June 17th, 2013
The biological importance of protein phosphorylation is underlined by the existence of 500 or more protein kinases within the human genome. In most cases, phosphorylation of serine residues creates binding surfaces for a variety of phospho-amino acid binding proteins. Phosphorylation is a key post-translational modification necessary for normal cell signaling and is a key player in cellular function. Phosphorylated proteins mediate cell division, differentiation, signal transduction and other key cell signaling processes.

Phosphorylation of serine residues on proteins is one of the key triggers to a cascade of reactions that follow and are of great interest to several researchers. Phosphorylation of several proteins within the cells and tissues at serine residues has been detected by Immunoflorescence, Immunochemistry and by western blotting using anti-Phosphoserine antibodies in several types of cancers (1), neurological disorders (2) and in several other chronic diseases (3). Phosphorylation of pathogenic proteins is a routine phenomenon that contributes to the disease process and hyper-phosphorylation of aberrant and pathological proteins at serine residues offers a viable strategy for therapeutic interventions.
- PMID: 17092701
- PMID: 19914335
- PMID: 22178943
Novus Biologicals offers various phosphoserine reagents for your products research needs including:
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June 14th, 2013
Synaptonemal Complex Protein 1 (SCP1) is a novel tumor antigen that belongs to the growing family of cancer/testis antigens (CTAs). CTAs are theoretically ideal targets for tumor immunotherapy. Unlike most auto-antigens, CTAs are highly immunogenic, even in the autologous cancer-bearing patients. Furthermore, because of their very restricted normal tissue expression, immunotherapy targeting CTAs is expected to be more specific and less toxic. These two theoretical properties of CTAs have arisen from the belief that, because they are testicular-specific, they are normally only expressed in the immune privileged testicles where there is an apparent lack of human leukocyte antigen (HLA) class I molecules on the surface of germ cells (1).

SCP1 has been shown to be expressed during the meiotic prophase of spermatocytes and is involved in the pairing of homologous chromosomes during meiosis. The aberrant expression of SCP1 in tumors might be a contributing factor to their genomic instability and suggests that the functional role of other CTAs (2). Expression of SCP1 in epithelial ovarian cancer (EOC) by IHC in paraffin-fixed EOC human samples and ELISA using anti-SCP1 antibodies revealed that 15 % of the primary tumors had elevated levels of SCP1, while SCP1 mRNA was found to be 14.3% (4/28) in nasopharyngeal carcinoma (3, 4). These observations suggest that SCP1 might be a new tumor target antigen of carcinomas. Further research on the exact role of SCP1 CTAs is warranted and is an open area of research.
- PMID: 18451240
- PMID: 9560255
- PMID: 15487888
- PMID: 17608150
Novus Biologicals offers various SCP1 reagents for your products research needs including:
Posted in Antibodies, Antibody catalog, Antibody database, Antibody suppliers, Cancer, Tumor, Uncategorized | No Comments »
June 13th, 2013
Niemann-Pick type C (NPC) disease is a severe cell lipidosis characterized by the accumulation of unesterified cholesterol in the endosomal/lysosomal system. It is a lysosomal storage disorder that affects the viscera and the central nervous system which is caused by the accumulation of cholesterol in lysosomes (1). Niemann-Pick disease type C1 has a highly variable clinical phenotype and clinical features include variable hepatosplenomegaly and severe progressive neurological dysfunction such as ataxia, dystonia and dementia (2).

In a recent study biochemical tests were done using brain and liver sub cellular fractions from mice using anti-NPC antibodies to determine whether NPC1 and NPC2 might have unrelated functions within the lysosome in addition to their roles in cholesterol transport. Results obtained highlighted biochemical alterations in the lysosomal system of the NPC-mutant mice that appear secondary to lipid storage (3). Endolysosomal processing of cholesterol and other lipids as a contributing factor to the progression of a variety of diseases is a growing area of research.
- PMID: 20525256
- PMID: 18832164
- PMID: 21887293
Novus Biologicals offers various Niemann-Pick C1 reagents for your products research needs including:
Posted in Antibodies, Antibody catalog, Antibody database, Antibody suppliers, Lipid & Metabolism, Uncategorized | No Comments »
June 12th, 2013
E-cadherin (also known as Arc-1, uvomorulin, and cell-CAM 120/80) is a calcium-regulated adhesion molecule expressed in most normal epithelial tissues and the loss of E-cadherin can cause dedifferentiation and invasiveness in several cancers (1). Loss of E-Cadherin expression correlated with the invasiveness of carcinoma (2). Carcinoma cell lines with an epithelioid phenotype were noninvasive and expressed E-cadherin suggesting a reciprocal relationship between levels of E-Cadherin expression and their invasiveness as detected by E-Cadherin antibodies (3).
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Reduced expression of E-cadherin by IHC has been observed in several aggressive tumors supporting the notion that E-cadherin is a classic tumor suppressor gene (4). Invasiveness of these latter cells could be prevented by transfection with E-cadherin cDNA and was again induced by treatment of the transfected cells with anti-E-cadherin mAbs. These findings indicate that the selective loss of E-cadherin expression can generate dedifferentiation and invasiveness of human carcinoma cells, and further suggest that E-cadherin acts as a tumor suppressor (5).
- PMID: 8814984
- PMID: 22558599
- PMID: 10439038
- PMID: 2070412
- PMID: 2007622
Novus Biologicals offers various E-cadherin reagents for your products research needs including:
Posted in Antibodies, Antibody catalog, Antibody database, Antibody suppliers, Cancer, Tumor, Uncategorized | No Comments »
June 7th, 2013
FOXP3, a member of forkhead/winged-helix family of transcription factors acts as a “master” regulator for the development and suppressive function of regulatory T cells (Tregs). Its constitutive expression is necessary for the suppressive function of Tregs, and mutation or deficiency of FOXP3 leads to development of autoimmune diseases (1). FOXP3 expression has also been reported in a variety of solid tumors, including melanoma.

