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Proteintech polyclonal antibody to ctsh

Figure 1 Effect of T3 on the amount of cysteine proteases and <t>CTSH</t> mRNA and protein in HepG2-TR cell lines. HepG2 cell lines that consistently express wild-type TRa1 (HepG2-TRa1#1, #2) and TRb1 (HepG2-TRb1) were used. As a control, HepG2 cells were transfected with the empty vector, yielding a cell line expressing the Neo protein (HepG2-Neo cells). (a) The CTSH mRNA expression level in four TR stable lines. HepG2-TRa1 or b1 cell lines were incubated for 24–72 h in the absence or presence of T3, after which total RNA was isolated and subjected (20 mg per lane) to Northern blot analysis with 32P-labeled CTSH and 18S RNA probes. Positions of the 1.5-kb CTSH and 18S RNAs are indicated. Student’s t-test. **Po0.01; *Po0.05, T3-depleted (Td) vs 1 or 10 nM T3 treated. (b) Three TR stable lines and Neo cells were incubated in Td medium in the absence or presence of T3 for 24–72 h, after which cell lysates (20 mg protein) were subjected to immunoblot analysis with antibodies to CTSH. The pro-form (upper arrow) and active form (lower arrow) of CTSH band is shown. Actin was used as an internal control. (c) Quantitative real-time PCR analysis of CTSH mRNA in Huh7 cells after 1–10 nM T3 for 24–48 h treatment. (d) Western blot analysis of total cell lysates or extracellular forms of CTSH in Huh7 cells. Huh7 cells were incubated in serum-free medium and 1–10 nM T3 for 24 and 48 h on 10 cm dishes. The culture medium was collected and 20 mg of media were subjected to immunoblot analysis with CTSH antibodies and loading control by using coomassie blue stained. Data are means±s.e. of values from three independent experiments.

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1) Product Images from "Cathepsin H regulated by the thyroid hormone receptors associate with tumor invasion in human hepatoma cells."

Article Title: Cathepsin H regulated by the thyroid hormone receptors associate with tumor invasion in human hepatoma cells.

Journal: Oncogene

doi: 10.1038/onc.2010.585

Figure 1 Effect of T3 on the amount of cysteine proteases and CTSH mRNA and protein in HepG2-TR cell lines. HepG2 cell lines that consistently express wild-type TRa1 (HepG2-TRa1#1, #2) and TRb1 (HepG2-TRb1) were used. As a control, HepG2 cells were transfected with the empty vector, yielding a cell line expressing the Neo protein (HepG2-Neo cells). (a) The CTSH mRNA expression level in four TR stable lines. HepG2-TRa1 or b1 cell lines were incubated for 24–72 h in the absence or presence of T3, after which total RNA was isolated and subjected (20 mg per lane) to Northern blot analysis with 32P-labeled CTSH and 18S RNA probes. Positions of the 1.5-kb CTSH and 18S RNAs are indicated. Student’s t-test. **Po0.01; *Po0.05, T3-depleted (Td) vs 1 or 10 nM T3 treated. (b) Three TR stable lines and Neo cells were incubated in Td medium in the absence or presence of T3 for 24–72 h, after which cell lysates (20 mg protein) were subjected to immunoblot analysis with antibodies to CTSH. The pro-form (upper arrow) and active form (lower arrow) of CTSH band is shown. Actin was used as an internal control. (c) Quantitative real-time PCR analysis of CTSH mRNA in Huh7 cells after 1–10 nM T3 for 24–48 h treatment. (d) Western blot analysis of total cell lysates or extracellular forms of CTSH in Huh7 cells. Huh7 cells were incubated in serum-free medium and 1–10 nM T3 for 24 and 48 h on 10 cm dishes. The culture medium was collected and 20 mg of media were subjected to immunoblot analysis with CTSH antibodies and loading control by using coomassie blue stained. Data are means±s.e. of values from three independent experiments.

