Antibody News

Altered expression of BCL2 in cancer

Friday, September 23, 2016 - 09:14

Similar to other cell processes, the balance between cell survival and cell death is an important equilibrium that when altered expression of genes can lead to a variety of disease.  For example, too little cell death can promote cell overgrowth and eventually cancer, whereas too much cell death can lead to neurodegeneration (among other things).  Bcl-2 in particular is a pro-survival protein that is part of the Bcl-2 family of proteins, consisting of Bax, Bid, PUMA, and Noxa.  While overexpression of Bcl-2 has rescued cells from certain toxic stimuli, such as hypoxia, of greater interest is its ability to prevent cell death during a chemotherapeutic treatment and its resistance to these drugs.  In fact, an upregulation of Bcl-2 family member proteins has been used as a light prognostic factor in diagnosing certain cancers.  Given this information, the use of Bcl-2 primary antibodies in research has been successful in elucidating...

The effect of antioxidants and the NFkB p65 pathway in inflammation

Tuesday, September 20, 2016 - 13:48

NFkB is a transcription factor that plays a role in the expression of genes involved in immune response, inflammation, metastasis, cell survival and more. RelA (p65) is one member of the NFkB mammalian family, alongside other subunits. NFkB subunits have recognition sites on the “Rel” homology domain, where they form protein complexes to bind DNA and regulate gene expression.  The RelA (p65) subunit also has an extended carboxy terminal that can act as a transactivator (a form of gene regulation that increases the rate of gene expression in response to stimuli).  The NFkB p65 subunit is thought to shuttle between the cytoplasm and the nucleus, however it is also shown to stay localized to the cytoplasm by its inhibitor, IKK beta.  Over the past ten years or so, introduction of antioxidants to inflammation or aging has had interesting response on a cellular level.  Given that the NFkB pathway regulates the levels of endogenous reactive oxygen species (ROS),...

Alpha-smooth muscle actin and the modulation of endothelial and epithelial cell biology

Friday, September 16, 2016 - 14:21

Actin is essential for a wide range of cell functions, ranging from cell division and chromatin remodeling to vesicle trafficking and maintenance of cellular structure. In fact, mislocalization of actin to cell junctions during development leads to facial malformations such as cleft lip.  Actin is successful in the regulation of a variety of cell functions due to its high number of isoforms.  One such isoform of actin is alpha-smooth muscle actin (alpha-SMA), which is plentiful in vascular smooth-muscle cells and plays an important role in fibrogenesis and fibrosis (the thickening of tissue). There are distinct phenotypes associated with a lack of alpha-SMA during and after development.  Studies have shown that mutated alpha-SMA during development results in disarray of cardiac muscles and intense muscle weakness in young rodent infants.  In adults, mutations in smooth muscle actin can lead to cardiac and blood pressure complications. 


Beta Tubulin III and neurogenesis

Thursday, September 15, 2016 - 13:29

Beta tubulin III, also known as Tuj-1, is a class III member of the beta tubulin protein family. Beta tubulins are one of two structural components that form our microtubule network. While general tubulins play a role in a wide range of cellular processes (mitosis, motility, etc) beta tubulin III is specifically localized to neurons.  In particular, beta III tubulin’s expression correlates with the earliest phases of neuronal differentiation.  For this reason, beta tubulin III has implications in neurogenesis, axon guidance and maintenance.  Since it was discovered that the human brain generates new neurons from stem cell pools, beta tubulin III has been used as a marker of positive neuronal activity in many research studies.  The following articles use a beta III tubulin antibody in their research of embryonic stem cell and neural progenitor activity. 


MMP-2: More Than a Cancer Marker

Friday, September 9, 2016 - 14:35

Matrix metalloproteinases (MMP) are a family of endopeptidases involved in the breakdown of extracellular matrix (ECM) during both normal physiological and disease processes. MMP-2 is a zinc-dependent family member that selectively cleaves collagen and elastin, major structural components of the basement membrane. In addition, MMP-2 has been found to affect a number of non-matrix proteins such as big endothelin-1 (Fernandez-Patron et al., 1999), KISS (Takino et al., 2003), GSK3B (Kandasamy et al., 2009), and CHUK (Olivotto et al., 2013). This diverse activity has led MMP-2 to be linked to a wide variety of physiological processes.

While most MMP members must be proteolytically activated after secretion, MMP2 may be activated while still on the membrane. Specifically, pro-MMP-2 can be activated either extracellularly by proteases, or intracellularly via S-Glutathionylation (Okamoto et al., 2001). Researchers have speculated that MMP-2...

