) and no hydroxylation of Lys-382 (B) by JMJD6

Journal: Molecules

Article Title: Computational and Mass Spectrometry-Based Approach Identify Deleterious Non-Synonymous Single Nucleotide Polymorphisms (nsSNPs) in JMJD6

doi: 10.3390/molecules26154653

Figure Lengend Snippet: Figure 4. JMJD6 (H187R) abolishes the lysyl-hydroxylation of p53 and cannot inhibit p21 expression. (A,B) MS/MS analysis of recombinant p53 reveals the hydroxylation of Lys-382 (A) by JMJD6 (WT) and no hydroxylation of Lys-382 (B) by JMJD6

Article Snippet: The sources of antibodies against the following proteins were as follows: β-actin (SAB3500350) from Sigma (Sigma-Aldrich, Inc., St. Louis, MO, USA), JMJD6 (sc-28348) from Santa Cruz (Santa Cruz Biotechnology, Inc., Santa Cruz, CA, USA), p53 monoclonal antibody (K0181-3), and p21 (K0081-3) from MBL (Medical & Biological Laboratories Co., Ltd, Tokyo, Japan).

Techniques: Expressing, Tandem Mass Spectroscopy, Recombinant