Figure Legend Snippet: Figure 1 Effect of T3 on the amount of cysteine proteases and CTSH mRNA and protein in HepG2-TR cell lines. HepG2 cell lines that consistently express wild-type TRa1 (HepG2-TRa1#1, #2) and TRb1 (HepG2-TRb1) were used. As a control, HepG2 cells were transfected with the empty vector, yielding a cell line expressing the Neo protein (HepG2-Neo cells). (a) The CTSH mRNA expression level in four TR stable lines. HepG2-TRa1 or b1 cell lines were incubated for 24–72 h in the absence or presence of T3, after which total RNA was isolated and subjected (20 mg per lane) to Northern blot analysis with 32P-labeled CTSH and 18S RNA probes. Positions of the 1.5-kb CTSH and 18S RNAs are indicated. Student’s t-test. **Po0.01; *Po0.05, T3-depleted (Td) vs 1 or 10 nM T3 treated. (b) Three TR stable lines and Neo cells were incubated in Td medium in the absence or presence of T3 for 24–72 h, after which cell lysates (20 mg protein) were subjected to immunoblot analysis with antibodies to CTSH. The pro-form (upper arrow) and active form (lower arrow) of CTSH band is shown. Actin was used as an internal control. (c) Quantitative real-time PCR analysis of CTSH mRNA in Huh7 cells after 1–10 nM T3 for 24–48 h treatment. (d) Western blot analysis of total cell lysates or extracellular forms of CTSH in Huh7 cells. Huh7 cells were incubated in serum-free medium and 1–10 nM T3 for 24 and 48 h on 10 cm dishes. The culture medium was collected and 20 mg of media were subjected to immunoblot analysis with CTSH antibodies and loading control by using coomassie blue stained. Data are means±s.e. of values from three independent experiments.

Techniques Used: Control, Transfection, Plasmid Preparation, Expressing, Incubation, Isolation, Northern Blot, Labeling, Western Blot, Real-time Polymerase Chain Reaction, Staining

Figure 2 Regulation of CTSH expression by T3 at the transcriptional level. (a) Schematic representation of CTSH promoter with potential TRE-binding sites indicated by oval shapes. The numbers beside each construct indicate the base pair at which the site starts based on the transcription start site ( þ 1). A series of pA3TK-luc reporter constructs containing progressively smaller amounts of CTSH 50-ﬂanking DNA (1 mg per well) were co-transfected with pcDNA-TRa1#1 in HepG2 cells. After transfection, cells were harvested after T3 treatment for 24 h. Data were normalized to co-transfected b-galactosidase, and fold-activation was calculated relative to each pA3TK-luc control. Results are presented as means s.d. of data from three independent experiments performed in triplicate. (b) In vitro-translated TRa1 or TRb1 incubated with wild-type or mutated TRE of CTSH gene promoter 2038 to 1966 along with TNT in vitro-translated RXRa in a ﬁnal volume of 20 ml. Antibody C4 is a mouse monoclonal antibody against TR proteins, and MOPC21 is a nonspeciﬁc monoclonal antibody. The position of probe complexed with TR and RXR is indicated by the arrows. SS: TR complexes supershifted by C4 or RXRa antibody. The wild-type or mutated TRE of CTSH gene promoter 1565 to 1501 were ampliﬁed and labeled with [a-32P-dCTP] as probe.

