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hprm1  (OriGene)


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    Structured Review

    OriGene hprm1
    Figure 2. Optimization of <t>hPRM1.</t> (a) Amino acid sequence alignment of protamine from salmon and humans. [*] indicates a conserved residue, [:] indicates groups with a strong similarity in their properties, and [.] indicates groups of weakly similar properties. (b) Partial, arginine-rich hPRM1 sequence of human- and E. coli-optimized genes. (c) Western blot of recombinant hPRM1 protein expressed in E. coli, using the human- or the E. coli-optimized DNA. (d) MTRasym plots and Western blot analysis (inset) of E. coli lysates from cells expressing either hPRM1 (red) or CD (blue). (e) The comparison of mean MTRasym values of hPRM1 (red bars) and CD (blue bars) at the 1.5 and 3.6 ppm frequency offsets. The mean MTRasym (+SD) were calculated from four independent measurements for each cell type (n = 4). CEST data were acquired at 11.7T, 37 °C, pH = 7.4, B1 = 4.7 μT, and tsat = 4000 ms.
    Hprm1, supplied by OriGene, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/nm+002761/pm24138139-107-4-9?v=OriGene
    Average 90 stars, based on 1 article reviews
    hprm1 - by Bioz Stars, 2026-06
    90/100 stars

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    1) Product Images from "Human protamine-1 as an MRI reporter gene based on chemical exchange."

    Article Title: Human protamine-1 as an MRI reporter gene based on chemical exchange.

    Journal: ACS chemical biology

    doi: 10.1021/cb400617q

    Figure 2. Optimization of hPRM1. (a) Amino acid sequence alignment of protamine from salmon and humans. [*] indicates a conserved residue, [:] indicates groups with a strong similarity in their properties, and [.] indicates groups of weakly similar properties. (b) Partial, arginine-rich hPRM1 sequence of human- and E. coli-optimized genes. (c) Western blot of recombinant hPRM1 protein expressed in E. coli, using the human- or the E. coli-optimized DNA. (d) MTRasym plots and Western blot analysis (inset) of E. coli lysates from cells expressing either hPRM1 (red) or CD (blue). (e) The comparison of mean MTRasym values of hPRM1 (red bars) and CD (blue bars) at the 1.5 and 3.6 ppm frequency offsets. The mean MTRasym (+SD) were calculated from four independent measurements for each cell type (n = 4). CEST data were acquired at 11.7T, 37 °C, pH = 7.4, B1 = 4.7 μT, and tsat = 4000 ms.
    Figure Legend Snippet: Figure 2. Optimization of hPRM1. (a) Amino acid sequence alignment of protamine from salmon and humans. [*] indicates a conserved residue, [:] indicates groups with a strong similarity in their properties, and [.] indicates groups of weakly similar properties. (b) Partial, arginine-rich hPRM1 sequence of human- and E. coli-optimized genes. (c) Western blot of recombinant hPRM1 protein expressed in E. coli, using the human- or the E. coli-optimized DNA. (d) MTRasym plots and Western blot analysis (inset) of E. coli lysates from cells expressing either hPRM1 (red) or CD (blue). (e) The comparison of mean MTRasym values of hPRM1 (red bars) and CD (blue bars) at the 1.5 and 3.6 ppm frequency offsets. The mean MTRasym (+SD) were calculated from four independent measurements for each cell type (n = 4). CEST data were acquired at 11.7T, 37 °C, pH = 7.4, B1 = 4.7 μT, and tsat = 4000 ms.

    Techniques Used: Sequencing, Residue, Western Blot, Recombinant, Expressing, Comparison

    Figure 4. MR imaging of hPRM1 reporter gene expression in live cells in a three-dimensional cell culture system. (a) Bright-field microscopic images of encapsulated 293HEK cells. (b) T2-weighted images and overlaid MTRasym maps of encapsulated cells obtained at the 1.5 and 3.6 ppm frequency offsets. (c) p-values as a function of the frequency offset from water (Dw), as calculated using a Student’s t test (two- tailed distribution, paired test). Red line represents p-value of 0.05 (significance level). (d) Mean MTRasym (±SD) at 1.5 ppm calculated from three samples containing encapsulated cells (293hPRM1 and 293wt). CEST data were acquired at 11.7 T, 37 °C, pH = 7.4, B1 = 3.6 μT, and tsat = 3000 ms.
    Figure Legend Snippet: Figure 4. MR imaging of hPRM1 reporter gene expression in live cells in a three-dimensional cell culture system. (a) Bright-field microscopic images of encapsulated 293HEK cells. (b) T2-weighted images and overlaid MTRasym maps of encapsulated cells obtained at the 1.5 and 3.6 ppm frequency offsets. (c) p-values as a function of the frequency offset from water (Dw), as calculated using a Student’s t test (two- tailed distribution, paired test). Red line represents p-value of 0.05 (significance level). (d) Mean MTRasym (±SD) at 1.5 ppm calculated from three samples containing encapsulated cells (293hPRM1 and 293wt). CEST data were acquired at 11.7 T, 37 °C, pH = 7.4, B1 = 3.6 μT, and tsat = 3000 ms.

