Novus Biologicals Blog

Integrin beta 1 binding protein 2

September 19th, 2014

ITGB1BP2 is a muscle-specific protein cloned by a rat created by Branccio’s group in Italy that was found to interact with the cytoplasmic domain of integrin beta 11. It is expressed only in heart and skeletal muscle but is not essential for normal development and differentiation of these tissues. Branccio’s group published a follow-up study in Nature Medicine using an ITGB1BP2 antibody that the protein plays a critical role in sensing mechanical stress due to pressure overloading2. This response protects against subsequent compensatory dilated cardiomyopathy and contractile dysfunction. Further work from this group confirmed that ITGB1BP2 nucleotide variations are found in families of patients with hypertension and/or primary dilated or hypertrophic cardiomyopathy3.

Immunocytochemistry/Immunofluorescence: ITGB1BP2 Antibody

Immunocytochemistry/Immunofluorescence: ITGB1BP2 Antibody

Gu et al believe that altered ITGB1BP2 expression and signaling parallels the recovery of cardiac function (or lack of it) after myocardial infarctions (MI) and can be measured as one component in a profile panel of remodeling markers4. A recently submitted grant5 suggests that used a monoclonal ITGB1BP2 antibody for western blot to show test the functional activity of recombinant melusin. IGB1BP2 activates the downstream AKT and ERK signaling pathways by acting as a chaperone and binding to the Hsp90 machinery.

Novus Biologicals offers ITGB1BP2 reagents for your research needs including:


  1. 10506186
  2. 12496958
  3. 20017903
  4. 2154627
  5. US8658598 B2

Beta III tubulin

September 18th, 2014

The Beta III tubulin protein is abundantly present in both the central and peripheral nervous systems (CNS and PNS), where it is predominantly expressed during fetal and postnatal development. In cerebellar and sympathoadrenal neurogenesis, Beta III distribution is neuron-associated and present in distinct temporal-spatial gradients that are dictated by the regional neuroepithelia of origin. In addition, CNS subventricular zones consisting of neuronal and glial precursor cells exhibit transient beta III expression, where it may enable the identification of presumptive neurons derived from embryonic stem cells. In contrast, Beta III distribution is almost exclusively neuron-specific in adult tissues. Researchers published in Cell share their findings that the receptor tyrosine kinase Ret is required for motor axon attraction by integrating diffusible- and contact-axon guidance signaling in a hierarchical GPI-receptor signaling system1.

Immunocytochemistry/Immunofluorescence: Tubulin Beta 3 Antibody

Immunocytochemistry/Immunofluorescence: Tubulin Beta 3 Antibody

Their experiments with the Beta III tubulin antibody allowed them to construct a network from combinatorial components. Rudenko’s group from NIH used the Beta III tubulin antibody in their aging studies centered on the role of autosomal-dominant missense mutations on the multidomain leucine-rich repeat kinase 2 (LRRK2) that contains both kinase and ATPase activity2. They determined that the G2385R variant is a partial loss-of-function mutant in Parkinson’s disease (PD) that appears to be kinase-activating-independent. Immunoblotting and immunohistochemistry studies with the Beta III tubulin antibody performed in the Yoo lab focused on the chronic effects of pyridoxine vitamin B6 on forebrain ischemic damage and subsequent neuroblast differentiation3.  Using the Beta III tubulin antibody, Ghod’s group examined the role of the anti-inflammatory drug dimethylfumarate (DMF) on proliferation, apoptosis, and differentiation in glioma models4. They found DMF to be promising as a new treatment modality for brain tumors. The Beta III tubulin antibody allowed Kong et al to monitor the effects of chronic exposure to low doses of methylmercury on adult rat somatosensory cortexes5. Their comparative proteomic studies demonstrated the induction of a state of metabolic deficit.

Novus Biologicals offers Tubulin Beta 3 reagents for your research needs including:


  1. 22304922
  2. 22612223
  3. 22228142
  4. 24404403
  5. 23984759

CD19: An Undoubted Biomarker for B Cells

September 17th, 2014

CD19 is a cell surface protein member of the large immunoglobulin superfamily that complexes with CD21, CD81, and CD225 in the membrane of mature B-cells. A major function of CD19 is to assemble with the antigen receptor of B-lymphocytes to decrease the threshold for receptor-dependent stimulation, thus enhancing the specificity and sensitivity of B-cells towards antigens. CD19 plays a large role in regulating B-cell growth. Its expression is confined to only B-lymphocytes and follicular dendritic cells of the hematopoietic system. Leukemia phenotype studies suggest that CD19 is the earliest and broadest B-cell restricted marker. Because increased CD19 expression stimulates autoantibody production, CD19 studies provide insight into the autoimmunity process.

