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Proteintech palb2
Validation of the expression of 6 hub genes in CRC and AS by molecular biology experiments. (A-F) RT-qPCR validation of the differential expression of prognostic genes between normal and tumor tissues in CRC patients. (G) Western blot validation of the differential expression of 2 newly identified genes (HMMR and <t>PALB2)</t> between normal and tumor tissues in CRC. (H) Quantitative analysis of the relative grayscale values of Western blot bands for the 2 newly identified genes (HMMR and PALB2) in normal and tumor tissues of CRC. Data are presented as mean ± standard deviation (SD), with statistical significance indicated as * p < 0.05, *** p < 0.001, and **** p < 0.0001. ns indicates no statistical significance.
Palb2, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Images

1) Product Images from "Prognostic value and experimental validation of atherosclerosis-derived pathogenic genes in colorectal cancer"

Article Title: Prognostic value and experimental validation of atherosclerosis-derived pathogenic genes in colorectal cancer

Journal: Frontiers in Oncology

doi: 10.3389/fonc.2025.1728087

Validation of the expression of 6 hub genes in CRC and AS by molecular biology experiments. (A-F) RT-qPCR validation of the differential expression of prognostic genes between normal and tumor tissues in CRC patients. (G) Western blot validation of the differential expression of 2 newly identified genes (HMMR and PALB2) between normal and tumor tissues in CRC. (H) Quantitative analysis of the relative grayscale values of Western blot bands for the 2 newly identified genes (HMMR and PALB2) in normal and tumor tissues of CRC. Data are presented as mean ± standard deviation (SD), with statistical significance indicated as * p < 0.05, *** p < 0.001, and **** p < 0.0001. ns indicates no statistical significance.
Figure Legend Snippet: Validation of the expression of 6 hub genes in CRC and AS by molecular biology experiments. (A-F) RT-qPCR validation of the differential expression of prognostic genes between normal and tumor tissues in CRC patients. (G) Western blot validation of the differential expression of 2 newly identified genes (HMMR and PALB2) between normal and tumor tissues in CRC. (H) Quantitative analysis of the relative grayscale values of Western blot bands for the 2 newly identified genes (HMMR and PALB2) in normal and tumor tissues of CRC. Data are presented as mean ± standard deviation (SD), with statistical significance indicated as * p < 0.05, *** p < 0.001, and **** p < 0.0001. ns indicates no statistical significance.

Techniques Used: Biomarker Discovery, Expressing, Quantitative RT-PCR, Quantitative Proteomics, Western Blot, Standard Deviation

IHC staining validation. (A) The differential expression of PALB2 and HMMR in CRC tissues compared with normal tissues; (B) displays the differential expression of HMMR , PALB2 and PRR11 in AS tissues versus normal tissues. * p < 0.05.
Figure Legend Snippet: IHC staining validation. (A) The differential expression of PALB2 and HMMR in CRC tissues compared with normal tissues; (B) displays the differential expression of HMMR , PALB2 and PRR11 in AS tissues versus normal tissues. * p < 0.05.

Techniques Used: Immunohistochemistry, Biomarker Discovery, Quantitative Proteomics



