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Antibody News

TRIF/TICAM1 and mitochondrial dynamics in the innate immune response

Friday, August 26, 2016 - 13:10

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 - 08:49

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 - 14:15

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 - 14:24

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 - 11:16

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 - 14:56

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 - 09:17

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 - 14:49

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).

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FANCD2 and DNA damage repair

Friday, July 22, 2016 - 13:30

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.  

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

Wednesday, July 20, 2016 - 11:39

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...

Cluster of Differentiation 3 (CD3) (OKT3 clone) 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...

The affects of Perilipin 2 on diet and metabolism

Monday, June 27, 2016 - 14:51

Perilipin 2 belongs to the Perilipin family, which consists of proteins that coat intracellular lipid storage droplets. Perilipin 2 in particular is involved in lipid globule surface membrane composition, and has also been implicated in the development and maintenance of adipose tissue. Contrary to previous findings, Perilipin 2 is found in a variety of cells aside from adipocytes, ranging from fibroblasts to skin cells. Overall, perilipins regulate cellular lipid metabolism and homeostasis.  On the contrary, excess lipid stores are linked to both exercise and obese conditions.  Maintaining the correct balance of lipid storage is very important to avoid lipocytotoxicity and is the focus of obese and metabolism related pathologies. 

Perilipin 2 antibody

Perilipin-2/ADFP Antibody [NB110-40877] -...

Synapsin I: Implicated in synaptic activity across a diverse range of studies

Wednesday, June 22, 2016 - 11:29

Synapsins are a family of neuronal proteins that are most renowned for their activity in modulating the pre-synaptic terminal.  Synapsin’s behavior is regulated by protein kinases and phosphatases, which alter the way that synapsin’s interact with actin filaments and other nearby proteins.  There are three isoforms of Synapsin – Synapsin I, II and III.  Synapsin I specifically localizes to the membrane of presynaptic vesicles and plays a role in regulation of axonogenesis and synaptogenesis. Mutations in Synapsin I have been associated with X-linked disorders with primary neuronal degeneration and epilepsy. 

Federici et al used a Synapsin I antibody (Cat# NB300-104) as a biomarker in their study on depression of synaptic dopamine release with cocaine and methylphenidate use.  The Synapsin I antibody was used in western blot to follow the effects of...

FOXP3

Monday, June 20, 2016 - 11:52

Is has been established that the regulatory transcription factor FOXP3 (a member of the forkhead/winged-helix family of transcription factors) is imperative to immune system homeostasis through CD4+CD25+ regulatory T cell function.  Distinctively, FOXP3 binds to specific regions of DNA to modulate the activity of genes that are involved in regulating the immune system.  Interruption of FOXP3 activity leads to autoimmune disorder, due to Treg cells not having their full ability to act as an immune system balancer.

However, it has also been shared that FOXP3 is also expressed and correlated to a number of cancer tissues. This does not come as a surprise, given that FOXP3 regulates a broad spectrum of target genes through histone modifications of target promoters.  The FOXP3 locus itself has CpG dinucleotides that are methylated in naïve CD4/CD25 T cells, activated CD4 T cells, and TGF induced adaptive Tregs.  Now, the FOXP3...

Analysis of Total & pSer724 IRE1 alpha, the Sensor of ER Stress

Friday, June 17, 2016 - 13:01

Inositol-requiring protein 1/IRE1 alpha (also called Endoplasmic Reticulum to Nucleus Signaling 1/ERN1; predicted mol wt 110 kDa) is a serine-threonine protein kinase/endoribonuclease which plays a highly critical role in unfolded protein response/UPR signaling, a mechanism by which eukaryotic cells sense and deal with ER stress. The latter triggers growth arrest and apoptosis in cells with misfolded proteins. ER stress is initiated by three different ER-resident proteins: PERK (PRKR-like ER kinase), ATF-6 (activating transcription factor 6), and IRE1 Alpha, but the signaling mediated by IRE1 Alpha is the most conserved mechanism of UPR/ER stress in eukaryotes. IRE1 Alpha is expressed as a type-1 transmembrane protein in the ER and it has bifunctional cytosolic kinase as well as RNase domains....

