human small cell lung carcinoma line nci h1930  (ATCC)

Journal: Biochemistry and Biophysics Reports

Article Title: Integrated transcriptomic and proteomic validation identifies SLC35D3 as a tumor-selective surface antigen for colorectal and neuroendocrine carcinomas

doi: 10.1016/j.bbrep.2026.102587

Figure Lengend Snippet: Immunohistochemical analysis of SLC35D3 expression in human tumors, normal tissues, and positive-control samples. (A) SLC35D3 staining in human tumors: (a) primary colon tumor; (b) corresponding lymph-node metastasis; (c) normal adjacent tissue (NAT) of a; (d) primary rectal tumor; (e) corresponding lymph-node metastasis; (f) NAT of d; (g–h) small-cell lung carcinoma (SCLC); (i) pancreatic neuroendocrine neoplasm; (j) pancreatic islet tumor. (B) SLC35D3 staining in human normal tissues: (a) cerebrum; (b) bone marrow; (c) lung; (d) heart; (e) liver; (f) kidney; (g) eye; (h) colon; (i) adrenal gland; (j) pancreas; (k) hypophysis; (l) stomach; (m) small intestine; (n) prostate. Arrowheads indicate SLC35D3-positive cells. (C) SLC35D3 staining of negative and positive control cell lines: (a) HCT 116-mock (negative control); (b) HCT 116-hSLC35D3 (engineered overexpression); (c) NCI–H1930 (endogenously SLC35D3-expressing).

Article Snippet: The human pancreatic islet cell carcinoma line QGP-1 (Japanese Collection of Research Bioresources Cell Bank, Osaka, Japan; Cat. No. JCRB0183), human small-cell lung carcinoma line NCI–H1930 (American Type Culture Collection (ATCC), Manassas, VA, USA; Cat. No. CRL-5906), human colorectal carcinoma line LoVo (ATCC; Cat. No. CCL-229), human gastric carcinoma line SNU-16 (ATCC; Cat. No. CRL-5974), and human colorectal carcinoma line HCT 116 (ATCC; Cat. No. CCL-247) were used.

Techniques: Immunohistochemical staining, Expressing, Positive Control, Staining, Negative Control, Over Expression

Journal: Biochemistry and Biophysics Reports

Article Title: Integrated transcriptomic and proteomic validation identifies SLC35D3 as a tumor-selective surface antigen for colorectal and neuroendocrine carcinomas

doi: 10.1016/j.bbrep.2026.102587

Figure Lengend Snippet: Validation of cell-surface SLC35D3 expression in cancer cell lines by flow cytometry and comparison with CCLE transcriptomic data. Flow cytometry histograms of cell-surface SLC35D3 staining in human cancer cell lines (HCT 116, LoVo, QGP-1, NCI–H1930, and SNU-16). For each cell line, the MFI ratio (anti-SLC35D3/isotype) and the corresponding mRNA expression level (log2[TPM+1]) from the CCLE are indicated below the histogram. HCT 116 served as a negative control and showed minimal surface staining, consistent with a CCLE value of log2[TPM+1] = 0.0.

Article Snippet: The human pancreatic islet cell carcinoma line QGP-1 (Japanese Collection of Research Bioresources Cell Bank, Osaka, Japan; Cat. No. JCRB0183), human small-cell lung carcinoma line NCI–H1930 (American Type Culture Collection (ATCC), Manassas, VA, USA; Cat. No. CRL-5906), human colorectal carcinoma line LoVo (ATCC; Cat. No. CCL-229), human gastric carcinoma line SNU-16 (ATCC; Cat. No. CRL-5974), and human colorectal carcinoma line HCT 116 (ATCC; Cat. No. CCL-247) were used.

Techniques: Biomarker Discovery, Expressing, Flow Cytometry, Comparison, Staining, Negative Control

Journal: bioRxiv

Article Title: HIPK2-and IKKβ-dependent phosphorylation stabilizes TAp63α during the oocyte DNA damage response