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Bioss palb2 c ter
Key domains and interaction regions of <t>PALB2</t> protein and the P-T1 and P-T2 variants. ( A ) Domains and interaction regions of the PALB2 protein. The upper circles show the molecular surface representation of the Coiled–coil PALB2 (orange) dimerization, coil–coil PALB2-BRCA1 (green) interaction, PALB2-MRG15 (yellow) interaction, and PALB2-BRCA2 (cyan) interaction. The lower circles show the intrinsically disordered structure of the N-terminal (AlphaFold 2 prediction) and the β-sheet structure of the WD40 domain at the C-terminal. Ab1 and Ab2 represent the antigenic regions recognized by the PA5-48258 and BS-0588R PALB2 antibodies, respectively. ( B , C ) Diagram of the domains and interaction regions of PALB2 variants P-T1 and P-T2, respectively. CC, coil–coil motif; ChAM, chromatin association motif; FX, FXLP motif; NLS, nuclear export signal; BRCA1, BRCA1 DNA repair-associated; KEAP1, Kelch-like ECH-associated protein 1; RAD51, RAD51 recombinase; MRG15, MORF-related gene 15; BRCA2, BRCA2 DNA repair-associated; RAD51C, RAD51 paralog C; XRCC3, X-ray repair cross complementing 3; POLE, DNA polymerase epsilon (catalytic subunit) and RNF168, ring finger protein 168.
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Key domains and interaction regions of <t>PALB2</t> protein and the P-T1 and P-T2 variants. ( A ) Domains and interaction regions of the PALB2 protein. The upper circles show the molecular surface representation of the Coiled–coil PALB2 (orange) dimerization, coil–coil PALB2-BRCA1 (green) interaction, PALB2-MRG15 (yellow) interaction, and PALB2-BRCA2 (cyan) interaction. The lower circles show the intrinsically disordered structure of the N-terminal (AlphaFold 2 prediction) and the β-sheet structure of the WD40 domain at the C-terminal. Ab1 and Ab2 represent the antigenic regions recognized by the PA5-48258 and BS-0588R PALB2 antibodies, respectively. ( B , C ) Diagram of the domains and interaction regions of PALB2 variants P-T1 and P-T2, respectively. CC, coil–coil motif; ChAM, chromatin association motif; FX, FXLP motif; NLS, nuclear export signal; BRCA1, BRCA1 DNA repair-associated; KEAP1, Kelch-like ECH-associated protein 1; RAD51, RAD51 recombinase; MRG15, MORF-related gene 15; BRCA2, BRCA2 DNA repair-associated; RAD51C, RAD51 paralog C; XRCC3, X-ray repair cross complementing 3; POLE, DNA polymerase epsilon (catalytic subunit) and RNF168, ring finger protein 168.
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Validation of the expression of 6 hub genes in CRC and AS by molecular biology experiments. (A-F) RT-qPCR validation of the differential expression of prognostic genes between normal and tumor tissues in CRC patients. (G) Western blot validation of the differential expression of 2 newly identified genes (HMMR and <t>PALB2)</t> between normal and tumor tissues in CRC. (H) Quantitative analysis of the relative grayscale values of Western blot bands for the 2 newly identified genes (HMMR and PALB2) in normal and tumor tissues of CRC. Data are presented as mean ± standard deviation (SD), with statistical significance indicated as * p < 0.05, *** p < 0.001, and **** p < 0.0001. ns indicates no statistical significance.
Palb2, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Proteintech rabbit anti palb2 antibody
( A ) Sanger sequencing confirmation of Mettl14 arginine methylation deficient mouse model. In total, 13 arginine resides located at the C-terminal disordered region of Mettl14 were mutated to lysine residues. ( B ) The arginine methylation levels of Mettl14 in WT, heterozygous (WT/RK), and homozygous (RK/RK) mice were detected by IP-western blot using tissue lysates from mouse spleen and thymus. ( C ) The protein expression levels of several DNA repair genes, including BRCA1, ATRIP, and <t>PALB2,</t> were detected by western blot using Thymus tissues from WT, WT/RK, and RK/RK mice. ( D ) Mettl14 arginine methylation deficiency increases the population of primitive hematopoietic cells (LK cells). ** P = 0.0019. ( E ) Mettl14 arginine methylation deficiency increases the population of myeloid (Mac1 + Gr1 + ) cells in the BM, but not in the spleen. * P = 0.013. ( F ) Mettl14 arginine methylation deficiency decreases the B lymphoid (B220 + ) population in the BM, but not in the spleen. * P = 0.011. ( G ) Mettl14 arginine methylation deficiency decreases the T lymphoid (CD3 + ) population in the BM, but not in the spleen. Data from three independent replicates were analyzed by Student’s t test and shown as mean ± SD. ** P = 0.0097. .
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( A ) Sanger sequencing confirmation of Mettl14 arginine methylation deficient mouse model. In total, 13 arginine resides located at the C-terminal disordered region of Mettl14 were mutated to lysine residues. ( B ) The arginine methylation levels of Mettl14 in WT, heterozygous (WT/RK), and homozygous (RK/RK) mice were detected by IP-western blot using tissue lysates from mouse spleen and thymus. ( C ) The protein expression levels of several DNA repair genes, including BRCA1, ATRIP, and <t>PALB2,</t> were detected by western blot using Thymus tissues from WT, WT/RK, and RK/RK mice. ( D ) Mettl14 arginine methylation deficiency increases the population of primitive hematopoietic cells (LK cells). ** P = 0.0019. ( E ) Mettl14 arginine methylation deficiency increases the population of myeloid (Mac1 + Gr1 + ) cells in the BM, but not in the spleen. * P = 0.013. ( F ) Mettl14 arginine methylation deficiency decreases the B lymphoid (B220 + ) population in the BM, but not in the spleen. * P = 0.011. ( G ) Mettl14 arginine methylation deficiency decreases the T lymphoid (CD3 + ) population in the BM, but not in the spleen. Data from three independent replicates were analyzed by Student’s t test and shown as mean ± SD. ** P = 0.0097. .
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Proteintech anti palb2
( A ) Sanger sequencing confirmation of Mettl14 arginine methylation deficient mouse model. In total, 13 arginine resides located at the C-terminal disordered region of Mettl14 were mutated to lysine residues. ( B ) The arginine methylation levels of Mettl14 in WT, heterozygous (WT/RK), and homozygous (RK/RK) mice were detected by IP-western blot using tissue lysates from mouse spleen and thymus. ( C ) The protein expression levels of several DNA repair genes, including BRCA1, ATRIP, and <t>PALB2,</t> were detected by western blot using Thymus tissues from WT, WT/RK, and RK/RK mice. ( D ) Mettl14 arginine methylation deficiency increases the population of primitive hematopoietic cells (LK cells). ** P = 0.0019. ( E ) Mettl14 arginine methylation deficiency increases the population of myeloid (Mac1 + Gr1 + ) cells in the BM, but not in the spleen. * P = 0.013. ( F ) Mettl14 arginine methylation deficiency decreases the B lymphoid (B220 + ) population in the BM, but not in the spleen. * P = 0.011. ( G ) Mettl14 arginine methylation deficiency decreases the T lymphoid (CD3 + ) population in the BM, but not in the spleen. Data from three independent replicates were analyzed by Student’s t test and shown as mean ± SD. ** P = 0.0097. .
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Bioss cat bs 0588r
Key domains and interaction regions of PALB2 protein and the P-T1 and P-T2 variants. ( A ) Domains and interaction regions of the PALB2 protein. The upper circles show the molecular surface representation of the Coiled–coil PALB2 (orange) dimerization, coil–coil PALB2-BRCA1 (green) interaction, PALB2-MRG15 (yellow) interaction, and PALB2-BRCA2 (cyan) interaction. The lower circles show the intrinsically disordered structure of the N-terminal (AlphaFold 2 prediction) and the β-sheet structure of the WD40 domain at the C-terminal. Ab1 and Ab2 represent the antigenic regions recognized by the PA5-48258 and <t>BS-0588R</t> PALB2 antibodies, respectively. ( B , C ) Diagram of the domains and interaction regions of PALB2 variants P-T1 and P-T2, respectively. CC, coil–coil motif; ChAM, chromatin association motif; FX, FXLP motif; NLS, nuclear export signal; BRCA1, BRCA1 DNA repair-associated; KEAP1, Kelch-like ECH-associated protein 1; RAD51, RAD51 recombinase; MRG15, MORF-related gene 15; BRCA2, BRCA2 DNA repair-associated; RAD51C, RAD51 paralog C; XRCC3, X-ray repair cross complementing 3; POLE, DNA polymerase epsilon (catalytic subunit) and RNF168, ring finger protein 168.
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Image Search Results


