Log In Sign up
The largest database of trusted experimental protocols
> Chemicals & Drugs > Amino Acid > Proliferating Cell Nuclear Antigen

Proliferating Cell Nuclear Antigen

Proliferating Cell Nuclear Antigen (PCNA) is a key regulator of cell cycle progression and DNA replication.
It serves as a processivity factor for DNA polymerase, ensuring efficient DNA synthesis during cell division.
PCNA is widely used as a marker of cellular proliferation and is implicated in various cellular processes, including DNA repair, chromatin remodeling, and cell cycle control.
Its expression is tightly regulated and can provide insights into the proliferative state of cells in normal and pathological conditions, such as cancer.
Researchers leveraging PCNA analysis can gain valuable insights into cellular dynamics and proliferative potential.

Most cited protocols related to «Proliferating Cell Nuclear Antigen»

1
Constructing Meta-PCNA Signature
Cited 22 times
We computed the Pearson correlation between PCNA and all the genes in the Ge et al. [54] (link) dataset and selected the 1% most positively correlated, i.e., 131 genes out of 13,077, to form the meta-PCNA signature (Table S1). The meta-PCNA index of a tissue was computed from its expression profile by taking the median expression of these genes.
Venet D., Dumont J.E, & Detours V. (2011). Most Random Gene Expression Signatures Are Significantly Associated with Breast Cancer Outcome. PLoS Computational Biology, 7(10), e1002240.
Full text: Click here
Publication 2011
Gene Expression Genes Proliferating Cell Nuclear Antigen Tissues
2
Generating Fluorescent Fusion Proteins
Cited 21 times
Mouse C2C12 myoblast cells were used for all experiments unless otherwise stated and transiently transfected by the calcium phosphate–DNA coprecipitation method as described previously (10 (link)) with equal amounts of plasmid DNA for cotransfections. C2C12 cells stably expressing either GFP-PCNAL2 [human PCNA (1 (link))] or GFP-Ligase [human DNA Ligase I (10 (link))] were established and grown as described previously (1 (link)). A GFP–FEN1 fusion protein was constructed by fusing an N-terminal SV40 nuclear localization signal followed by enhanced GFP and a 15 amino acid linker sequence to the mouse FEN1 ORF, isolated from a mouse embryo cDNA library (Clontech) by PCR and confirmed by DNA sequencing. mRFP1 fusion proteins were obtained by replacing enhanced GFP in previously described PCNA and Ligase plasmids by the mRFP1 coding sequence (11 (link)). The structure of the chimeric proteins, as well as their characterization (expression and localization in mammalian cells) is shown in Supplementary Figure S1 and in refs (1 (link),9 (link),10 (link)).
Sporbert A., Domaing P., Leonhardt H, & Cardoso M.C. (2005). PCNA acts as a stationary loading platform for transiently interacting Okazaki fragment maturation proteins. Nucleic Acids Research, 33(11), 3521-3528.
Publication 2005
Amino Acid Sequence Calcium Phosphates cDNA Library Cells Chimera Embryo Flap Endonuclease-1 Homo sapiens Ligase Ligase I, DNA Mammals Mrfp1 protein Mus Myoblasts Nuclear Localization Signals Open Reading Frames Plasmids Proliferating Cell Nuclear Antigen Proteins Simian virus 40
3
Automated Outcome Association Estimation
Cited 17 times
In order to systematically compare the published signatures to random signatures and evaluate the relation between outcome association and meta-PCNA, we needed an outcome association estimation procedure that is robust and fully automated. We systematically compared three procedures and selected among them the most sensitive and stable one. This is described in Supporting Information (Text S3.), only the selected method is described here. It consists in computing the first principal component (PC1) of the signature (with R's prcomp) and then split the cohort according to the median of PC1. Probes mapping to the same gene were averaged and, following Ramaswamy et al. [57] (link), data were median polished (R's medpolish) before the dimension reduction step.