FOXP3 expression in both tumor-infiltrating Tregs and melanoma cells was detected by immunohistochemical analysis of human melanoma tissues, in melanoma cell lines by flow cytometry, confocal microscopy, and Western blotting using anti-FOXP3 antibodies. Results from this study suggest that the mimicking of Treg function by melanoma cells may represent a possible mechanism of tumor resistance to immune destruction in the tumor microenvironment (2). The complex effects of post-translational modifications at individual lysines within the FOXP3 forkhead domain have been known to affect Treg function (3) modulation of these events using small molecule inhibitors may allow regulation of Foxp3+ Treg function clinically.
- PMID: 16551248
- PMID: 21547596
- PMID: 18641318
Novus Biologicals offers various FOXP3 reagents for your products research needs including:
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June 5th, 2013
Integrins are a group of trans-membrane receptors which encompass alpha and beta subunits acting as adhesion particles in addition to various other important cellular functions. Integrins are recognized to enable cell-cell, cell-ECM, cell-pathogen interface along with signaling through the plasma membrane comprising of critical cellular functions such as differentiation, migration in addition to survival. Several investigators have documented variations in integrin expression and function in several cancers. Numerous integrins such as αVβ3, αVβ5 and α5β1 are attributed to angiogenesis, a critical factor in tumor metastasis and tumor growth. In a recent study (1) it has been demonstrated that the integrins are capable of regulating the expression and activity of several proteases through various pathways there by contributing to the invasive potential of several tumors. FACS has also been successfully implemented in the quantitative analysis of serious effusions in clinical settings. It has been well documented that it is possible to quantitate the integrin molecule expression as detected by anti-alpha6 integrin subunit antibodies and by alpha and beta1 in malignant mesothelioma suggesting a role in tumor attachment to extracellular matrix (2). Novus Biologicals in the forefront specializing in flow cytometry reagents and offer the latest range of FACS related anti-integrin antibodies with cross reactivity against several species for your research needs.
- PMID: 22437309
- PMID: 16240402
Posted in Angiogenesis, Antibodies, Antibody catalog, Antibody database, Antibody suppliers, Cancer, Flow Cytometry, Uncategorized | No Comments »
June 3rd, 2013
Florescence activated cell sorting or Flow cytometry is responsible for many of the current innovations made against HIV. Newer-generation FACS machines, proficient of using multi-color panels, are allowing researchers to measure lymphocyte subsets more precisely and cost-effectively. In the case of HIV, flow cytometry can identify which cell subsets are affected by the infection among individual patients. Initial studies using flow cytometry outlined the alterations to major cell pedigrees that occur after HIV infection resulting in a decrease in CD4 positive T-cells and a shared surge in CD8 positive T-cells (1). Consequently, investigators documented the elevated degree at which T-cells were absent in HIV positive human subjects by executing kinetic analyses of T-cell turnover (2). These studies utilized flow cytometry to compute CD4 positive T-cells numbers prior and subsequent to the development of new therapy. Advances in flow cytometry, have led researchers to enhance their comprehension of how the T-cells emerge upon infection. During the initial stages of HIV infection a sizeable number of memory CD4 positive T-cells cause destruction to the gut which in turn allows the translocation of infectious byproducts into systemic circulation. These microbial ligands for toll-like receptors, attach to CD4 and CD8 positive T-cells, triggering the loss of T-cells accompanied in the initial HIV infection. FACS have also bestowed vital clinical data that facilitates disease outcomes suggesting that CD4 positive T-cell count and viral load are the most relevant predictors of the disease (3) in addition to several extracellular and intracellular markers are commercially available to test HIV-specific T-cells a across a wide variety of patient groups, ranging from early to acute and chronic HIV infection.
- PMID: 8133451
- PMID: 7816094
- PMID: 7686224
Novus Biologicals is in the fore front specializing in flow cytometry reagents for your research studies and offer a wide variety of exploratory tools for your FACS needs.
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May 31st, 2013
The extracellular matrix ECM) is the material found in the extracellular environment of all tissues and organs. The composition of the extracellular framework of all vertebrates is dominated by a class of molecules known as collagens, each with unique features suited for a particular function and location.