Transferrin and the blood brain barrier

Wednesday, September 7, 2016 - 14:50

Transferrin, an iron binding protein that facilitates iron uptake in cells, is an integral part of a mechanism that may introduce antibody therapies to the central nervous system. Currently, the brain’s ability to take in antibody therapies is limited by the presence of the blood brain barrier. While novel mechanisms to manipulate the transfer of important proteins and antibodies across the BBB have been tested, endogenous receptor-mediated transcytosis (RMT) is one mechanism of particular interest.  Iron transfer is achieved when transferrin bound iron connects with the transferrin receptor, and iron subsequently enters the cell by way of clathrin-mediated endocytosis.  Once inside the cell, transferrin is trafficked to early endosomes, where the iron is dropped off.  After iron delivery, transferrin is directed to recycling endosomes to be brought back to the cell surface.  Using this pathway to deliver therapeutic antibodies across the BBB has shown both...

The relationship between Ki67 and HIF-1 in cancer

Friday, September 2, 2016 - 13:24

Ki67, also known as MKI67, is best known as the leading marker of cellular proliferation. Ki67 is regulated by a balance between synthesis and degradation, and often carries a very short half-life.  First discovered to be located to dividing cells, Ki67 has since been specifically localized to the G1, S, G2 and M phases of mitosis. Soon after, it was discovered that there was a high correlation of Ki67 alongside the p53 (tumor suppressing protein 53), suggesting an implication in cancer. What’s more, the expression of Ki67 is higher in malignant cells versus control cells. With this data, researchers are taking a closer look between the behaviors of Ki67 alongside proliferation in cancer cells.  In particular, the following articles use the Ki67 primary antibody when investigating the role of HIF-1 in different types of cancers.  Hif-1, or hypoxia inducing factor 1, controls our adaptive response...

Tools for Isolation, Quantification and Analysis of Exosomes

Tuesday, August 30, 2016 - 15:58

Exosomes are spherical to cup-shaped bilayered membrane enclosed nanosize vesicles (30-100 nm) which have the ability to shuttle active cargoes between cells. Johnstone et al. 1987 pioneered in documenting the generation of exosomes in differentiating reticulocytes as a result of the fusion of multi-vesicular endosomes/MVBs with the plasma membrane. However, later studies established that exosomes are actively secreted by almost all types of cells through the process of exocytosis and that exosomes can be found in most of the body fluids (blood, saliva, semen and urine). Structurally, exosomes contain various types of biomolecules (lipids, proteins, DNA, RNA etc.) from the parent cells, and the bacterial/viral proteins or nuclear acids in infected cells. Exosomes act as signalosomes and facilitate intercellular communication through delivering bioactive molecules (Tran et al. 2015)


TRIF/TICAM1 and mitochondrial dynamics in the innate immune response

Friday, August 26, 2016 - 13:09

TRIF, also known as toll like receptor adaptor molecule 1 or TICAM1, is known for its role in invading foreign pathogens as part of our innate immune response. TRIF/TICAM1 is a TIR-domain adaptor protein (toll/interleukin-1 receptor) that interacts with the Toll-like receptors (TLRs) through intracellular signaling and recognition of its TIR site.  TLRs are expressed on a variety of cell types, including macrophages, mast cells, endothelial cells, and more.  In addition to TRIF/TICAM1, another universal adaptor for TLRs is myeloid differentiation factor-88 (MyD88).  The activation of both MyD88 and TRIF/TICAM1 results in subsequent activation of the nuclear factor kappa beta pathway (NF-κB). The NF-κB then influences a large range of biological processes, including immunity, inflammation and stress response.  One way that TRIF/TICAM1 defends a host from foreign pathogens is to initiate autophagy or apoptosis in order to clear the intracellular space from these particles...

The identification of dopaminergic neurons using Tyrosine Hydroxylase in Parkinson's research and LRRK2

Thursday, August 25, 2016 - 08:48

Tyrosine hydroxylase (TH) is a crucial enzyme involved in the biosynthesis of dopamine, norepinephrine and epinephrine in the brain.  Specifically, TH catalyzes the conversion of l-tyrosine to l-dihydroxyphenylalanine (l-dopa).  The importance of tyrosine hydroxylase was established early on in when Zhou et al found that TH deficient mice had a lethal phenotype.  While TH is vital to neurotransmitter and neural hormone development, mutations in TH are not solely responsible for Parkinson’s disease (PD).  In fact, mutations in the LRRK2 gene and marked loss of dopaminergic neurons in the substantia nigra are the hallmark signs of PD. However, mutations in TH lead to dystonia DOPA-responsive autosomal recessive disorder, also known as autosomal recessive Segawa syndrome. Using a TH antibody in Parkinson’s research is an effective and popular way to monitor...