Venet D., Dumont J.E, & Detours V. (2011). Most Random Gene Expression Signatures Are Significantly Associated with Breast Cancer Outcome. PLoS Computational Biology, 7(10), e1002240.
Full text: Click here
Publication 2011
Proliferating Cell Nuclear Antigen
4
Western Blot Protein Expression Analysis
Cited 15 times
Western blot was performed referring to our previous articles 24 (link)-26 (link). In brief, proteins from cultured cells or homogenized left ventricles were separated by 10% SDS-PAGE and were electrophoretically transferred onto PVDF membranes (EMD Millipore, Billerica, MA, USA; No. IPFL00010). Membranes were blocked with 5% nonfat milk for 60min at room temperature, and were subsequently probed with indicating primary antibodies overnight at 4°C, followed with the secondary antibodies at 37°C for 1 hour. The bands were scanned and quantified by Odyssey Infrared Imaging System (LI-COR Biosciences, Lincoln, NE, USA), and protein expressions were normalized to total proteins or GAPDH. Nuclear and cytosolic protein fractions were separated by a commercial kit as our previously described 9 (link), 21 (link). Proteins from cytosolic lysates were normalized to GAPDH, whereas proteins from nuclear lysates were normalized to PCNA.
Total RNA was isolated using TRIzol according to our previous studies and reverse transcribed with Maxima First Strand cDNA Synthesis Kit (Thermo Fisher Scientific, MA, USA)27 (link). The expression level of each individual transcript was normalized to Gapdh.
Zhang X., Zhu J.X., Ma Z.G., Wu H.M., Xu S.C., Song P., Kong C.Y., Yuan Y.P., Deng W, & Tang Q.Z. (2019). Rosmarinic acid alleviates cardiomyocyte apoptosis via cardiac fibroblast in doxorubicin-induced cardiotoxicity. International Journal of Biological Sciences, 15(3), 556-567.
Publication 2019
Anabolism Antibodies Cultured Cells Cytosol DNA, Complementary GAPDH protein, human Left Ventricles Milk, Cow's Nuclear Proteins polyvinylidene fluoride Proliferating Cell Nuclear Antigen Proteins SDS-PAGE Tissue, Membrane trizol Western Blotting
5
Ischemic Stroke Evaluation and Treatment
Cited 15 times
A total of 138 mice were used in this study (102 C57BL/6 male mice and 36
nestin-CreERT2-R26R-YFP male mice). Male mice were used in this study to reduce
experimental variability in stroke. The animals were subjected to the following
experiments: 28 mice were subjected to MCAo and received either vehicle or SAG
treatment from post-stroke day3–8. Mice were subject to locomotion
behavioral functional test before MCAo and at 3, 7, 21, 28 days after MCAo.
Additional 36 mice were subjected to MCAo and received either vehicle or SAG
treatment (post-stroke day3–8) and were evaluated for Barnes maze test
to evaluate memory and learning at 30 days post stroke. 18 mice from the Barnes
maze test group were subjected to MRI study on post-stroke day2 and 30 to
evaluate ischemic damage and CBF. To evaluate the effect of SAG treatment on
Barnes maze performance on control mice, mice received SAG or vehicle treatment
(10mg/kg for 6 days, n= 9 for each group) without surgery and were
subjected to Barnes Maze test 21 days later. To evaluate the proliferation of
SVZ and SGZ cells, Bromodeoxyuridine (BrdU) pulse labeling were carried out on
post-stroke day 6 after either vehicle or SAG treatment and brain were harvested
24 hours later to quantify BrdU+, PCNA+ (proliferating cell
nuclear antigen) or Ki67+ cells (20 mice). To evaluate neurogenesis and
long-term survival of NSC progeny: 20 nestin-CreERT2-R26R-YFP mice were treated
with tamoxifen (TAM) to induce yellow fluorescent protein (YFP) labeling of SVZ
and SGZ NSCs and treated with either vehicle or SAG (post-stroke day
3–8). YFP+, DCX+ or NeuN+ cells were analyzed by
unbiased stereological method at 30 days post stroke. Mice from the MRI study
and the nestin-CreERT2-R26R-YFP were combined to analyze the DCX+ cells
and angiogenesis as well. To examine gene expression in SVZ NSCs, additional 16
nestin-CreERT2-R26R-YFP mice were subjected to MCAo and SAG or vehicle treatment
(post-stroke day 3–8) and SVZ tissue microdissected using methods
described in 13 (link) for
quantitative RT-PCR. To evaluate angiogenesis by histochemistry, brain sections
from post-stroke day 30 mice were subjected to immunostaining using two
different markers, alpha-smooth muscle actin (α-SMA) and CD31 and
quantitatively analyzed as described in detail in the supplemental information.