Collagen proteins are composed of three subunit polypeptides that vary in length and interact to form a triple helix due to a unique repeated (Gly-x-y) sequence. Collagen I is one of the most common forms and is found in skin, tendon, vascular ligature, organs, and bone. Because of its basic and fundamental role in ECM architecture, Collagen I antibodies are helpful in identifying and/or verifying tissue-specific origin and sample tissue typing. Collagen I antibodies have been used to assess fibroblast primary sources in pulmonary fibrosis (1). Studies looking at transcriptional regulation of Procollagen Lysyl Hydroxylase 2 (PLOD2) and Hypoxia-Inducible Factor 1 (HIF-1) in breast cancer metastasis relied upon Collagen I antibodies (2,3). Collagen I antibodies helped monitor murine spleen cell differentiation in serum-free culturing conditions (4). Wound healing studies looking at liver regeneration also relied upon Collagen I antibodies (5).
- PMID: 14722616
- PMID: 23378577
- PMID: 23423382
- PMID: 20888336
- PMID: 23228176
Novus Biologicals is proud to offer a wide selection of Collagen reagents including antibodies, lysates, proteins, RNAi and more!
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May 20th, 2013
PINK1 (PTEN-induced putative kinase 1) is a mitochondrial directed serine-threonine kinase, that regulates normal mitochondrial function and transport vital to normal performance of neurons and neuronal survival. PINK1 has been shown to be localized to the cytosol, endoplasmic reticulum and the mitochondria. Some investigators have associated PINK1 localization to the intermembrane space, outer membrane insertion with a kinase domain facing towards the cytosol. Loss of PINK1 has been demonstrated to be accompanied with amplified oxidative stress and diminished membrane potential along with low levels of ATP.

Immunocytochemistry/Immunofluorescence: PINK1 Antibody
More recently, PINK1 has also been implicated in regulating mitophagy and mitochondrial biogenesis while mutations in PINK1 are known to cause autosomal recessive Parkinson’s disease. Studies carried out using cell imaging of both the mouse and human neurons have demonstrated that PINK1 regulates calcium efflux from mitochondria and deficiency of PINK1 leads to calcium overload and increased oxidation in the mitochondria and cytosol (1). There is a huge body of data to confirm that PINK1 functions to safeguard neurons against stress-induced cell death. PINK1 functions may vary contingent to mitochondrial and cellular signals, permitting PINK1 to act as a sensor to mitochondrial well-being. Further research and a better understanding of PINK1 functions may provide useful insights in to what may go wrong in Parkinson’s and other neuronal diseases.
- PMID: 19285945.
Novus Biologicals in the fore front specializing in PINK1 reagents including:
Tags: PINK1, PINK1 antibodies, PINK1 antibody
Posted in Antibodies, Antibody catalog, Antibody database, Antibody suppliers, Neurodegeneration, Neuroscience, Parkinsons | No Comments »
May 17th, 2013
GFP (green florescent protein), originally discovered in the jellyfish Aequorea victoria, (1) is one of the most extensively investigated and exploited proteins in the area of life sciences. GFP is well known for its proficiency emit fluorescence and has proven itself as an indicating marker of gene expression and protein target in intact cells and organisms. To date GFP variants can be chiefly distributed into seven classes based on their elements of their chromophores. One of the first proposed applications of GFP was to detect the gene expression in vivo as a marker protein, thereby allowing the gene product to be detected in subcellular localization studies.

WB analysis of GFP transfected in HeLa whole cell lysate.
GFP has been successfully employed by various investigators to act as a genetic fusion partner to the host proteins there by allowing researchers to monitor the localization and fate of GFP along with the gene encoding the endogenous protein and the resulting byproduct being expressed in the cell or organism under investigation. GFP has also served as a powerful marker in the studies where investigators were interested in the understanding of protein-protein interactions along with the dynamic prost-translational modifications. With the help of florescence microscopy investigators can easily monitor the intracellular processes within the live cells. Scientists have been successful in generating several transgenic animal models that express GFP in specific sites that could enable them to monitor the biological processes in the dearth of several cofactors paving a way for the gene therapy. However enormous challenges and opportunities remain on how GFP can be exploited as a marker protein for the better understanding of the complicated processes leading to several disorders in various organisms and is an open area of research. Novus Biologicals is the vanguard specializing in GFP reagents for your research needs by offering the latest range of GFP antibodies with reactivity against various species.
- PMID: 14051839
Tags: GFP, GFP antibody, Green Fluorescent Protein
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