Key domains and interaction regions of PALB2 protein and the P-T1 and P-T2 variants. ( A ) Domains and interaction regions of the PALB2 protein. The upper circles show the molecular surface representation of the Coiled–coil PALB2 (orange) dimerization, coil–coil PALB2-BRCA1 (green) interaction, PALB2-MRG15 (yellow) interaction, and PALB2-BRCA2 (cyan) interaction. The lower circles show the intrinsically disordered structure of the N-terminal (AlphaFold 2 prediction) and the β-sheet structure of the WD40 domain at the C-terminal. Ab1 and Ab2 represent the antigenic regions recognized by the PA5-48258 and BS-0588R PALB2 antibodies, respectively. ( B , C ) Diagram of the domains and interaction regions of PALB2 variants P-T1 and P-T2, respectively. CC, coil–coil motif; ChAM, chromatin association motif; FX, FXLP motif; NLS, nuclear export signal; BRCA1, BRCA1 DNA repair-associated; KEAP1, Kelch-like ECH-associated protein 1; RAD51, RAD51 recombinase; MRG15, MORF-related gene 15; BRCA2, BRCA2 DNA repair-associated; RAD51C, RAD51 paralog C; XRCC3, X-ray repair cross complementing 3; POLE, DNA polymerase epsilon (catalytic subunit) and RNF168, ring finger protein 168.