Figure Legend Snippet: Figure 2 Regulation of CTSH expression by T3 at the transcriptional level. (a) Schematic representation of CTSH promoter with potential TRE-binding sites indicated by oval shapes. The numbers beside each construct indicate the base pair at which the site starts based on the transcription start site ( þ 1). A series of pA3TK-luc reporter constructs containing progressively smaller amounts of CTSH 50-ﬂanking DNA (1 mg per well) were co-transfected with pcDNA-TRa1#1 in HepG2 cells. After transfection, cells were harvested after T3 treatment for 24 h. Data were normalized to co-transfected b-galactosidase, and fold-activation was calculated relative to each pA3TK-luc control. Results are presented as means s.d. of data from three independent experiments performed in triplicate. (b) In vitro-translated TRa1 or TRb1 incubated with wild-type or mutated TRE of CTSH gene promoter 2038 to 1966 along with TNT in vitro-translated RXRa in a ﬁnal volume of 20 ml. Antibody C4 is a mouse monoclonal antibody against TR proteins, and MOPC21 is a nonspeciﬁc monoclonal antibody. The position of probe complexed with TR and RXR is indicated by the arrows. SS: TR complexes supershifted by C4 or RXRa antibody. The wild-type or mutated TRE of CTSH gene promoter 1565 to 1501 were ampliﬁed and labeled with [a-32P-dCTP] as probe.

Techniques Used: Expressing, Binding Assay, Construct, Transfection, Activation Assay, Control, In Vitro, Incubation, Labeling

Figure 3 Identiﬁcation of the TR proteins that are associated with the TRE regions of CTSH gene promoter in vivo. (a) Nuclear extracts (NE) were isolated from HepG2-TRa#1 cells, and 5 mg of protein were incubated with [a-32P-dCTP] labeled probes men- tioned in Figure 2. A upstream region 2264 to 2054 in the CTSH promoter gene devoid of the TRE region was a nonspeciﬁc (ns) probe. (b) ChIP assay as described in Materials and methods section. DNA corresponding to TRE of CTSH promoter region was analyzed by PCR with the indicated primers. Furin or glyceraldehyde 3-phosphate dehydrogenase (GAPDH) promoter region was used as a positive or negative control, respectively. Another positive control was used chromatin before immunopre- cipitation (input) and negative controls were immunoprecipitates with MOPC21 antibody. ChIP assays were also performed in HepG2-TRa or b cells.

Figure Legend Snippet: Figure 3 Identiﬁcation of the TR proteins that are associated with the TRE regions of CTSH gene promoter in vivo. (a) Nuclear extracts (NE) were isolated from HepG2-TRa#1 cells, and 5 mg of protein were incubated with [a-32P-dCTP] labeled probes men- tioned in Figure 2. A upstream region 2264 to 2054 in the CTSH promoter gene devoid of the TRE region was a nonspeciﬁc (ns) probe. (b) ChIP assay as described in Materials and methods section. DNA corresponding to TRE of CTSH promoter region was analyzed by PCR with the indicated primers. Furin or glyceraldehyde 3-phosphate dehydrogenase (GAPDH) promoter region was used as a positive or negative control, respectively. Another positive control was used chromatin before immunopre- cipitation (input) and negative controls were immunoprecipitates with MOPC21 antibody. ChIP assays were also performed in HepG2-TRa or b cells.

Techniques Used: In Vivo, Isolation, Incubation, Labeling, Negative Control, Positive Control

Figure 4 The CTSH was regulated by TR in thyroidectomized rats and human HCC specimens. (a) Induction of CTSH expression by thyroid hormone in rat liver. The protein expression of CTSH in normal (N, sham-operated), TX, or TX þ T3 male Sprague–Dawley rat liver was determined by western blot analysis. Student’s t-test. **Po0.01, TX þ T3 or N vs TX treated. (b) The mRNA expression of CTSH was determined by quantitative reverse transcription (Q-RT)–PCR. (c) TR and CTSH protein overexpression in 15 representative pairs of human HCC specimens. The band intensities were quantiﬁed and normalized to actin. The normalized tumor/ non-tumor (T/N) ratio is shown in the right panel.