Epithelial-Mesenchymal Transition (EMT) Markers

Thursday, August 18, 2016 - 14:17

Epithelial-Mesenchymal Transition (EMT) is the trans-differentiation of stationary epithelial cells into motile mesenchymal cells. During EMT, epithelial cells lose their junctions and apical-basal polarity, reorganize their cytoskeleton, undergo a change in the signaling cascade that defines cell shape and reprograms gene expression. Collectively, these changes increase the motility of individual cells and enables the development of an invasive phenotype. At the molecular signaling level, EMT is regulated through several pathways which are triggered by TGF-beta, HGF, EGF, FGF, VEGF, Wnt, SHH, IL6, HIF1 alpha, and other proteins. At the transcription level, SNAI1/Snail, ZEB1/ZEB2 and basic helix-loop-helix transcription factors (bHLH) drive EMT progression. Accumulating evidence has established involvement of EMT in several biological processes including (but not limited to) embryonic and post-embryonic development, tissue regeneration/wound healing, stem cell...

The role of Smoothened in pulmonary pathologies

Monday, August 15, 2016 - 14:23

The Hedgehog (Hh) family of secreted proteins is involved in a number of developmental processes, one of which is the development of cancer. Past data suggests that the Sonic hedgehog (Shh) receptor is composed of two transmembrane proteins, Patched and Smoothened.  The Hedgehog (Hh) signaling pathway is vital to the development of many tissues during embryogenesis, however, it also has an important role after development.  After development, Hh signaling regulates stem cells and their regenerative function.  When the Hh pathway is awry, signaling may turn oncogenic in nature. This has been witnessed in interactions between Patched and Smoothened, where Patch inhibits the function of Smoothened.  When normal Smoothened activity is restricted or mutated, it can cause unregulated activation of the Hh pathway which leads to cancer.  This post will delve into research using a Smoothened antibody to further elucidate its role...

The recent relationship of BRCA1 and 53BP1

Friday, August 12, 2016 - 11:14

The p53-binding protein 1 (53BP1) is a DNA damage response factor, which is recruited to nuclear structures at the site of DNA damage.  DNA double-strand breaks (DSBs) are mutations that are detrimental to cell viability and genome stability, and must be repaired either through homologous recombination (HR) or non-homologous end joining (NHEJ). 53BP1 specifically promotes both NHEJ as well as the inhibition of HR repair, yet the decision making on a molecular level between these two routes not clearly understood. Recently, a focus has been placed on 53BP1 and the breast cancer gene BRCA1, given that BRCA1 is also an important mediator of our DNA damage response, partially by antagonizing 53BP1 dependent NHEJ.  The following studies take a closer look at the relationship with 53BP1 and BRCA1

Zhang et al introduced the hypothesis that a cell cycle dependent BRCA1-...

The effects of ethanol consumption on glutamate production and xCT

Monday, August 8, 2016 - 14:03

xCT is a sodium independent glutamate transporter that regulates the exchange of extracellular l-cystine and intracellular l-glutamate across the plasma membrane. This process is critical to glutathione production and protection from subsequent oxidative stress. Aside from its standard function, xCT participates in a variety of central nervous system (CNS) functions, including formation of the blood–brain barrier, involvement in drug addiction pathways, neurodegeneration caused by lack of oxidative stress protection, and more.  xCT is primarily localized to neurons and glia in the CNS, which is considering its role in glutathione production and efficacy, given that there are an abundance of enzymes and metabolites that can generate reactive oxygen species in these areas.

xct antibody

xCT Antibody [...

The role of DNMT3B in the co-incidence of methyltransferase and tumor suppressor expression in malignancies

Thursday, August 4, 2016 - 15:18

Epigenetics is the process of heritable change in gene activity despite alteration of the hosts DNA sequence, essentially causing a change in a phenotype without a change in the genotype of a host. To change the gene sequence without interfering with the DNA is accomplished by histone and DNA methylation.  Gene silencing in DNA methylation is carried out by DNA methyltransferases 1, 2 and 3a/b (DNMT1, DNMT2, DNMT3A/B). On a broad level, DNMT’s methylate the fifth carbon of cytosine residues in DNA within CG dinucleotides. However, DNMT3B is required for genome-wide de novo methylation and is during development.  DNMT3B also specifically regulates DNA of nucleosomal DNA, however it can also act as a transcriptional co-repressor by associating with CBX4 in lieu of methylation. Studies on the structure of DNMT3 have revealed that DNMT3A and DNMT3B are highly similar in that they both contain a PWWP domain, a PHD-...