Journal: Biomedicines

Article Title: Functional Disruption of IQGAP1 by Truncated PALB2 in Two Cases of Breast Cancer: Implications for Proliferation and Invasion

doi: 10.3390/biomedicines13081804

Figure Lengend Snippet: Key domains and interaction regions of PALB2 protein and the P-T1 and P-T2 variants. ( A ) Domains and interaction regions of the PALB2 protein. The upper circles show the molecular surface representation of the Coiled–coil PALB2 (orange) dimerization, coil–coil PALB2-BRCA1 (green) interaction, PALB2-MRG15 (yellow) interaction, and PALB2-BRCA2 (cyan) interaction. The lower circles show the intrinsically disordered structure of the N-terminal (AlphaFold 2 prediction) and the β-sheet structure of the WD40 domain at the C-terminal. Ab1 and Ab2 represent the antigenic regions recognized by the PA5-48258 and BS-0588R PALB2 antibodies, respectively. ( B , C ) Diagram of the domains and interaction regions of PALB2 variants P-T1 and P-T2, respectively. CC, coil–coil motif; ChAM, chromatin association motif; FX, FXLP motif; NLS, nuclear export signal; BRCA1, BRCA1 DNA repair-associated; KEAP1, Kelch-like ECH-associated protein 1; RAD51, RAD51 recombinase; MRG15, MORF-related gene 15; BRCA2, BRCA2 DNA repair-associated; RAD51C, RAD51 paralog C; XRCC3, X-ray repair cross complementing 3; POLE, DNA polymerase epsilon (catalytic subunit) and RNF168, ring finger protein 168.

Article Snippet: PALB2 (C-ter) , , Rabbit polyclonal , , 1:200 , Bioss 2 , BS-0588R.

Techniques:

PALB2 full-length protein. Western blot of isolated proteins from HeLa cells and from circulating white cells from control IDC and cases with truncated variants of PALB2, P-T1, and P-T2 probed with PALB2 C-terminus antibody.

Journal: Biomedicines

Article Title: Functional Disruption of IQGAP1 by Truncated PALB2 in Two Cases of Breast Cancer: Implications for Proliferation and Invasion

doi: 10.3390/biomedicines13081804

Figure Lengend Snippet: PALB2 full-length protein. Western blot of isolated proteins from HeLa cells and from circulating white cells from control IDC and cases with truncated variants of PALB2, P-T1, and P-T2 probed with PALB2 C-terminus antibody.