All the experimental groups are randomized and all outcome analysis was
carried out by independent study team members blinded to the treatment
condition. Details on experimental timeline, randomization and blinding of
groups, animal numbers for each experiment, and survival rate/exclusions due to
death are included in online
supplemental data. Details on each assay are also included in online supplemental
data.
Jin Y., Barnett A., Zhang Y., Yu X, & Luo Y. (2017). Post-stroke shh agonist treatment improves functional recovery by enhancing neurogenesis and angiogenesis. Stroke, 48(6), 1636-1645.
Publication 2017
alpha-Actin angiogen Animals Antigens Biological Assay Brain Bromodeoxyuridine Cells Cerebrovascular Accident Gene Expression Histocytochemistry Males Maze Learning MAZE protocol Memory Mice, Inbred C57BL Mus Neurogenesis Operative Surgical Procedures Proliferating Cell Nuclear Antigen Protein, Nestin Proteins Pulse Rate Reverse Transcriptase Polymerase Chain Reaction Smooth Muscles Tamoxifen TimeLine Tissues

Most recents protocols related to «Proliferating Cell Nuclear Antigen»

1
Protein Expression Analysis in RL95-2 Cells and ESCs
Total proteins were obtained from RL95-2 cells treated with or without 5, 10 or 20 µM PD for 24 h, or from ESCs by lysis using cold RIPA lysis buffer (Beyotime Institute of Biotechnology). Protein concentration was determined using a BCA Protein Assay kit (Beijing Solarbio Science & Technology Co., Ltd.) and protein samples (20 µg per lane) were separated on 10% gels by SDS-PAGE (Thermo Fisher Scientific, Inc.), transferred onto PVDF membranes (MilliporeSigma) and incubated for 1 h at room temperature with 5% skimmed milk. The membranes were then incubated at 4°C overnight with the following primary antibodies: Ki67 (1:1,000; ab92742), proliferating cell nuclear antigen (PCNA; 1:1,000; ab92552), MMP2 (1:1,000; ab92536), MMP9 (1:1,000; ab76003), ADRA2A (1:1,000; ab85570), phospho (p)-PI3K (1:1,000; ab182651), p-Akt (1:1,000; ab192623), PI3K (1:1,000; ab191606), Akt (1:1,000; ab179463) and GAPDH (1:2,500; ab9485), all from Abcam. After washing with TBST (0.1% Tween), the membranes were incubated with Goat Anti-Rabbit IgG H&L (HRP) secondary antibody (1:2,000; ab6721; Abcam) at 37°C for 1 h. The immunoreactive protein bands were visualized using an enhanced chemiluminescence detection system (Amersham; Cytiva) according to the manufacturer's instructions. Subsequently, protein brands were observed using ImageJ (v1.8.0; National Institutes of Health) and quantified by densitometry (QuantityOne 4.5.0 software; Bio-Rad Laboratories, Inc.). GAPDH served as an internal reference.
Ni Z., Dawa Z., Suolang D., Pingcuo Q., Langga Z., Quzhen P, & Deji Z. (2023). Platycodin D inhibits the proliferation, invasion and migration of endometrial cancer cells by blocking the PI3K/Akt signaling pathway via ADRA2A upregulation. Oncology Letters, 25(4), 136.