The role of DNMT3A in development

Tuesday, August 2, 2016 - 14:53

Epigenetics is the study of heritable change in gene activity despite alteration of the hosts DNA sequence.  Change in gene activity done independently of the DNA sequence is achieved by way of histone and DNA methylation.  Gene silencing in DNA methylation is carried out by DNA methyltransferases 1, 2 and 3a/b (DNMT1, DNMT2, DNMT3A/B). On a broad level, DNMTs methylate the fifth carbon of cytosine residues in DNA within CG dinucleotides. However, DNMT3 on its own is a de novo methyltransferase required for the establishment of genomic methylation patterns during development and reproduction. Studies on the structure of DNMT3 have revealed that DNMT3A and DNMT3B are highly similar in that they both contain a PWWP domain, a PHD-like ADD domain and a catalytic domain. What’s more, the catalytic activities of DNMT3A and DNMT3B have been shown to be attracted to...

Niemann Pick-C1 and cholesterol dynamics

Friday, July 29, 2016 - 09:16

Niemann-Pick type C1 (NPC1) mediates low-density cholesterol transport from late endosomes and lysosomes to other areas of the cell via receptor mediation endocytosis.  Although cholesterol moves freely inside the cell, it cannot independently export out of the lysosome, which is where NPC1 steps in. After NPC1 interacts with lipoproteins and removes or delivers them to their destined compartments, they are hydrolyzed and released as free cholesterol.  Mutations in the NPC1 gene cause Niemann-Pick type C disease, a rare autosomal recessive neurodegenerative disorder characterized by over accumulation of cholesterol in lysosomes and is characterized by both neural and liver degeneration.

Niemann Pick C1 antibody

Niemann-Pick C1 Antibody [NB400-148] - Staining of human...

Application Highlight: Recent uses of TERF2 in immunofluorescence (IF)

Monday, July 25, 2016 - 14:48

Telomeres are a region of repeat nucleotide sequences located at the end of chromosomes to protect our DNA from becoming damaged via end-to-end fusion.  TERF2, or telomeric-repeat binding factor 2, is important for telomere integrity and aids in the formation of the telosome, the telomeric loop, and control of the amount of DNA needed for telomere replication.  When TERF2 is down regulated, an induction of apoptosis and senescence is also witnessed.  TERF2 also interacts with an abundance of proteins in all of the above pathways, including RAP1, Apollo, TOP1, TOP2A and TOP2B.  The visualization of telomeres on chromosomal structures through immunofluorescence (IF) is an important diagnostic tool and is examined more closely in the following research projects using a Novus Biologicals TRF-2 Antibody (NB100-56506).


FANCD2 and DNA damage repair

Friday, July 22, 2016 - 13:28

Fanconi anemia (FA) is a genetically inherited disorder that yields cytogenetic instability, hypersensitivity to DNA crosslinking compounds and defective DNA repair. A variety of genes have been identified within the FA pathway that are referred to as the Fanconi anemia complementation group.  One member of this group, FANCD2, is monoubiquitinated in response to DNA damage.  At this point, FANCD2 specifically localizes to the nucleus to represent the site of DNA repair, often times to the DNA replication fork. In addition to monoubiquitination, FANCD2 can also be phosphorylated by the cell checkpoint kinases ATM and ATR.  Using a FANCD2 antibody to further elucidate the role of FANCD2 the DNA damage pathway is a popular approach to understanding DNA repair in a variety of experimental models.  


Tat-Beclin 1: The pioneering of an autophagy-inducing peptide

Wednesday, July 20, 2016 - 11:37

Autophagy is an essential process that maintains cellular homeostasis and carries out lysosome-mediated degradation of unwanted proteins in the cytoplasm.  Because of this regulatory function, autophagy is often examined when looking at disease pathways.  While our immune system initiates the removal of viruses and pathogens through the autophagic pathway, viruses, such as HIV, have developed a way to evade this process through inhibition.  Therefore, developing a reliable way to examine the molecular process of this inhibition and interaction is very desired.  The central autophagy protein, Beclin 1, became a quick target to create an autophagy manipulation factor and ultimately lead to the formation of an autophagy inducing peptide. Novus Biologicals carries three new isoforms of the Tat-beclin-1 peptide in the form of Tat-Beclin 1 D11 (NBP2-49888),...