Article Snippet: PALB2 (C-ter) , , Rabbit polyclonal , , 1:200 , Bioss 2 , BS-0588R.

Techniques: Western Blot, Isolation, Control

PALB2 (green) and IQGAP1 (red) expression in breast cancer control (CC1 and in CC2) mutated breast cancer (P-T1) labeled with antibodies binding to N-terminal or C-terminal domains. In CC2, PALB2-specific fluorescence at high intensity in cytosol and to a lesser extent in the nuclei of tumor cells (white arrowheads); IQGAP1-specific immunofluorescence in the plasma membrane and cytosol of most cells (yellow arrows) at two different intensities, high and medium level, in a dot-like pattern distribution; in the PALB2-IQGAP1 merged image, these two levels are more evident, and colocalization exists to a certain extent. B-T1 anti-PALB2-N-terminus antibody immunofluorescence signal present in both cytosol (high) and nucleus (medium and homogeneous); IQGAP1-specific immunofluorescence is displayed at a homogeneous medium intensity level in the plasma and cytosol of most cells. C-terminus anti-PALB2 antibody in CC1 samples exhibited similar immunolabeling to the N-terminus (white arrowheads). The IQGAP1 localization pattern of two intensity levels and localization is also shown in the first lane of the images. B-T1 and C-terminus anti-PALB2 antibody fluorescence at medium–high intensity, mainly in cytosol and at much lower intensity in the nuclei of cancer cells (white arrowheads). IQGAP-specific immunofluorescence at medium- to high-level intensity in cytosol and plasma membrane, frequently colocalizing (merged) in some tumor areas (yellow arrows). Scale bar = 40 µm.

Journal: Biomedicines

Article Title: Functional Disruption of IQGAP1 by Truncated PALB2 in Two Cases of Breast Cancer: Implications for Proliferation and Invasion

doi: 10.3390/biomedicines13081804

Figure Lengend Snippet: PALB2 (green) and IQGAP1 (red) expression in breast cancer control (CC1 and in CC2) mutated breast cancer (P-T1) labeled with antibodies binding to N-terminal or C-terminal domains. In CC2, PALB2-specific fluorescence at high intensity in cytosol and to a lesser extent in the nuclei of tumor cells (white arrowheads); IQGAP1-specific immunofluorescence in the plasma membrane and cytosol of most cells (yellow arrows) at two different intensities, high and medium level, in a dot-like pattern distribution; in the PALB2-IQGAP1 merged image, these two levels are more evident, and colocalization exists to a certain extent. B-T1 anti-PALB2-N-terminus antibody immunofluorescence signal present in both cytosol (high) and nucleus (medium and homogeneous); IQGAP1-specific immunofluorescence is displayed at a homogeneous medium intensity level in the plasma and cytosol of most cells. C-terminus anti-PALB2 antibody in CC1 samples exhibited similar immunolabeling to the N-terminus (white arrowheads). The IQGAP1 localization pattern of two intensity levels and localization is also shown in the first lane of the images. B-T1 and C-terminus anti-PALB2 antibody fluorescence at medium–high intensity, mainly in cytosol and at much lower intensity in the nuclei of cancer cells (white arrowheads). IQGAP-specific immunofluorescence at medium- to high-level intensity in cytosol and plasma membrane, frequently colocalizing (merged) in some tumor areas (yellow arrows). Scale bar = 40 µm.

Article Snippet: PALB2 (C-ter) , , Rabbit polyclonal , , 1:200 , Bioss 2 , BS-0588R.