Figure Legend Snippet: Figure 4 The CTSH was regulated by TR in thyroidectomized rats and human HCC specimens. (a) Induction of CTSH expression by thyroid hormone in rat liver. The protein expression of CTSH in normal (N, sham-operated), TX, or TX þ T3 male Sprague–Dawley rat liver was determined by western blot analysis. Student’s t-test. **Po0.01, TX þ T3 or N vs TX treated. (b) The mRNA expression of CTSH was determined by quantitative reverse transcription (Q-RT)–PCR. (c) TR and CTSH protein overexpression in 15 representative pairs of human HCC specimens. The band intensities were quantiﬁed and normalized to actin. The normalized tumor/ non-tumor (T/N) ratio is shown in the right panel.

Techniques Used: Expressing, Western Blot, Reverse Transcription, Reverse Transcription Polymerase Chain Reaction, Over Expression

Figure 5 Functional assay of CTSH in hepatoma cells. (a) Overexpression of CTSH promotes migration and invasion. In all, 20 mg of media were subjected to immunoblot analysis with CTSH antibodies. Bottom was shown as loading control using coomassie blue stained. Overexpression of CTSH increases (b) migration and (c) invasion. J7 cells stably expresses CTSH (CTSH#1, #2 clones) and J7 cells stably expresses control vector (control) migration over a time period of 24 h was quantiﬁed with a Transwell migration assay and an invasion assay through a Matrigel-coated membrane. The mean migration or invasion of J7-vector cells was assigned a value of 1. Student’s t test. **Po0.01; *Po0.05, CTSH#1, #2 or pool vs vector. (d) Two Huh7 CTSH knockdown (KD) stable lines (CTSH- KD#1, #2), one pool (CTSH-KD pool) stable cells and one Huh7 luciferase knockdown control cell line (KD-control) were used. Knockdown of CTSH in Huh7 cells was conﬁrmed by western blot in cell lysate or conditioned medium. Knockdown of CTSH reduces (e) migration and (f) invasion. Cell image was shown in the bottom of b, c, e and f.

Figure Legend Snippet: Figure 5 Functional assay of CTSH in hepatoma cells. (a) Overexpression of CTSH promotes migration and invasion. In all, 20 mg of media were subjected to immunoblot analysis with CTSH antibodies. Bottom was shown as loading control using coomassie blue stained. Overexpression of CTSH increases (b) migration and (c) invasion. J7 cells stably expresses CTSH (CTSH#1, #2 clones) and J7 cells stably expresses control vector (control) migration over a time period of 24 h was quantiﬁed with a Transwell migration assay and an invasion assay through a Matrigel-coated membrane. The mean migration or invasion of J7-vector cells was assigned a value of 1. Student’s t test. **Po0.01; *Po0.05, CTSH#1, #2 or pool vs vector. (d) Two Huh7 CTSH knockdown (KD) stable lines (CTSH- KD#1, #2), one pool (CTSH-KD pool) stable cells and one Huh7 luciferase knockdown control cell line (KD-control) were used. Knockdown of CTSH in Huh7 cells was conﬁrmed by western blot in cell lysate or conditioned medium. Knockdown of CTSH reduces (e) migration and (f) invasion. Cell image was shown in the bottom of b, c, e and f.

Techniques Used: Functional Assay, Over Expression, Migration, Western Blot, Control, Staining, Stable Transfection, Clone Assay, Plasmid Preparation, Transwell Migration Assay, Invasion Assay, Membrane, Knockdown, Luciferase