Publication 2023
ADRA2A protein, human anti-IgG Antibodies Biological Assay Buffers Cells Chemiluminescence Cold Temperature Densitometry Enhanced S-Cone Syndrome GAPDH protein, human Gels Goat Immunoglobulins Milk, Cow's MMP2 protein, human MMP9 protein, human Phosphatidylinositol 3-Kinases polyvinylidene fluoride Proliferating Cell Nuclear Antigen Proteins Rabbits Radioimmunoprecipitation Assay SDS-PAGE Tissue, Membrane Tweens
2
Western Blot Analysis of Protein Expression
Protein was isolated from cells following treatment with RIPA lysis buffer (Life-iLab Bio) and quantified using a Nano 300 protein detector (YPH-Bio). Protein separation (30 µg per lane) was achieved using 10% SDS-polyacrylamide gel electrophoresis and the separated proteins were transferred to PVDF membranes (Roche Diagnostics). The membranes were incubated with 5% skimmed milk for 2 h at room temperature, with primary antibodies overnight at 4°C and HRP-conjugated secondary antibodies for 2 h at room temperature in sequence. The primary antibodies against LPCAT1 (cat. no. ab214034; 1:2,000), FOXA1 (cat. no. ab170933; 1:1,000), Ki67 (cat. no. ab92742; 1:5,000), proliferating cell nuclear antigen (PCNA; cat. no. ab92552; 1:1,000), MMP2 (cat. no. ab92536; 1:1,000), MMP9 (cat. no. ab76003; 1:1,000), Bcl-2 (cat. no. ab32124; 1:2,000), Bax (cat. no. ab32503; 1:1,000), cleaved caspase 3 (cat. no. ab32042; 1:500) and GAPDH (cat. no. ab9485; 1:2,500), and the secondary antibodies (cat. no. ab6721; 1:4,000) were all from Abcam. Blots were visualized after treatment with Immobilon ECL Ultra Western HRP (Merck KGaA) and gray values were analyzed with ImageJ software (v1.8.0; National Institutes of Health).
Zhang H, & Zheng Y. (2023). LPCAT1 is transcriptionally regulated by FOXA1 to promote breast cancer progression and paclitaxel resistance. Oncology Letters, 25(4), 134.
Publication 2023
Aftercare Antibodies BCL2 protein, human Buffers Caspase 3 Cells Diagnosis FOXA1 protein, human GAPDH protein, human Immobilon Milk, Cow's MMP2 protein, human MMP9 protein, human polyvinylidene fluoride Proliferating Cell Nuclear Antigen Proteins Radioimmunoprecipitation Assay SDS-PAGE Tissue, Membrane
3
Immunofluorescence Analysis of BrdU-Labeled Cells
Two types of immunofluorescence detections were performed on the BrdU-treated lizards. For those in the first group, with survival times of 1.5 h or 3 days (n = 3 each), a triple immunofluorescence detection for GFAP/DCX/BrdU was performed. For those in the second group, with a survival time of 7 days from the first injection and 3 days from the last injection (n = 3), a double immunofluorescence for BrdU/PCNA was performed.