Techniques: Expressing, Control, Labeling, Binding Assay, Fluorescence, Immunofluorescence, Clinical Proteomics, Membrane, Immunolabeling

Diagrams of PALB2 and IQGAP1 expression in truncated PALB2 human breast invasive ductal carcinoma. AU—arbitrary units. ( A ) Specific PALB2 expression in nucleus or cytosol in control (CC) IDC and in truncated PALB2 (P-T) IDC samples probed with antibodies against N- or C-terminus of PALB2 protein (* p < 0.05). ( B ) IQGAP1 total expression and peri-plasma membrane expression ( p < 0.05). ( C ) In subpopulations of cells (25–30% of total cells), correlation between the expression of IQGAP1 and PCNA evidenced that high expression of PCNA corresponded to lower expression of IQGAP1, which was higher in truncated PALB2 cases ( p < 0.05). ( D ) Correlation of IQGAP1/CK7 expression-level quotients in control and in PALB2-truncated cases. The correlation is lower in PALB2-truncated cases ( p > 0.05). In ( C , D ), point clouds are not represented to improve the clarity of the plots. ( E ) The Pearson correlation coefficient (PCC) was calculated for each sample to quantify the degree of colocalization between fluorophores.

Journal: Biomedicines

Article Title: Functional Disruption of IQGAP1 by Truncated PALB2 in Two Cases of Breast Cancer: Implications for Proliferation and Invasion

doi: 10.3390/biomedicines13081804

Figure Lengend Snippet: Diagrams of PALB2 and IQGAP1 expression in truncated PALB2 human breast invasive ductal carcinoma. AU—arbitrary units. ( A ) Specific PALB2 expression in nucleus or cytosol in control (CC) IDC and in truncated PALB2 (P-T) IDC samples probed with antibodies against N- or C-terminus of PALB2 protein (* p < 0.05). ( B ) IQGAP1 total expression and peri-plasma membrane expression ( p < 0.05). ( C ) In subpopulations of cells (25–30% of total cells), correlation between the expression of IQGAP1 and PCNA evidenced that high expression of PCNA corresponded to lower expression of IQGAP1, which was higher in truncated PALB2 cases ( p < 0.05). ( D ) Correlation of IQGAP1/CK7 expression-level quotients in control and in PALB2-truncated cases. The correlation is lower in PALB2-truncated cases ( p > 0.05). In ( C , D ), point clouds are not represented to improve the clarity of the plots. ( E ) The Pearson correlation coefficient (PCC) was calculated for each sample to quantify the degree of colocalization between fluorophores.

Article Snippet: PALB2 (C-ter) , , Rabbit polyclonal , , 1:200 , Bioss 2 , BS-0588R.

Techniques: Expressing, Control, Clinical Proteomics, Membrane

Validation of the expression of 6 hub genes in CRC and AS by molecular biology experiments. (A-F) RT-qPCR validation of the differential expression of prognostic genes between normal and tumor tissues in CRC patients. (G) Western blot validation of the differential expression of 2 newly identified genes (HMMR and PALB2) between normal and tumor tissues in CRC. (H) Quantitative analysis of the relative grayscale values of Western blot bands for the 2 newly identified genes (HMMR and PALB2) in normal and tumor tissues of CRC. Data are presented as mean ± standard deviation (SD), with statistical significance indicated as * p < 0.05, *** p < 0.001, and **** p < 0.0001. ns indicates no statistical significance.

Journal: Frontiers in Oncology

Article Title: Prognostic value and experimental validation of atherosclerosis-derived pathogenic genes in colorectal cancer

doi: 10.3389/fonc.2025.1728087

Figure Lengend Snippet: Validation of the expression of 6 hub genes in CRC and AS by molecular biology experiments. (A-F) RT-qPCR validation of the differential expression of prognostic genes between normal and tumor tissues in CRC patients. (G) Western blot validation of the differential expression of 2 newly identified genes (HMMR and PALB2) between normal and tumor tissues in CRC. (H) Quantitative analysis of the relative grayscale values of Western blot bands for the 2 newly identified genes (HMMR and PALB2) in normal and tumor tissues of CRC. Data are presented as mean ± standard deviation (SD), with statistical significance indicated as * p < 0.05, *** p < 0.001, and **** p < 0.0001. ns indicates no statistical significance.