Immunohistochemistry: CD19 Antibody

Immunohistochemistry: CD19 Antibody

Defects in CD19 cause hypogammaglobulinemia. As reviewed by Gold et al, a key step in B-cell receptor (BCR) signaling involves using CD19, Cbl, Gab1 and Gab2 as docking proteins to recruit PI3K to the plasma membrane through Src homology (SH) domains1. Because most B-cell malignancies express CD19, much research is focused on new therapies for these malignancies that do not respond to standard therapies. The latest studies are focused on the development of chimeric antigen receptor (CARs) – fusion proteins that are hybrids of antigen recognition moieties and T-cell activation domains, as reviewed in Kochenderfer’s paper from the NIH2. Experiments with the CD19 antibody from Ogembo’s lab examined the regulation of RBC-pathogen clearance and filtration of altered self3. They embarked on a marker characterization of the littoral cell (LC) found within the venous sinus-lining of the red pulp within the spleen. Their profiling compared humans and closely related primates and they were able to identify SIRP alpha (CD172a) and FHOD1 as unique markers to humans.

Novus Biologicals offers CD19 reagents for your research needs including:


  1. 11043767
  2. 23546520
  3. 22490440

Glucose-6-phosphatase (G6PC) – A key to regulate your blood sugar level!

September 16th, 2014

The integral endoplasmic reticulum membrane-based enzyme G6PC hydrolyzes its substrate glucose-6-phosphate into glucose. Specifically, G6PC breaks down D-glucose 6-phosphate to D-glucose and orthophosphate. Because G6PC forms with the glucose-6-phosphate transporter (SLC37A4/G6PT), the resulting complex is responsible for glucose production. Thus, G6PC is the key enzyme in glucose homeostasis, functioning in both the processes of gluconeogenesis and glycogenolysis. Defects in the enzyme cause glycogen storage disease type I (von Gierke disease). Not surprisingly, G6PC is localized mainly in the liver and kidneys.  It is unique in that it is membrane-bound, unlike most other enzymes that act upon water soluble substrates.

Immunohistochemistry-Paraffin: G6PC Antibody

Immunohistochemistry-Paraffin: G6PC Antibody

An overview of the G6PC system including discussions of its regulation by glucose, insulin, cAMP, and glucocorticoids can be found in van Schaftingen’s review article1. Banka and Newman have more recently presented a clinical and molecular review on G6PC mutations and their physiological manifestations and links to various diseases2. Cicherchi et al employed the G6PC antibody to help them document the downstream effects of uric acid-dependent inhibition of AMP kinase (AMPK) in diabetes and starvation through an evolutionary standpoint3. Their data shows that an uricase mutation dating back 1.5 x 107 yrs ago to the hominid Miocene period (and triggered by a widespread famine period in Europe) when expressed in modern cell lines, likely conferred a survival advantage. This adaptation helped human ancestors to maintain critical glucose levels under situations of near-starvation, but in modern times, only serves to feed diabetes and insulin resistance.

Novus Biologicals offers G6PC reagents for your research needs including:


  1. 11879177
  2. 23758768
  3. 24755741

Von Willebrand Factor: An important mediator and carrier of hemostasis

September 11th, 2014

Human Von Willebrand Factor (factor VIII R: Ag) is a 270 kDa multimeric plasma gylcoprotein. Important in the maintenance of hemostasis, it mediates platelet adhesion to injured vessel walls and serves as a carrier and stabilizer for coagulation factor VIII. The Von Willebrand factor has functional binding domains to platelet glycoprotein Ib, glycoprotein IIb/IIIa, collagen and heparin. The factor is synthesized by endothelial cells and is also present in platelets and megakaryocytes.

The essential biologic properties of VWF have been explicated, particularly in the areas of genetic regulation, biosynthesis, and specific bimolecular interactions. The three-dimensional structure of selected domains has been solved, but our understanding of detailed structure-function relationships is still fragmented because of the complexity and size of the VWF molecule. The biomechanical properties of the interaction between the VWF A1 domain and the platelet receptor glycoprotein (GP) Ib alpha are better known, but little is known how this adhesive bond can oppose the fluid dynamic effects of rapidly flowing blood to initiate thrombus formation and contribute to platelet activation. Developments in these areas of research will lead to a more satisfactory definition of the role of platelets in atherothrombosis and better understanding of the role played by VWF in vascular biology and pathology. (1)

Mutations in this gene or deficiencies in this protein result in Von Willebrand’s disease. VWD is characterized by frequent bleeding (gingival, minor skin quantitative lacerations, menorrhagia, etc.).  Some findings have been obtained on the link between regulation of VWF multimer size and microvascular thrombosis. This progress in basic research has provided critical information to define with greater precision the role of VWF in vascular biology and pathology, including its possible involvement in the onset of atherosclerosis and its acute thrombotic complications. (2)

Shi’s group employed Novus Von Willebrand Factor Antibody [FITC] Endothelial Cell Marker, NB120-8822, in a study that highlights the beneficial influence of nanotopography on the differentiation of Adipose-derived stem cells (ADSC) into endothelial cells which play an important role in vascularization. (3)

Novus Biologicals offers Von Willebrand Factor reagents for your research needs including:


  1. 15662611
  2. 12871266
  3. 22628362

TdT (Terminal Deoxynucleotidyl Transferase)

September 8th, 2014

The enzyme family of DNA polymerases plays a fundamental role in the replication, repair, and recombination of nucleic acid. Its members include DNA Polymerase b (Pol b), DNA Polymerase g (Pol g), and DNA Polymerase m (Pol m). TdT is a very unique and fascinating member of this family because, unlike all other DNA polymerases, TdT synthesizes DNA from only single-stranded DNA. This unusual ability to work in a completely template-independent manner was discovered early on (TdT was one of the first activities found in mammals) but not well understood1. An excellent summary of the history, structure, and function of TdT can be found in Motea and Berdis’ review2. It is now evident that such random nucleotide addition allows V(D)J recombination and therefore drives the evolution, flexibility, and diversity of the vertebrate immune system.