In both cases the protocol for fluorescence immunohistochemistry was similar, except for the antibodies used. First, the slides were deparaffinized and hydrated. Then, they were treated with HCl 2N for 10 min at 37°C for DNA denaturation, rinsed in 0.1 M borate buffer and washed in phosphate buffered saline containing 0.1% Triton X-100 and BSA 0.1% (PTA). Subsequently, the sections were incubated in a blocking solution containing 10% casein (Vector) or 5% normal goat serum (NGS) (Sigma, San Luis, MO, USA) in PTA for 1 h, for triple or double immunoassay, respectively. After rinsing in PTA, the sections were incubated in blocking solution with the corresponding primary antibodies overnight at 4°C. The primary antibodies used for the first group were: mouse anti-BrdU (1:150, Dako), rabbit anti-GFAP (1:500, Dako), and goat anti-DCX (1:200, Sta. Cruz Biotechnologies); and for the second group: mouse anti-PCNA (1:500, Sigma, San Luis, MO, USA), and rat anti-BrdU (1:200, Abcam, Cambridge, UK). Sections were then washed with PTA and incubated with fluorescent secondary antibodies at 1:500 in blocking solution for 1 h at room temperature in the dark. The secondary antibodies used for the first group were: donkey anti-mouse Alexa 647 (1:500, Invitrogen, Walthan, MA, USA), donkey anti-rabbit Alexa 488 (1:500, Invitrogen, Walthan, MA, USA), and donkey anti-goat Alexa 555 (1:500, Invitrogen, Walthan, MA, USA); and for the second group: goat anti-mouse Alexa 555 (1:500, Invitrogen, Walthan, MA, USA), and goat anti-rat Alexa 488 (1:500, Invitrogen, Walthan, MA, USA). The sections were then washed in 0.1 M PB and incubated for 10 min with DAPI 1:1000 in H2O (Sigma, San Luis, MO, USA) at room temperature in the dark. Finally, the slides were washed with 0.1 M PB and mounted with Fluorsave (Calbiochem). The sections were analyzed with a Leica (Wetzlar, Germany) SP2 TCS AOBS inverted confocal microscope.
González-Granero S., Font E., Desfilis E., Herranz-Pérez V, & García-Verdugo J.M. (2023). Adult neurogenesis in the telencephalon of the lizard Podarcis liolepis. Frontiers in Neuroscience, 17, 1125999.
Full text: Click here
Publication 2023
Antibodies Borates Bromodeoxyuridine Caseins Cloning Vectors DAPI DNA Denaturation Equus asinus Fluorescence Fluorescent Antibody Technique Glial Fibrillary Acidic Protein Goat Immunoassay Immunohistochemistry Lizards Mice, House Microscopy, Confocal Phosphates Proliferating Cell Nuclear Antigen Rabbits Saline Solution Serum Triton X-100
4
Protein Expression Analysis by Western Blot
After being quantified protein concentration, protein was separated using SDS-PAGE electrophoresis. The membranes were incubated with the primary antibodies, including anti-PCNA (1:1,000, 13110T; Cell Signaling Technology, Danvers, MA, USA), anti-MMP9 (1:500, ab76003; Abcam, Burlingame, CA, USA), anti-VEGFA (1:1,000, ab214424; Abcam), anti-MFGE8 (1:500, AF2767; NOVUS, Littleton, CO, USA), and anti-β-actin (1:4,000, ab8227; Abcam). Next, the corresponding HRP-conjugated secondary antibodies (Abcam) were employed to block the membrane. After 2 hours, the protein band was visualized using ECL chromogenic substrate (Beyotime, Shanghai, China).
Wu Y., Wang F., Shi J., Guo X, & Li F. (2023). CircSMAD2 accelerates endometrial cancer cell proliferation and metastasis by regulating the miR-1277-5p/MFGE8 axis. Journal of Gynecologic Oncology, 34(2), e19.