Article Snippet: After blocking non-specific binding sites with 5% BSA at 37°C for 1 h, primary antibodies [HMMR (15820-1-AP, Proteintech), PALB2 (14340-1-AP, Proteintech), and PRR11 (BD-PE4086, Biodragon)], all diluted at 1:50, were applied and incubated overnight at 4°C.

Techniques: Biomarker Discovery, Expressing, Quantitative RT-PCR, Quantitative Proteomics, Western Blot, Standard Deviation

IHC staining validation. (A) The differential expression of PALB2 and HMMR in CRC tissues compared with normal tissues; (B) displays the differential expression of HMMR , PALB2 and PRR11 in AS tissues versus normal tissues. * p < 0.05.

Journal: Frontiers in Oncology

Article Title: Prognostic value and experimental validation of atherosclerosis-derived pathogenic genes in colorectal cancer

doi: 10.3389/fonc.2025.1728087

Figure Lengend Snippet: IHC staining validation. (A) The differential expression of PALB2 and HMMR in CRC tissues compared with normal tissues; (B) displays the differential expression of HMMR , PALB2 and PRR11 in AS tissues versus normal tissues. * p < 0.05.

Article Snippet: After blocking non-specific binding sites with 5% BSA at 37°C for 1 h, primary antibodies [HMMR (15820-1-AP, Proteintech), PALB2 (14340-1-AP, Proteintech), and PRR11 (BD-PE4086, Biodragon)], all diluted at 1:50, were applied and incubated overnight at 4°C.

Techniques: Immunohistochemistry, Biomarker Discovery, Quantitative Proteomics

( A ) Sanger sequencing confirmation of Mettl14 arginine methylation deficient mouse model. In total, 13 arginine resides located at the C-terminal disordered region of Mettl14 were mutated to lysine residues. ( B ) The arginine methylation levels of Mettl14 in WT, heterozygous (WT/RK), and homozygous (RK/RK) mice were detected by IP-western blot using tissue lysates from mouse spleen and thymus. ( C ) The protein expression levels of several DNA repair genes, including BRCA1, ATRIP, and PALB2, were detected by western blot using Thymus tissues from WT, WT/RK, and RK/RK mice. ( D ) Mettl14 arginine methylation deficiency increases the population of primitive hematopoietic cells (LK cells). ** P = 0.0019. ( E ) Mettl14 arginine methylation deficiency increases the population of myeloid (Mac1 + Gr1 + ) cells in the BM, but not in the spleen. * P = 0.013. ( F ) Mettl14 arginine methylation deficiency decreases the B lymphoid (B220 + ) population in the BM, but not in the spleen. * P = 0.011. ( G ) Mettl14 arginine methylation deficiency decreases the T lymphoid (CD3 + ) population in the BM, but not in the spleen. Data from three independent replicates were analyzed by Student’s t test and shown as mean ± SD. ** P = 0.0097. .

Journal: EMBO Reports

Article Title: Arginine methylation-dependent METTL14-SMN interaction regulates RNA m 6 A homeostasis

doi: 10.1038/s44319-025-00590-7

Figure Lengend Snippet: ( A ) Sanger sequencing confirmation of Mettl14 arginine methylation deficient mouse model. In total, 13 arginine resides located at the C-terminal disordered region of Mettl14 were mutated to lysine residues. ( B ) The arginine methylation levels of Mettl14 in WT, heterozygous (WT/RK), and homozygous (RK/RK) mice were detected by IP-western blot using tissue lysates from mouse spleen and thymus. ( C ) The protein expression levels of several DNA repair genes, including BRCA1, ATRIP, and PALB2, were detected by western blot using Thymus tissues from WT, WT/RK, and RK/RK mice. ( D ) Mettl14 arginine methylation deficiency increases the population of primitive hematopoietic cells (LK cells). ** P = 0.0019. ( E ) Mettl14 arginine methylation deficiency increases the population of myeloid (Mac1 + Gr1 + ) cells in the BM, but not in the spleen. * P = 0.013. ( F ) Mettl14 arginine methylation deficiency decreases the B lymphoid (B220 + ) population in the BM, but not in the spleen. * P = 0.011. ( G ) Mettl14 arginine methylation deficiency decreases the T lymphoid (CD3 + ) population in the BM, but not in the spleen. Data from three independent replicates were analyzed by Student’s t test and shown as mean ± SD. ** P = 0.0097. .