Figure 6 Mediated overexpression of CTSH by thyroid hormone promotes hepatocyte migration. (a) J7-control or J7-CSTH SCID mice (n ¼ 4 per group) were established. All analyses were carried out 7 weeks after inoculation of tumor cells. Immunohistochemical staining of metastasized J7-control or J7-CSTH cells in lung sections are displayed. The metastasis index (fold, density of tumor numbers in J7-CSTH or J7-control per cm2 area) in lung is shown in the lower panel. (b) Effect of T3-mediated migration activity in HepG2-TRa#1 and Huh7 cells, which knocked down CTSH expression. HepG2-TRa or Huh7 cells were transient transfected with either control (luc short hairpin RNA (shRNA)) or CTSH shRNA by electroporation. After puromycin selection, stable clones were pooled for migration assay. The cell lines were added to the upper chamber of Transwell units and incubated in the absence or presence of T3 (10 nM) for 24 h. The number of cells that transversed the ﬁlter to the lower chamber was then determined and expressed as the relative migration activity. (c) Effect of anti-green ﬂuorescent protein (GFP) or anti-CTSH antibody treatment on migration activity in HepG2-TRa#1 and Huh7 cells. The cell lines were added to the upper chamber of Transwell units and incubated in the absence or presence of T3 (10 nM) and anti-GFP or anti-CTSH antibody (10 mg/ml) for 24 h. (d) Two different control cell clones (J7-control#1 and J7-control#2) that stably express neo proteins and two J7-CTSH stable clones were used for MMP assays. J7-control or J7-CSTH cells (2 106) were plated in Dulbecco’s modiﬁed Eagle’s medium (DMEM) with 10% fetal bovine serum. After 24-h incubation and subsequent washing, the medium was replaced with serum-free medium. Medium was collected for MMP detection. Gelatin zymography was performed; the position of proenzyme and active form of MMPs is shown to the left. (e) HepG2-TRa#1 and J7- derived cells were treated in serum-free medium and were incubated in T3 (0, 1 and 10 nM) for 24 or 48 h. Medium was collected for western blot analysis of MMP3. (f) J7-control or J7-CSTH cells were cultured in serum-free medium for 24 h. Cell lysates were western blotted with anti-ERK and anti-phospho-ERK antibodies. Actin was used as an internal control. (g) HepG2-TRa#1 or Huh7 cells were stimulated to migrate T3 by in the presence or absence of indicated MEK inhibitors (U0126). The relative migration means that in response to T3 ( þ or – inhibitor) normalized to dimethylsulphoxide (DMSO) treated, T3-deprived controls. Data are means±s.e. of values from three independent experiments.

Figure Legend Snippet: Figure 6 Mediated overexpression of CTSH by thyroid hormone promotes hepatocyte migration. (a) J7-control or J7-CSTH SCID mice (n ¼ 4 per group) were established. All analyses were carried out 7 weeks after inoculation of tumor cells. Immunohistochemical staining of metastasized J7-control or J7-CSTH cells in lung sections are displayed. The metastasis index (fold, density of tumor numbers in J7-CSTH or J7-control per cm2 area) in lung is shown in the lower panel. (b) Effect of T3-mediated migration activity in HepG2-TRa#1 and Huh7 cells, which knocked down CTSH expression. HepG2-TRa or Huh7 cells were transient transfected with either control (luc short hairpin RNA (shRNA)) or CTSH shRNA by electroporation. After puromycin selection, stable clones were pooled for migration assay. The cell lines were added to the upper chamber of Transwell units and incubated in the absence or presence of T3 (10 nM) for 24 h. The number of cells that transversed the ﬁlter to the lower chamber was then determined and expressed as the relative migration activity. (c) Effect of anti-green ﬂuorescent protein (GFP) or anti-CTSH antibody treatment on migration activity in HepG2-TRa#1 and Huh7 cells. The cell lines were added to the upper chamber of Transwell units and incubated in the absence or presence of T3 (10 nM) and anti-GFP or anti-CTSH antibody (10 mg/ml) for 24 h. (d) Two different control cell clones (J7-control#1 and J7-control#2) that stably express neo proteins and two J7-CTSH stable clones were used for MMP assays. J7-control or J7-CSTH cells (2 106) were plated in Dulbecco’s modiﬁed Eagle’s medium (DMEM) with 10% fetal bovine serum. After 24-h incubation and subsequent washing, the medium was replaced with serum-free medium. Medium was collected for MMP detection. Gelatin zymography was performed; the position of proenzyme and active form of MMPs is shown to the left. (e) HepG2-TRa#1 and J7- derived cells were treated in serum-free medium and were incubated in T3 (0, 1 and 10 nM) for 24 or 48 h. Medium was collected for western blot analysis of MMP3. (f) J7-control or J7-CSTH cells were cultured in serum-free medium for 24 h. Cell lysates were western blotted with anti-ERK and anti-phospho-ERK antibodies. Actin was used as an internal control. (g) HepG2-TRa#1 or Huh7 cells were stimulated to migrate T3 by in the presence or absence of indicated MEK inhibitors (U0126). The relative migration means that in response to T3 ( þ or – inhibitor) normalized to dimethylsulphoxide (DMSO) treated, T3-deprived controls. Data are means±s.e. of values from three independent experiments.

Techniques Used: Over Expression, Migration, Control, Immunohistochemical staining, Staining, Activity Assay, Expressing, Transfection, shRNA, Electroporation, Selection, Clone Assay, Incubation, Stable Transfection, Zymography, Derivative Assay, Western Blot, Cell Culture

Incubation:

Article Title: Identification of Cathepsin H and Metabolic Traits as Potential Biomarkers for Lung Cancer by Mendelian Randomization and Single‐Cell Transcriptomics
Article Snippet: Equal protein amounts were subjected to SDS‐PAGE and transferred onto PVDF membranes (EMD Millipore Corp). .. Membranes were blocked with 5% BSA for 2 h at room temperature and incubated overnight at 4°C with the primary antibody against CTSH (Proteintech, 1:1000) and β‐actin (Proteintech, 1:1000). .. After washing three times with TBST, the membranes were incubated with the horseradish peroxidase‐labeled secondary antibody (1:10000; Jackson ImmunoResearch) for 2 h. The protein bands were visualized using enhanced chemiluminescence (Millipore) and captured with the Tanon 4600 imaging system (Tanon Science, China). β‐actin was utilized to normalize the target protein expression.

Article Title: Integrating bulk, single-cell, and spatial transcriptomics to identify and functionally validate novel targets to enhance immunotherapy in NSCLC
Article Snippet: Equal volumes of protein samples were separated by SDS-PAGE (PG112, Epizyme Biotech, Shanghai, China) and transferred to PVDF membranes (ISEQ00010, Millipore, USA). .. After blocking, the membranes were incubated with the following primary antibodies under specified conditions: CTSH (1:1000, Cat#10315-1-AP, RRID: AB_2087534, Proteintech, Wuhan, China), PTGES3 (1:1000, Cat#15216-1-AP, RRID: AB_2284772, Proteintech, Wuhan, China), MLKL (1:1000, Cat.#: 380559, Zen Biotechnology Co., Ltd., Chengdu, China), Phospho-MLKL (Ser358) (1:1250, Cat# 382136, Zen Biotechnology Co., Ltd., Chengdu, China), RIPK3 (1:1000, Cat# AF4808, RRID: AB_2844793, Affinity Biosciences, China), Phospho-RIPK3 (1:5000, Cat# 93654, RRID: AB_2800206, Cell Signaling Technology, China), RIPK1 (1:1000, Cat.# 3493, RRID: AB_2305314, Cell Signaling Technology, China), and GAPDH (1:2000, Cat.# 60004-1-Ig, RRID: AB_2107436, Proteintech, Wuhan, China). .. The following secondary antibodies were used to amplify the signal of the target protein: HRP-conjugated Affinipure Goat Anti-Mouse IgG (H+L) (1:2000, Cat#SA00001-1, RRID: AB_2722565) and HRP-conjugated Affinipure Goat Anti-Rabbit IgG (H+L) (1:2000, Cat#SA00001-2, RRID: AB_2722564, Proteintech, China).