Publication 2023
Actins Antibodies Cardiac Arrest Chromogenic Substrates Electrophoresis MFGE8 protein, human MMP9 protein, human Novus Proliferating Cell Nuclear Antigen Proteins SDS-PAGE Tissue, Membrane
5
Protein Expression Analysis of H9c2 Cells
H9c2 cell protein was extracted using RIPA lysis buffer (Beyotime Institute of Biotechnology), and a BCA kit was used for protein determination (Beyotime Institute of Biotechnology). Protein (45 µg per lane) was separated by SDS-PAGE (12%) and then transferred to PVDF membranes (MilliporeSigma). The membranes were blocked with 5% skim milk for 60 min at 4˚C. Subsequently, membranes were treated overnight with primary antibodies at 4˚C, namely anti-proliferating cell nuclear antigen (PCNA; 1:2,000 dilution; cat. no. 10205-2-AP; ProteinTech Group, Inc.), anti-Ki-67 (1:2,000 dilution; cat. no. 27309-1-AP; ProteinTech Group, Inc.), anti-Bax (1:2,000 dilution; cat. no. 50599-2-Ig; ProteinTech Group, Inc.), anti-Bcl-2 (1:2,000 dilution; cat. no. 12789-1-AP; ProteinTech Group, Inc.), anti-Cleaved Caspase-3 (1:1,000 dilution; cat. no. ab2302; Abcam), anti-Cleaved Caspase-9 (1:1,000 dilution; cat. no. ab2324; Abcam), anti-phosphorylated (p)-JNK (1:2,000 dilution; cat. no. 80024-1-RR; ProteinTech Group, Inc.), anti-JNK (1:2,000 dilution; cat. no. 24164-1-AP; ProteinTech Group, Inc.), anti-p-p38 (1:2,000 dilution; cat. no. 28796-1-AP; ProteinTech Group, Inc.), anti-p38 (1:2,000 dilution; cat. no. 14064-1-AP; ProteinTech Group, Inc.), anti-p-ERK (1:2,000 dilution; cat. no. 28733-1-AP; ProteinTech Group, Inc.), anti-ERK (1:2,000 dilution; cat. no. 16443-1-AP; ProteinTech Group, Inc.) and anti-β-actin (1:5,000 dilution; cat. no. 20536-1-AP; ProteinTech Group, Inc.). β-actin was regarded as the endogenous control. Then, the membranes were then treated for 1 h at room temperature with an HRP-labeled secondary antibody: Goat Anti-Rabbit IgG (H+L) HRP [1:5,000 dilution; cat. no. GAR007; MultiSciences (Lianke) Biotech Co., Ltd.]. Lastly, protein blots were visualized using an enhanced chemiluminescence kit (ECL; MilliporeSigma) and quantification was performed using ImageJ Software (National Institutes of Health; version 4.3).
Qian X., Xiong S., Chen Q., Zhang J, & Xie J. (2023). Parecoxib attenuates inflammation injury in septic H9c2 cells by regulating the MAPK signaling pathway. Experimental and Therapeutic Medicine, 25(4), 150.
Publication 2023
Actins anti-IgG Antibodies BCL2 protein, human Buffers Caspase 3 Caspase 9 Cells Chemiluminescence Goat Immunoglobulins Milk, Cow's Mitogen-Activated Protein Kinase 3 polyvinylidene fluoride Proliferating Cell Nuclear Antigen Proteins Rabbits Radioimmunoprecipitation Assay SDS-PAGE Technique, Dilution Tissue, Membrane

Top products related to «Proliferating Cell Nuclear Antigen»

1
Proliferating cell nuclear antigen (pcna) by Cell Signaling Technology
Sourced in United States, United Kingdom, China
PCNA (Proliferating Cell Nuclear Antigen) is a protein that plays a critical role in DNA replication and repair. It acts as a processivity factor, ensuring that DNA polymerases remain attached to the DNA template during replication, thereby enhancing the efficiency of DNA synthesis. PCNA is a widely used marker for cell proliferation and is often employed in research applications to study cell cycle dynamics and DNA damage response pathways.
2
Proliferating cell nuclear antigen (pcna) by Santa Cruz Biotechnology
Sourced in United States, United Kingdom, Germany, China, Japan
PCNA (Proliferating Cell Nuclear Antigen) is a lab equipment product used in molecular biology research. It functions as a processivity factor, enabling DNA polymerase to replicate DNA efficiently. PCNA is essential for DNA replication and repair processes.
3
Pvdf membrane by Merck Group
Sourced in United States, Germany, China, United Kingdom, Morocco, Ireland, France, Italy, Japan, Canada, Spain, Switzerland, New Zealand, India, Hong Kong, Sao Tome and Principe, Sweden, Netherlands, Australia, Belgium, Austria
PVDF membranes are a type of laboratory equipment used for a variety of applications. They are made from polyvinylidene fluoride (PVDF), a durable and chemically resistant material. PVDF membranes are known for their high mechanical strength, thermal stability, and resistance to a wide range of chemicals. They are commonly used in various filtration, separation, and analysis processes in scientific and research settings.
4
Proliferating cell nuclear antigen (pcna) by Abcam
Sourced in United States, United Kingdom, China, Morocco
PCNA is a protein that plays a crucial role in DNA replication and repair. It serves as a processivity factor, enabling DNA polymerases to replicate DNA efficiently.
5
Ab92552 by Abcam
Sourced in United States, United Kingdom, China
Ab92552 is a rabbit monoclonal antibody against the protein Histone H3. It is intended for use in research applications.
6
Anti pcna by Santa Cruz Biotechnology
Sourced in United States, Germany, United Kingdom, China, Denmark
Anti-PCNA is a primary antibody that recognizes the Proliferating Cell Nuclear Antigen (PCNA) protein. PCNA is an essential component of the DNA replication machinery and serves as a processivity factor for DNA polymerase. This antibody can be used for the detection and analysis of PCNA in various applications, such as Western blotting, immunohistochemistry, and immunocytochemistry.
7
Anti pcna by Abcam
Sourced in United Kingdom, United States, China
Anti-PCNA is a primary antibody that recognizes the Proliferating Cell Nuclear Antigen (PCNA) protein, a key component involved in DNA replication and repair processes. This antibody can be used as a tool for detecting and quantifying PCNA expression in various cell and tissue samples.
8
Ripa lysis buffer by Beyotime
Sourced in China, United States, Switzerland, Germany, Japan, United Kingdom
RIPA lysis buffer is a detergent-based buffer solution designed for the extraction and solubilization of proteins from cells and tissues. It contains a mixture of ionic and non-ionic detergents that disrupt cell membranes and solubilize cellular proteins. The buffer also includes additional components that help to maintain the stability and activity of the extracted proteins.
9
Cleaved caspase 3 by Cell Signaling Technology
Sourced in United States, United Kingdom, China, Germany, Canada, Japan, Morocco, Denmark, Switzerland, France, Netherlands, Macao
Cleaved caspase-3 is an antibody that detects the activated form of caspase-3 protein. Caspase-3 is a key enzyme involved in the execution phase of apoptosis, or programmed cell death. The cleaved caspase-3 antibody specifically recognizes the active, cleaved form of the enzyme and can be used to monitor and quantify apoptosis in experimental systems.
10
β actin by Cell Signaling Technology
Sourced in United States, United Kingdom, China, Germany, Japan, Canada, Morocco, Sweden, Netherlands, Switzerland, Italy, Belgium, Australia, France, India, Ireland
β-actin is a cytoskeletal protein that is ubiquitously expressed in eukaryotic cells. It is an important component of the microfilament system and is involved in various cellular processes such as cell motility, structure, and integrity.

More about "Proliferating Cell Nuclear Antigen"

Proliferating Cell Nuclear Antigen (PCNA) is a crucial regulator of cell cycle progression and DNA replication.
As a processivity factor for DNA polymerase, PCNA ensures efficient DNA synthesis during cell division.
This protein is widely used as a marker of cellular proliferation and is implicated in various cellular processes, such as DNA repair, chromatin remodeling, and cell cycle control.
PCNA expression is tightly regulated and can provide valuable insights into the proliferative state of cells in normal and pathological conditions, including cancer.
Researchers can leverage PCNA analysis to gain deep insights into cellular dynamics and proliferative potential.
PVDF membranes are commonly used for PCNA detection and quantification, often in combination with Anti-PCNA antibodies (e.g., Ab92552) and RIPA lysis buffer.
Cleaved caspase-3, a marker of apoptosis, and β-actin, a housekeeping protein, are also frequently used in PCNA studies to provide a more comprehensive understanding of cellular processes.
By utilizing the power of PubCompare.ai, researchers can effortlessly locate the best PCNA analysis methods from literature, pre-prints, and patents, while comparing products and protocols side-by-side to identify the most efficient and effective approaches.
This AI-driven tool can streamline PCNA research and help proliferate scientific discoveries.