doi: 10.64898/2026.04.17.719163

Figure Lengend Snippet: (A) Schematic overview of the experimental workflow used to identify TAp63α-interacting proteins from ovarian tissue. (B) Western blot analysis confirming successful immunoprecipitation of endogenous TAp63α from goat ovary lysates. (C) STRING network analysis of proteins identified by mass spectrometry, highlighting predicted interactions between TAp63α and the kinases HIPK2 and IKKβ. (D) Western blot analysis of ovarian lysates from mice of different ages showing that HIPK2 and TAp63α protein levels decrease with age, whereas IKKβ levels remain relatively constant. Two pairs of ovaries were pooled per sample. (E) Co-immunoprecipitation of endogenous TAp63α from mouse ovaries (eight pairs pooled per sample), followed by immunoblot detection of TAp63α and associated IKKβ. (F) Schematic representation of the experimental workflow used for interaction validation in a cell-based system. (G) Co-immunoprecipitation analysis in H1299 cells transiently expressing TAp63α, confirming interaction with HIPK2 and IKKβ. Whole-cell extracts and immunoprecipitates were probed with antibodies against TAp63α, HIPK2, and IKKβ. Due to differences in protein abundance and detection sensitivity, blots were processed and exposed separately to ensure optimal signal detection.

Article Snippet: The human lung adenocarcinoma cell line H1299 (ATCC - CRL-5803) was obtained from ATCC and cultured in RPMI 1640 medium (Cat no. 11875085, Gibco) supplemented with 10% fetal bovine serum (FBS) (Cat no. 10270106, Gibco) and 1× penicillin-streptomycin (Cat no. P4333, Sigma) at 37°C in a humidified incubator with 5% CO2.

Techniques: Western Blot, Immunoprecipitation, Mass Spectrometry, Biomarker Discovery, Expressing, Quantitative Proteomics

Journal: bioRxiv

Article Title: HIPK2-and IKKβ-dependent phosphorylation stabilizes TAp63α during the oocyte DNA damage response

doi: 10.64898/2026.04.17.719163

Figure Lengend Snippet: (A) Schematic overview of the experimental approach used to assess kinase-dependent regulation of TAp63α following DNA damage. (B) Western blot analysis showing a phosphorylation-dependent mobility shift of TAp63α upon doxorubicin treatment. This shift is reduced by CHK2 and CK1 inhibition and is further diminished following calf intestinal phosphatase (CIP) treatment, confirming phosphorylation-dependent modification. (C) Inhibition of HIPK2 or IKKβ, individually or in combination, reduces TAp63α phosphorylation and is associated with decreased protein stability. In contrast, inhibition of CHK2 or CK1 reduces phosphorylation without affecting total TAp63α levels. (D) Schematic representation of the siRNA-mediated knockdown strategy in stable TAp63α-expressing H1299 cells. (E) Knockdown of HIPK2 or IKKβ reduces the phosphorylation-associated mobility shift of TAp63α compared to control and scrambled siRNA conditions. Immunoblotting with phospho-serine/threonine antibodies further confirms a reduction in overall phosphorylation levels upon kinase depletion. (F) Western blot analysis of TAp63α following inhibition of CHK2, HIPK2, and IKKβ under DNA damage conditions. CHK2 inhibition reduces the phosphorylation-associated mobility shift of TAp63α. Inhibition of HIPK2 and IKKβ decreases total TAp63α protein stability. Co-inhibition of CHK2 with HIPK2 and IKKβ restores TAp63α protein levels when applied prior to or concurrently, but not when CHK2 inhibition is applied after HIPK2 and IKKβ inhibition. (G) Schematic representation of the in vivo experimental workflow. (H) Western blot analysis of mouse ovarian lysates showing that cisplatin induces a phosphorylation-associated mobility shift of TAp63α. Co-treatment with HIPK2 or IKKβ inhibitors reduces both phosphorylation and total TAp63α levels. Five pairs of ovaries were pooled per sample. (I) Schematic overview of the experimental approach used for oocyte analysis. (J–K) Representative images showing distinct patterns of TAp63α nuclear distribution in oocytes, along with their quantification. Treatment with HIPK2 or IKKβ inhibitors under DNA damage conditions results in a shift toward reduced nuclear signal intensity. Statistical significance for Class III follicles: doxorubicin + HIPK2 inhibitor (P = 0.0001) and doxorubicin + IKKβ inhibitor (P = 0.0001) compared to doxorubicin alone. Data are presented as mean ± SD; unpaired t-test.

Article Snippet: The human lung adenocarcinoma cell line H1299 (ATCC - CRL-5803) was obtained from ATCC and cultured in RPMI 1640 medium (Cat no. 11875085, Gibco) supplemented with 10% fetal bovine serum (FBS) (Cat no. 10270106, Gibco) and 1× penicillin-streptomycin (Cat no. P4333, Sigma) at 37°C in a humidified incubator with 5% CO2.

Techniques: Western Blot, Phospho-proteomics, Mobility Shift, Inhibition, Modification, Knockdown, Expressing, Control, In Vivo