Immunocytochemistry/Immunofluorescence: TdT Antibody

Immunocytochemistry/Immunofluorescence: TdT Antibody

Without TdT, the body could not generate the sophisticated multitude of immunoglobulins and T-cell antigen receptors required for innate immunity as demonstrated by McElhinny’s group3. TdT expression is specifically limited to primary lymphoid tissues such as the thymus and bone marrow4,5.  There is an accumulated body of data to suggest that changes in TdT expression and activity modulate cancer initiation, tumor progression, and chemotherapy response. For example, it is overexpressed in ALL and AML (reviewed by Motea). Additionally, it appears to be an efficient method for labeling double-stranded DNA breaks both in vivo and in vitro through assays such as TUNEL.

Novus Biologicals offers TdT reagents for your research needs including:


  1. 13802334
  2. 2846215
  3. 15242391
  4. 2937062
  5. 11861602

MUL1 – A Mito’s best friend

September 4th, 2014

MUL1 is an E3 ubiquitin-protein ligase with a RING finger domain that controls mitochondrial morphology, fragmentation and localization. E3 ubiquitin ligases accept the component ubiquitin from a donor E2 ubiquitin-conjugating directly transfer this ubiquitin to designated targeted substrates. The largest, proteome-wide and site-specific quantitative mapping dataset assessment of endogenous putative ubiquitylation sites and regulation was executed by Wagner’s group in Denmark1.  Their compelling experiments also evaluated crosstalk between ubiquitylation and acetylation modifications using an MUL1 antibody. When overexpressed, MUL1 activates the JNK signal cascade and induces caspase-dependent apoptosis. MUL1 has also been shown to negatively regulate Akt kinase, suppressing cell proliferation and viability2.

Western Blot: MUL1 Antibody

Western Blot: MUL1 Antibody

Cilenti’s group used the MUL1 antibody in immunoblotting experiments investigating the Omi/HtrA2 protease3.  Omi/HtrA2 is a mitochondrial-specific serine protease with conflicting activity dependent on its subcellular localization – cytoplasmic release triggers apoptosis while inter-membrane space confinement produces a pro-survival activity. Cilenti’s used an MUL1 antibody in mutant mice to uncover a new stress-signaling pathway that starts in the mitochondria and could be a factor in motor neuron disease and premature aging.

Novus Biologicals offers MUL1 reagents for your research needs including:


  1. 21890473
  2. 22410793
  3. 24709290

SOX-11 seals your fate

September 3rd, 2014

The SOX-11 transcription factor is a member of the SOX family known to be involved in embryonic development regulation and cell fate determination. The protein acts as a transcriptional regulator and appears to modulate fundamental aspects of normal embryonic nervous system development and tumorigenesis. SOX-11 is not found expressed in adult tissues except for the adult immature neuron. Ek’s group in Sweden employed the SOX11 antibody to develop signatures comprised of mantle cell lymphoma (MCL)-associated genes through a comprehensive expression analysis of both normal and malignant B-cells1. These profiles were created to identify diagnostic and therapeutic targets that are efficient, genome-based modalities for this aggressive lymphoid malignancy. Additional studies that surveyed a wider range of lymphomas relied upon SOX11 antibody immunohistochemistry and widened the prognostic value of SOX-11 from MCL to also other lymphoblastic malignancies and Burkitt’s lymphomas2.

Immunohistochemistry-Paraffin: SOX11 Antibody

Immunohistochemistry-Paraffin: SOX11 Antibody

With the SOX11 antibody, Spanish researchers were able to define the molecular criteria to allow indolent, non-treatment-requiring forms of MCL to be identified through profiling of both genome and pathology3. Gustavsson et al used the SOX11 antibody to establish a key primary role for SOX-11 as a tumor suppressor in cellular growth4. This was done through extensive siRNA knockout and ectopic expression assays. This tumor suppressor role for SOX-11 was also validated in high-grade epithelial ovarian cancers (EOCs) by Sernbo’s group, who used the SOX11 antibody to evaluate survival and methylation-dependent silencing of SOX-11 by 5-Aza-dC 5. Such epigenetic-based drugs may be powerful anti-proliferative agents in SOX-11-negative tumors.

Novus Biologicals offers SOX11 reagents for your research needs including:


  1. 16524965
  2. 19880779
  3. 20124476
  4. 20624318
  5. 21943380