Article Snippet: Rabbit anti-PALB2 antibody , Proteintech , 14340-1-AP.

Techniques: Sequencing, Methylation, Western Blot, Expressing

Key domains and interaction regions of PALB2 protein and the P-T1 and P-T2 variants. ( A ) Domains and interaction regions of the PALB2 protein. The upper circles show the molecular surface representation of the Coiled–coil PALB2 (orange) dimerization, coil–coil PALB2-BRCA1 (green) interaction, PALB2-MRG15 (yellow) interaction, and PALB2-BRCA2 (cyan) interaction. The lower circles show the intrinsically disordered structure of the N-terminal (AlphaFold 2 prediction) and the β-sheet structure of the WD40 domain at the C-terminal. Ab1 and Ab2 represent the antigenic regions recognized by the PA5-48258 and BS-0588R PALB2 antibodies, respectively. ( B , C ) Diagram of the domains and interaction regions of PALB2 variants P-T1 and P-T2, respectively. CC, coil–coil motif; ChAM, chromatin association motif; FX, FXLP motif; NLS, nuclear export signal; BRCA1, BRCA1 DNA repair-associated; KEAP1, Kelch-like ECH-associated protein 1; RAD51, RAD51 recombinase; MRG15, MORF-related gene 15; BRCA2, BRCA2 DNA repair-associated; RAD51C, RAD51 paralog C; XRCC3, X-ray repair cross complementing 3; POLE, DNA polymerase epsilon (catalytic subunit) and RNF168, ring finger protein 168.

Journal: Biomedicines

Article Title: Functional Disruption of IQGAP1 by Truncated PALB2 in Two Cases of Breast Cancer: Implications for Proliferation and Invasion

doi: 10.3390/biomedicines13081804

Figure Lengend Snippet: Key domains and interaction regions of PALB2 protein and the P-T1 and P-T2 variants. ( A ) Domains and interaction regions of the PALB2 protein. The upper circles show the molecular surface representation of the Coiled–coil PALB2 (orange) dimerization, coil–coil PALB2-BRCA1 (green) interaction, PALB2-MRG15 (yellow) interaction, and PALB2-BRCA2 (cyan) interaction. The lower circles show the intrinsically disordered structure of the N-terminal (AlphaFold 2 prediction) and the β-sheet structure of the WD40 domain at the C-terminal. Ab1 and Ab2 represent the antigenic regions recognized by the PA5-48258 and BS-0588R PALB2 antibodies, respectively. ( B , C ) Diagram of the domains and interaction regions of PALB2 variants P-T1 and P-T2, respectively. CC, coil–coil motif; ChAM, chromatin association motif; FX, FXLP motif; NLS, nuclear export signal; BRCA1, BRCA1 DNA repair-associated; KEAP1, Kelch-like ECH-associated protein 1; RAD51, RAD51 recombinase; MRG15, MORF-related gene 15; BRCA2, BRCA2 DNA repair-associated; RAD51C, RAD51 paralog C; XRCC3, X-ray repair cross complementing 3; POLE, DNA polymerase epsilon (catalytic subunit) and RNF168, ring finger protein 168.

Article Snippet: Membranes were blocked in PBS/5% BSA for 1 h. Protein detection was performed using PALB2 (C-terminus) antibody (1:1000, Cat.# BS-0588R, Bioss, Woburn, MA, USA) and anti-rabbit Ig horseradish peroxidase-conjugated secondary antibody (Cat. # NA9340, Cytiva, Marlborough, MA, USA).

Techniques: