Antibody News

MCP1: One Chemoattractant that's Hard to Resist

Wednesday, July 18, 2012 - 07:00

Monocyte Chemoattractant Protein (MCP1) is a potent monocyte attractant, is a member of the CC chemokine subfamily. MCP1 exerts its effects through binding to G-protein-coupled receptors on the surface of leukocytes targeted for activation and migration. The role of MCP1 and its receptor, chemokine receptor-2 (CCR2), in monocyte recruitment during infection or under other inflammatory conditions is well known. Recent studies indicate that MCP-1 may play an important role in pulmonary inflammation. In vitro studies show that a number of cell types are capable of producing MCP1 (1). Rat macrophage subpopulations were examined by immunohistochemistry using various anti-rat macrophage monoclonal antibodies. These studies revealed that the main sources of MCP-1 production were alveolar and interstitial macrophages and polymorphonuclear leukocytes in the rat model of bleomycin-induced lung injury (2...

EZH2: Epigenetic Signaling, Stem Cell Maintenance and Oncogenesis Made Easy

Tuesday, July 17, 2012 - 12:41

The polycomb group (PcG) protein, enhancer of zeste homolog 2 (EZH2) is a methyl-transferase that plays a key role in transcriptional gene repression. EZH2 is frequently overexpressed in several malignant tumors, and is often associated with advanced disease stage in many solid tumors. Increased EZH2 levels were detected by Western blotting using anti-EZH2 antibodies in human pancreatic cancer cell lines, suggesting aberrant cell growth and invasiveness (1). EZH2 protein was overexpressed in invasive carcinomas compared to benign breast carcinomas as detected by immunohistochemistry using anti-EZH2 antibodies, suggesting a link between EZH2 and high grade and basal tumors (2).

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E-Cadherin as a Cancer Biomarker

Friday, July 13, 2012 - 10:59

E-cadherin is a calcium-regulated adhesion molecule expressed in most normal epithelial tissues. E-cadherin is also associated with gland formation, stratification, and epithelial polarization, while loss of E-cadherin can cause dedifferentiation and invasiveness in several human carcinomas (1). In a recent study, human breast cancer tissues were stained immunohistochemistry (IHC) by anti- E-Cadherin antibodies. Loss of E-Cadherin expression correlated with the invasiveness of carcinoma (2).

Immunohistochemistry: E-Cadherin Antibody

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Phosphotyrosine is Critical Signal Transduction and Regulation

Tuesday, July 10, 2012 - 12:16

Phosphotyrosine is the phosphorylated version of the amino acid tyrosine, which results from the activation of intracellular protein kinases (e.g. via growth factors) during normal growth and development, well as in transformation and oncogenesis. Phosphorylation of histidine, serine, threonine and tyrosine residues acts as a signaling system to control many cellular signaling pathways. The cellular networks which rely on these signals can be very complex, so phosphorylation often occurs on multiple sites on a given protein. This phosphorylation is reversible, allowing for exquisite regulation and modulation. Phosphotyrosine is one of the most frequent post-translational modifications that regulate protein-protein interaction and enzyme activity in eukaryotic cells.

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Perforin Antibodies Reveal Links to Apoptosis and Immune Response

Monday, July 9, 2012 - 09:25

Perforin, also known as the pore-forming protein, pfp, is a 70 kD cytolytic protein expressed in the cytoplasmic granules of cytotoxic T lymphocytes (CTLs) and natural killer (NK) cells. It is one of the major effector molecules used by CTL and NK cells to mediate targeted cell killing and lysis, and thus has an important role in the immune response against tumors and virus infections. Perforin is a membrane-disrupting protein that introduces the granzymes into a target cell, causing cytoplasmic protein degredation and eventual apoptosis.

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PCNA Antibodies: Marking Cell Proliferation & DNA Replication

Friday, July 6, 2012 - 09:35

Proliferating Cell Nuclear Antigen (PCNA), also known as the polymerase delta auxiliary protein, is a nuclear protein essential for DNA replication as well as DNA excision and mismatch repair pathways. It has a large role in cell cycle regulation and response of cells to stress. Studies with PCNA antibodies have determined its mechanism of action to be direct binding of downstream signaling molecules such as CDK inhibitor p21, the endonucleases FEN1 and XPG, and DNA cytosine 5-methyltransferase (DNMT1).

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Using EGF Protein from Novus Biologicals

Thursday, July 5, 2012 - 10:02

EGF (epidermal growth factor) stimulates differentiation, proliferation and cell growth by binding to its receptor, EGFR. EGF was first discovered in the mouse submandibular gland in 1986 by Stanley Cohen of Vanderbilt University, leading to a Nobel Prize in Physiology and Medicine. Since then, EGF has been found in many tissues of the human body (including urine, saliva, plasma, milk, macrophages and platelets) and has been the subject of intense study in many areas of clinical research due to its many abilities. EGF from the salivary gland has been shown to maintain oro-esophageal and gastric tissue integrity, including healing of ulcers, inhibiting gastric acid secretion and stimulation of DNA synthesis. Low levels of EGF have also been linked to Parkinson’s Disease in the elderly. EGF has been used to study de novo trastuzumab resistant...

Nucleolin Antibodies: Knowing When it's Time to Split

Thursday, June 28, 2012 - 10:54

Nucleolin is an abundant, 106 kDa nucleolar phosphoprotein that is a major protein in actively dividing cells. The stability of nucleolin is heavily cell proliferation-dependent, as nucleolin antibody studies have shown that degraded forms are relatively abundant in quiescent non-dividing cells, while nonexist in actively dividing cells. This protein plays multifunctional roles in global processes of rDNA transcription, organization, and rRNA processing. Hanakahi, et. al. believe nucleolin is a component of the B-cell-specific transcription factor LR1 through use of nucleolin antibodies (1). Immunoprecipitation with nucleolin antibodies shows in vitro nucleolin binding to the KLF2 transcription factor...

Myosin is More than Just a Heavy Lifter

Wednesday, June 27, 2012 - 10:24

Myosin is a well-known, hexameric molecular motor that is a key cytoskeletal component. It consists of a pair of myosin heavy chain subunits (MHC), a pair of essential myosin light chain subunits (MLC), and a pair of regulatory light chain subunits (RLCs). Non-muscle myosin heavy chain 10 (also known as Myosin-IIB, cellular myosin heavy chain type B, and NMMHCB) is encoded by the MYH10 gene, while non-muscle myosin heavy chain II-A is encoded by the MYH9 gene. Myosin antibodies have been used to characterize variants and isoforms (1,2).

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MyD88 Antibodies for IL Signaling and Immunity Research

Tuesday, June 26, 2012 - 13:30

The myeloid differentiation protein MyD88 (myeloid differentiation primary response protein) was originally identified and characterized as a primary upregulated response gene in interleukin-6 mediated myeloid differentiation. Now, MyD88 is known to be an essential cytosolic adaptor protein in the innate and adaptive immune responses controlled by the interleukin-1 signaling pathway, and MyD88 antibodies have shown that it is expressed in many tissues (1).

Immunohistochemistry: MyD88 Antibody

Studies with MyD88 antibodies have shown that MyD88 directly...

Mapping Signal Transduction with mTOR Antibodies

Thursday, June 21, 2012 - 13:00

The protein encoded by mTOR (mammalian target of rapamycin), also known as dTOR in Drosophila, belongs to a family of phosphatidylinositol kinase-related kinases. These kinases regulate fundamental processes of cell growth, proliferation, metabolism

, and migration. mTOR is the target for the cell-cycle arrest and immunosuppressive effects of the drug rapamycin. Deregulation of mTOR stimulates an environment favorable for tumor development and progression. mTOR knockout mice are embryonic lethal. Using mTOR antibodies, researchers have shown that mTOR is required for the maturation and differentiation of multiple cell lineages in a mouse knock-in system (1).

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Ku70/Ku80 Antibodies: Becoming Major Players in DNA Repair and Immune System Research

Wednesday, June 20, 2012 - 07:00

Originally identified as autoantigens from a Scleroderma Polymyositis Syndrome patient (1), the Ku protein family consists of nuclear proteins found in eukaryotes. Autoantibodies to both Ku subunits were subsequently found in other autoimmune diseases such as Systemic Lupus Erythematosus. The Ku heterodimer complex consists of Ku70 and Ku80 and is a very versatile protein that regulates a wide range of important and diverse cellular pathways such as DNA repair and DNA replication, telomere maintenance and telomere silencing, chromatin structure, V(D) J recombination, and Bax-mediated programmed cell death through apoptosis.

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EZH2: Epigenetic Regulation Made Easy!

Tuesday, June 19, 2012 - 09:29

Enhancer of Zeste homolog 2 (EZH2) is the methyltransferase enzyme responsible for trimethylating lysine 27 on histone H3 to produce H3K27Me3. EZH2 is a polycomb group protein that is an essential epigenetic regulator that is often found deregulated in a wide variety of malignant cancer types. Using a KMT/EZH2 antibody, researchers have shown that EZH2 is a key regulator in B cell progenitor cells that  uses a novel mechanism of IgH rearrangement control not previously known1. Further KMT/EZH2 antibody studies showed that the phosphorylation of EZH2 by the protein kinase Akt suppresses EZH2 methyltransferase...

Understanding the Reasons for Histone H3 K4 Trimethylation (H3K4Me3)

Monday, June 18, 2012 - 10:17

Epigenetic mechanisms allow distinction between the active and inactive compartments of the genome, allowing proper cell lineage and embryogenesis. The trimethylation of Histone 3 at lysine 4 (H3K4Me3) is a common epigenetic histone modification that occurs in close proximity to nearly two-thirds of human gene promoters, and seems to balance another modification, trimethylation at lysine 27 (H3K27Me3). Researchers have created global histone methylation maps for human ES cells by using an H3K4Me3 antibody for ChIP (chromatin immunoprecipitation) coupled with paired-end ditags sequencing and found that these two modifications work in...

Novus Adiponectin Reagents Help to Progress Obesity & Diabetes Research

Friday, June 15, 2012 - 10:50

Adiponectin is most well-known for its role in glucose metabolism and fatty acid breakdown. Adiponectin is secreted solely by adipose tissue, and a person with a higher percentage of body fat will express lower levels of Adiponectin. When higher levels of Adiponectin are present, a mouse will show a lack of adipocyte differentiation and a measurable increase in energy expenditure. These factors are of high interest to people studying obesity and diabetes, such as my lab. When Leptin and Adiponectin are coupled, insulin resistance has been shown to be completely reversed in mice. Adiponectin has a direct correlation with diabetics; a diabetic will have much lower levels in their blood stream, and weight loss will increase these levels.

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Shades of Ghrelin in Weight Homeostasis

Thursday, June 14, 2012 - 16:48

The neuropeptide and gut hormone Ghrelin is an endogenous ligand for the growth hormone (GH)-secretagogue receptor (GHSR) within the central nervous system. This pathway has received a great deal of attention and heavy study within the last decade because of its large role in numerous physiological processes including feeding and body weight homeostasis (1, 2). In particular, Ghrelin is a key regulator of reward-based eating behavior (2, 3). Specifically, Ghrelin is derived from preproghrelin, which also generates another peptide called obestatin.

Immunoperoxidase of monoclonal antibody to GHRL

Obestatin is an endogenous ligand for the orphan G protein-coupled...

E-Cadherin in Cell-Cell Adhesion and Cancer Diagnostics

Tuesday, June 12, 2012 - 11:05

E-Cadherin is a member of the cadherin superfamily and is fundamental player in a wide range of cellular processes such as development, morphology, polarity, migration and tissue integrity. Specifically, E-cadherin is an approximately 100 kDa epithelial cell glycoprotein whose extracellular domain interacts with that of other E-cadherin molecules on adjacent cells to establish cell-cell adhesion. This adhesion is Ca2+-dependent and a variety of interactions have been identified. E-cadherin antibodies have been extensively used in meta-analysis studies and systematic reviews to validate E-cadherin expression as a prognostic indicator and/or marker for breast cancer (infiltrating ductal and invasive lobular types) 1. A related breast cancer study found that immunohistochemistry with E-cadherin antibodies was helpful in...

Connexin: Bridging the Gap of Intercellular Communication

Monday, June 11, 2012 - 09:03

Connexin 43/GJA1 is a member of the connexin gene family and the most abundant protein component found within gap junctions. Gap junctions are the cell-to-cell contacts that provide direct intercellular communication between cells by regulating back and forth diffusion of low molecular weight molecules. As such, they regulate quite an extensive range of key cellular processes. Connexin 43/GJA1 antibodies are important tools in wound healing studies, as connexin expression changes dramatically in the skin during different stages of wound healing (1, 2). Clinical trials exploiting connexins as the newest and latest promising target for skin wound healing are ongoing (3).  Connexin 43/GJA1 has far-reaching potential therapeutic uses in other tissue and cell types.

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Transferrin: "Ironing" out the Details of Cellular Anemia

Friday, June 8, 2012 - 12:18

Transferrin is a protein found in the blood plasma, a glycoprotein that is specific for controlling free iron in the bodies' biological fluids. Transferrin has two binding sites that are specific for very tight and reversible iron binding. The binding of iron to transferrin can be related to pH levels, among other things, with a high binding affinity for a more acidic pH and decreasing levels as the blood pH becomes more basic. This binding affinity is the basis for the transport mechanism of Transferrin. When the protein, attached to iron, encounters a cell with a transferring receptor, it is transported in a vesicle. While traveling in the vesicle, the pH is reduced by hydrogen ion pumps to a more basic level, around 5.5, causing Transferrin to release the iron ions. The receptor is then transported via vesicle back to the cell surface, and the whole process repeats itself.

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TrkB: Docking for Neurotrophins and Beyond.

Thursday, June 7, 2012 - 14:03

Tropomyosin receptor kinase B (TrkB) is a member of the Trk receptor tyrosine kinases family consisting of TrkA, TrkB and TrkC. The sequence of these family members is highly conserved. TrK's are activated by several neurotrophins, which are small protein growth factors that play a role in survival and differentiation of distinct cell populations. Neurotrophins, particularly brain-derived neurotrophic factor (BDNF), are key molecules regulating neuronal survival, development, function and plasticity. BDNF binding to its receptor, TrkB, results in receptor dimerization and autophosphorylation in the kinase domain, followed by activation of various signaling pathways. Western blotting analysis of rat hippocampus using anti-TrkB antibodies revealed activation of TrkB upon external stimuli (1).

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SREBP2: From Cholesterol Homeostasis to Cancer Invasion

Wednesday, June 6, 2012 - 09:31

Sterol-regulatory-element-binding protein 2 (SREBP2) is a transcription factor that regulates cholesterol homeostasis by controlling enzymes involved in cholesterol synthesis and uptake, e.g. HMG-CoA. Along with another transcription factor LXR, SREBP2 modulates expression of the transmembrane protein ABCA1, which is responsible for managing cellular cholesterol efflux. ABCA1 mediates transport of lipids between the Golgi body and plasma membrane, as well as cholesterol and phospholipid efflux to the ApoA1 and ApoE apolipoproteins in the formation of...

Using CD31/PECAM1 Antibodies as Reliable Endothelial Cell Junction Markers

Tuesday, June 5, 2012 - 09:11

Platelet Endothelial Cell Adhesion Molecule 1 (PECAM1), also known as known as CD31 (cluster of differentiation 31), is an Ig supergene family cell adhesion and signaling membrane receptor. CD31/PECAM1 is critical for cell-cell interactions and is expressed on a variety of hematopoetic cells (platelets, granulocytes, monocytes/macrophages, dendritic cells, and T and B cell subsets). Because this adhesion molecule is expressed at high levels specifically localized to endothelial cell junctions, CD31/PECAM1 antibodies can be used as endothelial markers1.

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PCNA is a Universal Marker of Proliferating Cells

Monday, June 4, 2012 - 10:03

Proliferating cell nuclear antigen (PCNA) is an evolutionarily well-conserved protein found in all eukaryotic species as well as in Archaea. PCNA was first shown to be involved in DNA replication. However PCNA functions are associated with other vital cellular processes such as chromatin remodeling, DNA repair, sister-chromatid cohesion and cell cycle control as well (1). PCNA is considered to be a marker of cell proliferation in various cancers. Immunohistochemical staining using PCNA antibody was performed on skin from patients with various malignant and nonmalignant skin diseases.


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Nucleolin: To the Nucleus and Beyond!

Thursday, May 31, 2012 - 09:40

Nucleolin is a multifunctional phosphoprotein ubiquitously distributed in the nucleolus, nucleus and cytoplasm of the cell. Nucleolin has a bipartite nuclear localization signal sequence and is conserved across the species. Nucleolin levels are expressed in abundance in exponentially growing cells and it regulates various aspects of DNA and RNA metabolism, chromatin structure, rDNA transcription, rRNA maturation, cytokinesis, nucleogenesis, cell proliferation and growth (1). Studies carried out to investigate the role of nucleolin in proliferating human cells using siRNA and subsequent detection of nucleolin levels by anti-nucleolin antibodies demonstrated the importance of nucleolin in cell proliferation and regulation (2).

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The Myc Epitope Tags Along...

Tuesday, May 29, 2012 - 10:25

Recombinant DNA technology allows researchers to fuse epitope tags to their protein of interest and then identify that protein using tag specific antibodies. The Myc Tag can be used to purify tagged proteins by affinity chromatography or detect them by immnoflorescence, immunoprecipitation and by Western blotting assays. The presence of the Myc Tag also introduces a mechanism whereby the use of radioisotopes can be avoided; relying instead on the identification of newly synthesized proteins using Western blot technology.

Western Blot: c-Myc Antibody

In vivo overexpression of proteins is a powerful...

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