    Techniques Used: Imaging, Gene Expression, Cell Culture, Two Tailed Test

    Figure 3. CEST MRI of HEK293 cell extracts. (a) Western blot, using an anti-V5 antibody, showing hPRM1 expression. (b) MTRasym plots (±SD; n = 3). (c) Representative MTRasym maps obtained at the 1.5 and 3.6 ppm frequency offsets. (d) Mean MTRasym (±SD) at the 1.5 ppm and 3.6 ppm frequency offsets. CEST data were acquired at 11.7T, 37 °C, pH = 7.4, B1 = 4.7 μT, and tsat = 4000 ms.
    Figure Legend Snippet: Figure 3. CEST MRI of HEK293 cell extracts. (a) Western blot, using an anti-V5 antibody, showing hPRM1 expression. (b) MTRasym plots (±SD; n = 3). (c) Representative MTRasym maps obtained at the 1.5 and 3.6 ppm frequency offsets. (d) Mean MTRasym (±SD) at the 1.5 ppm and 3.6 ppm frequency offsets. CEST data were acquired at 11.7T, 37 °C, pH = 7.4, B1 = 4.7 μT, and tsat = 4000 ms.

    Techniques Used: Western Blot, Expressing



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    Figure 2. Optimization of <t>hPRM1.</t> (a) Amino acid sequence alignment of protamine from salmon and humans. [*] indicates a conserved residue, [:] indicates groups with a strong similarity in their properties, and [.] indicates groups of weakly similar properties. (b) Partial, arginine-rich hPRM1 sequence of human- and E. coli-optimized genes. (c) Western blot of recombinant hPRM1 protein expressed in E. coli, using the human- or the E. coli-optimized DNA. (d) MTRasym plots and Western blot analysis (inset) of E. coli lysates from cells expressing either hPRM1 (red) or CD (blue). (e) The comparison of mean MTRasym values of hPRM1 (red bars) and CD (blue bars) at the 1.5 and 3.6 ppm frequency offsets. The mean MTRasym (+SD) were calculated from four independent measurements for each cell type (n = 4). CEST data were acquired at 11.7T, 37 °C, pH = 7.4, B1 = 4.7 μT, and tsat = 4000 ms.
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    Figure 2. Optimization of <t>hPRM1.</t> (a) Amino acid sequence alignment of protamine from salmon and humans. [*] indicates a conserved residue, [:] indicates groups with a strong similarity in their properties, and [.] indicates groups of weakly similar properties. (b) Partial, arginine-rich hPRM1 sequence of human- and E. coli-optimized genes. (c) Western blot of recombinant hPRM1 protein expressed in E. coli, using the human- or the E. coli-optimized DNA. (d) MTRasym plots and Western blot analysis (inset) of E. coli lysates from cells expressing either hPRM1 (red) or CD (blue). (e) The comparison of mean MTRasym values of hPRM1 (red bars) and CD (blue bars) at the 1.5 and 3.6 ppm frequency offsets. The mean MTRasym (+SD) were calculated from four independent measurements for each cell type (n = 4). CEST data were acquired at 11.7T, 37 °C, pH = 7.4, B1 = 4.7 μT, and tsat = 4000 ms.
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    Image Search Results


    Figure 2. Optimization of hPRM1. (a) Amino acid sequence alignment of protamine from salmon and humans. [*] indicates a conserved residue, [:] indicates groups with a strong similarity in their properties, and [.] indicates groups of weakly similar properties. (b) Partial, arginine-rich hPRM1 sequence of human- and E. coli-optimized genes. (c) Western blot of recombinant hPRM1 protein expressed in E. coli, using the human- or the E. coli-optimized DNA. (d) MTRasym plots and Western blot analysis (inset) of E. coli lysates from cells expressing either hPRM1 (red) or CD (blue). (e) The comparison of mean MTRasym values of hPRM1 (red bars) and CD (blue bars) at the 1.5 and 3.6 ppm frequency offsets. The mean MTRasym (+SD) were calculated from four independent measurements for each cell type (n = 4). CEST data were acquired at 11.7T, 37 °C, pH = 7.4, B1 = 4.7 μT, and tsat = 4000 ms.

    Journal: ACS chemical biology

    Article Title: Human protamine-1 as an MRI reporter gene based on chemical exchange.

    doi: 10.1021/cb400617q

    Figure Lengend Snippet: Figure 2. Optimization of hPRM1. (a) Amino acid sequence alignment of protamine from salmon and humans. [*] indicates a conserved residue, [:] indicates groups with a strong similarity in their properties, and [.] indicates groups of weakly similar properties. (b) Partial, arginine-rich hPRM1 sequence of human- and E. coli-optimized genes. (c) Western blot of recombinant hPRM1 protein expressed in E. coli, using the human- or the E. coli-optimized DNA. (d) MTRasym plots and Western blot analysis (inset) of E. coli lysates from cells expressing either hPRM1 (red) or CD (blue). (e) The comparison of mean MTRasym values of hPRM1 (red bars) and CD (blue bars) at the 1.5 and 3.6 ppm frequency offsets. The mean MTRasym (+SD) were calculated from four independent measurements for each cell type (n = 4). CEST data were acquired at 11.7T, 37 °C, pH = 7.4, B1 = 4.7 μT, and tsat = 4000 ms.

    Article Snippet: The gene encoding to hPRM1 (NM_002761) was obtained from Origene (Rockville, MD).

    Techniques: Sequencing, Residue, Western Blot, Recombinant, Expressing, Comparison

    Figure 4. MR imaging of hPRM1 reporter gene expression in live cells in a three-dimensional cell culture system. (a) Bright-field microscopic images of encapsulated 293HEK cells. (b) T2-weighted images and overlaid MTRasym maps of encapsulated cells obtained at the 1.5 and 3.6 ppm frequency offsets. (c) p-values as a function of the frequency offset from water (Dw), as calculated using a Student’s t test (two- tailed distribution, paired test). Red line represents p-value of 0.05 (significance level). (d) Mean MTRasym (±SD) at 1.5 ppm calculated from three samples containing encapsulated cells (293hPRM1 and 293wt). CEST data were acquired at 11.7 T, 37 °C, pH = 7.4, B1 = 3.6 μT, and tsat = 3000 ms.

    Journal: ACS chemical biology

    Article Title: Human protamine-1 as an MRI reporter gene based on chemical exchange.

    doi: 10.1021/cb400617q

    Figure Lengend Snippet: Figure 4. MR imaging of hPRM1 reporter gene expression in live cells in a three-dimensional cell culture system. (a) Bright-field microscopic images of encapsulated 293HEK cells. (b) T2-weighted images and overlaid MTRasym maps of encapsulated cells obtained at the 1.5 and 3.6 ppm frequency offsets. (c) p-values as a function of the frequency offset from water (Dw), as calculated using a Student’s t test (two- tailed distribution, paired test). Red line represents p-value of 0.05 (significance level). (d) Mean MTRasym (±SD) at 1.5 ppm calculated from three samples containing encapsulated cells (293hPRM1 and 293wt). CEST data were acquired at 11.7 T, 37 °C, pH = 7.4, B1 = 3.6 μT, and tsat = 3000 ms.

    Article Snippet: The gene encoding to hPRM1 (NM_002761) was obtained from Origene (Rockville, MD).

    Techniques: Imaging, Gene Expression, Cell Culture, Two Tailed Test

    Figure 3. CEST MRI of HEK293 cell extracts. (a) Western blot, using an anti-V5 antibody, showing hPRM1 expression. (b) MTRasym plots (±SD; n = 3). (c) Representative MTRasym maps obtained at the 1.5 and 3.6 ppm frequency offsets. (d) Mean MTRasym (±SD) at the 1.5 ppm and 3.6 ppm frequency offsets. CEST data were acquired at 11.7T, 37 °C, pH = 7.4, B1 = 4.7 μT, and tsat = 4000 ms.

    Journal: ACS chemical biology

    Article Title: Human protamine-1 as an MRI reporter gene based on chemical exchange.

    doi: 10.1021/cb400617q

    Figure Lengend Snippet: Figure 3. CEST MRI of HEK293 cell extracts. (a) Western blot, using an anti-V5 antibody, showing hPRM1 expression. (b) MTRasym plots (±SD; n = 3). (c) Representative MTRasym maps obtained at the 1.5 and 3.6 ppm frequency offsets. (d) Mean MTRasym (±SD) at the 1.5 ppm and 3.6 ppm frequency offsets. CEST data were acquired at 11.7T, 37 °C, pH = 7.4, B1 = 4.7 μT, and tsat = 4000 ms.

    Article Snippet: The gene encoding to hPRM1 (NM_002761) was obtained from Origene (Rockville, MD).

    Techniques: Western Blot, Expressing