MHC Class I and the Herpes Simplex Virus

Friday, July 15, 2016 - 14:41

MHC molecules (also known as major histocompatibility complex molecules) assist in the presentation of antigens to T cells in order to eradicate foreign pathogens.  These molecules are highly polymorphic, meaning that they exist in multiple variants in order to avoid pathogens evading their activation of the immune response.  MHC Class I molecules in particular deliver cytosolic peptides to the cell surface so that they can continue on through the cytosol and ultimately the endoplasmic reticulum (ER).  The mechanisms by which different viruses invade our immune system are dynamic and specific to the genetic composition of the virus.  An interesting virus in its process of immune evasion is the Herpes Simplex Virus Infection, given its ability to establish a lifelong cycle of dormant and active phases.  Using a MHC Class I antibody is an effective tool to examine different approaches at virus evasion in the following...

Interactions between CENPF and the additional kinetochore assembly proteins PinX1, PHB2 and Sgt1

Tuesday, July 12, 2016 - 12:58

Mitosis, the process of cell division, involves unique interactions between spindle microtubules and chromosomes, which are regulated by protein structures located on chromosomes known as kinetochores.  CENPF is a kinetochore-associated protein that is localized to chromatin during the G2 and M phases of mitosis.  The main role of CENPF is to secure kinetochore proteins to the correct location surrounding the chromatid and centromere for proper function. Specifically, microtubule-dependent motor proteins work alongside the kinetochores to generate tension and ultimately power chromosomal movement. Outside of its role in cell division, CENPF also has a role in the regulation of the plasma membrane through its association with SNAP25 (a vesicle associated membrane protein).  Research has implicated a wide variety of proteins as regulators of kinetochore and chromatin dynamics; however, this article will review how a...

TIM-3, a critical immune checkpoint in HIV research

Friday, July 8, 2016 - 11:47

CD4+ T-helper cells (Th) are the white blood lymphocytes expressing surface glycoprotein antigen CD4. These T-helper cells play an important role in the adaptive immune system by releasing T cell cytokines that help other immune cells to suppress or regulate immune responses. CD4+ T-helper lymphocytes can be divided into two types (Th1 and Th2) based on their cytokine secretion. Th1 cells are involved in cell-mediated immune response to intracellular pathogens and delayed-type hypersensitivity reactions. Th2 cells are involved in the immune response to extracellular infections and the promotion of allergic diseases.

T-cell immunoglobulin and mucin-domain containing-3 (TIM-3), also known as HAVCR2, is a Th1-specific cell surface protein that serves as an immune checkpoint by inhibiting the immune response. Specifically, TIM-3 regulates macrophage activation, inhibits auto- and...

CD3 (OKT3) as a marker of immune response efficiency

Tuesday, July 5, 2016 - 15:03

Our immune system is a powerful defense mechanism against infection, however different variables can cause our immune response to work for or against us.  CD3 (cluster of differentiation 3) is one component of our immune signal response that is composed of four distinct chains (CD3-g, CD3-e, CD3-s and the zeta chain). These chains associate with a molecule known as the T-cell receptor (TCR) to comprise the TCR complex. Broadly, CD3 is expressed in pro-thymocytes (stem cells where T cells arise in the thymus) in order to mediate signals that are critical for T cell development and function in response to foreign pathogens.

The CD3 (OKT3 Clone) antibody (Cat# NBP2-24867) specifically reacts with an epitope on the epsilon subunit, which plays a vital role in the creation of new T cells.  OKT3 has been found to illustrate immunosuppressive properties and...

Nogo: A Promising Target for New Gene Therapies

Wednesday, June 29, 2016 - 15:31

Nogo is a neurite outgrowth inhibitor protein that plays an important role during central nervous system (CNS) development as well as in endoplasmic reticulum signaling regulation. Studies using Nogo antibodies have revealed Nogo proteins regulate precursor migration, neurite growth and branching in the developing CNS. In addition, Nogo serves as a negative regulator of neuronal growth in the adult CNS, causing wiring stabilization but greatly limiting any regeneration abilities (Schwab, 2010).

There are three Nogo isoforms; Nogo-A, Nogo-B and Nogo-C. Although Nogo-A was the first identified isoform and is the most widely studied, all three isoforms have shown significant potential as targets for a variety of new gene therapies.

A number of recent studies have shown that inhibition using...


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