The role of TLR4 in breast cancer

Wednesday, June 15, 2016 - 11:40

Toll like receptors (TLRs) are highly conserved proteins that are first known for their role in pathogen recognition and immune response activation.  In order to elicit the necessary immune response in reaction to a foreign pathogen, TLRs trigger cytokine production depending on the behavior patterns of the pathogen itself.  Specifically, TLR4 acts through bacterial lipopolysaccharide (LPS), which composes the outer wall of Gram-negative bacteria.  Bacterial LPS is also a potent activator of the immune system.  Essentially, LPS is a ligand to TLR4, which in turn interacts with myeloid differentiation protein 2 (MD-2), CD14 and LPS-binding protein (LBP), which exist in the extracellular space.  This interaction turns on a signaling cascade that leads to the production of the required cytokines to trigger an effective immune response. 

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Using SCP3/SYCP3 Antibodies as Meiosis Markers in Gametogenesis and DNA Repair Studies

Monday, June 13, 2016 - 11:08

The synaptonemal complex (SC) is a protein structure that forms during the synapsis of homologous chromosomes during meiosis. This structure is involved in the processes of chromosome synapsis, genetic recombination and subsequent chromosome segregation, and is essential for gametogenesis.

The SC is comprised of three component proteins SYCP1, SYCP2, and SYCP3. SYCP1 functions in SC assembly, meiotic recombination, and XY body formation (de Vries et al., 2005). SYCP2 is required for synaptonemal complex assembly and chromosomal synapsis (Yang et al., 2006). Synaptonemal complex protein 3 (SCP3/SYCP3) is an essential structural component of the SC lateral complex (Alsheimer et al., 2010). Mutations in the SYCP3 gene have been linked to azoospermia in males and recurrent pregnancy loss in females (Sazegari et al., 2014), suggesting it plays a critical role in proper gametogenesis.

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Synapsin I, a pre-synaptic marker

Wednesday, June 8, 2016 - 14:40

Synapsin-I, also called Synapsin 1/Syn1, is an ~80 kDa protein (predicted mol. wt. 74.1 kDa) which belongs to the Synapsin family (Synapsin I, Synapsin II, Synapsin III). Synapsins are the evolutionarily conserved phospho-proteins which are associated with the cytosolic side of the synaptic vesicles. They tether the vesicles to the actin cytoskeleton, thus forming a reserve pool. Synapsins I and II are generally found in mature synapses, whereas, Synapsin III is typically expressed in developing synapses with a relatively lower expression. Synapsins represents the most abundant of neuron-specific phospho-proteins, consisting of 9% of the total amount of all vesicle proteins in neurons wherein they play a critical role in the regulation of neurotransmitter release (Greengard et al. 1993)....

The diverse functions of RANKL/TRANCE/TNFSF11

Monday, June 6, 2016 - 11:39

RANKL (also known as TNF-related activation-induced cytokine), or receptor activator of nuclear factor-κB ligand, was first discovered as a key player in the RANKL/RANK/OPG osteoclast formation pathway. Osteoclasts are large multinucleate cells that absorb bone tissue throughout growth and healing cycles.  Osteoclasts express RANKL, which in turn binds to the RANK receptor to regulate osteoclast differentiation.  In healthy bone formation, dynamics shift between new bone formation and existing bone reabsorption, resulting in an important equilibrium that results in osteoporosis or other bone pathologies if disrupted.  Specifically, overstimulation of RANKL activity has been linked to osteoporosis, osteopetrosis, arthritis and additional bone malignancies. 

trance antibody

In the presence of Recombinant Mouse M-CSF (20 ng/mL, Catalog...

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