Article Title: Targeted-nanoformulation of cannabidiol attenuates endothelial injury and platelet hyperactivation for combating silicosis
Article Snippet: Silicosis, one of the major global occupational diseases, is an irreversible pulmonary fibrotic disorder caused by silicon dioxide (SiO2), characterized by persistent inflammatory responses, as well as endothelial cell (EC) dysregulation and platelet abnormalities.. Given the complexity of this pathological process, treatments relying solely on anti-inflammatory monotherapies often exhibit limited therapeutic efficacy.. Thus, developing a nanocomplex that can coordinately regulate EC and platelet functions and inhibit the inflammatory process is a promising strategy.

Article Title: Identification of Cathepsin H and Metabolic Traits as Potential Biomarkers for Lung Cancer by Mendelian Randomization and Single‐Cell Transcriptomics
Article Snippet: .. See the T erm s and C onditions (https://onlinelibrary.w iley.com /term s-and-conditions) on W iley O nline L ibrary for rules of use; O A articles are governed by the applicable C reative C om m ons L icense transferred onto PVDFmembranes (EMDMillipore Corp).Membranes were blocked with 5% BSA for 2 h at room temperature and incubated overnight at 4°Cwith the primary antibody against CTSH (Proteintech, 1:1000) and β-actin (Proteintech, 1:1000). .. After washing three times with TBST, the membranes were incubated with the horseradish peroxidase-labeled secondary antibody (1:10000; Jackson ImmunoResearch) for 2 h. The protein bands were visualized using enhanced chemiluminescence (Millipore) and captured with the Tanon 4600 imaging system (Tanon Science, China). β-actin was utilized to normalize the target protein expression.

Blocking Assay:

Western Blot:

Article Title: Characterization of gRNA-dependent and gRNA-independent off-target binding sites of PspCas13b and RfxCas13d in mammalian cells
Article Snippet: The target proteins were detected by the indicated antibodies and visualized by enhanced chemiluminescence (ECL) reagent (Thermo Fisher). .. The following antibodies were used for western blot analysis in this study: PTBP1 polyclonal antibody (Proteintech, 12582-1-AP), RHOA polyclonal antibody (Proteintech, 10749-1-AP), CTSH polyclonal antibody (Proteintech, 10315-1-AP), CDK19 polyclonal antibody (Proteintech, 13761-1-AP), HMGN2 polyclonal antibody (Proteintech, 10953-1-AP), ACVR2B antibody (Abmart, T58048 ), NUCKS1 polyclonal antibody (Proteintech, 12023-2-AP), HMGA1 polyclonal antibody (Proteintech, 29895-1-AP), EZH2 polyclonal antibody (Proteintech, 21800-1-AP), EFNA3 polyclonal antibody (Proteintech, 12480-1-AP), HPSE polyclonal antibody (Proteintech, 24529-1-AP), SPG7 polyclonal antibody (Proteintech, 27801-1-AP), TRAF3 polyclonal antibody (Proteintech, 18099-1-AP), MDK polyclonal antibody (Proteintech, 11009-1-AP), SCRN1 polyclonal antibody (Proteintech, 14303-1-AP), HA-Tag (26D11) mAb (Abmart, M20003L), GAPDH (3B3) mAb (Abmart, M20006L), ACSL1 polyclonal antibody (Proteintech, 13989-1-AP), FASN polyclonal antibody (Proteintech, 10624-2-AP), RPL14 polyclonal antibody (Proteintech, 14991-1-AP), ACOX1 polyclonal antibody (Proteintech, 10957-1-AP), ACO2 polyclonal antibody (Proteintech, 11134-1-AP), EIF2D polyclonal antibody (Proteintech, 12840-1-AP). ..

other:

Article Title: Characterization of gRNA-dependent and gRNA-independent off-target binding sites of PspCas13b and RfxCas13d in mammalian cells.
Article Snippet: After heating at 70 ◦C for 10 min, the lysed protein samples were resolved by SDS– PAGE and transferred onto a nitrocellulose membrane (Millipore).

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