Olink AB and Bethyl sign distribution agreement for the US market

UPPSALA, SWEDEN, November 2011 - Olink Bioscience, a Sweden based biotechnology company focused on innovative protein detection technologies, has entered into a distribution agreement with Bethyl Laboratories, Inc. Together with Bethyl Olink Bioscience will continue to expand the distribution of the Duolink® product line in the US market.

 “We are excited to enter into an agreement with Bethyl to distribute our Duolink product line in the USA. With an excellent reputation as a provider of first class products we believe Bethyl will help us expand the market for our products in the region”, comments Simon Fredriksson, President and CEO, Olink AB.

 “Bethyl is an established provider of premium quality antibody products and services for clinical and research applications and through the distribution agreement with Olink we now have the opportunity to offer a complete solution of antibodies together with a highly specific protein detection technology” says John Carwile, CEO, Bethyl Laboratories, Inc.

About Bethyl
Since 1972, Bethyl has provided quality antibody products and services for both clinical and research applications. We remain committed to manufacturing new and novel antibodies to facilitate and accelerate your discovery based research in cell biology. To ensure the quality of our antibodies, all antibodies are produced and affinity purified by antigen specific affinity chromatography at our sole facility in Montgomery, TX. Through our collaborations and scholarly searches we continue to identify new and emerging proteins of interests. We are aggressively producing antibodies to these new proteins as well as those classic proteins for which there is a dearth of quality antibodies. We test our antibodies in a wide range of applications including ELISA, western blot, immunoprecipitation, immunohistochemistry, immunocytochemistry and proximity ligation assay.

Bethyl Laboratories is a Registered Research Facility with the USDA under the Animal Welfare Act and complies daily with all requirements of the Act. Bethyl Laboratories, Inc. operates under Good Manufacturing Practices.

About Olink AB
Olink Bioscience, a company founded by scientists at Uppsala University, is commercializing cutting-edge technologies for analysis of proteins and nucleic acids revealing new insights into basic science, drug development, and diagnostics.  Our products are available worldwide through a network of distributors and through our web shop. The Duolink® product line enables users to visualize and quantify individual proteins, their interactions and modifications, in unmodified cells and tissues. Proseek® is an open assay development reagent kit for analyzing proteins in only 1 µl of serum or plasma sample with high sensitivity.

Olink Bioscience molecular technologies are also commercialized through partnerships with industry leading organizations such as Affymetrix, Life Technologies, and through Olink spin-out companies Halo Genomics and Qlinea. Olink Bioscience was founded in 2004 and is headquartered in Uppsala, Sweden

For more information, please contact:

John M. Carwile, MD

Chief Executive Officer

Bethyl Laboratories, Inc.

(800) 338-9579 (main)

jcarwile@bethyl.com

Focusing on Homologous Recombination

Double stranded breaks (DSBs) are a normal occurrence during DNA replication. The cellular response to DSBs is complex and highly orchestrated, and a cell’s inability to properly address DSBs can lead to genetic alterations such as loss of heterozygosity, mutations, deletions, genomic rearrangements, and chromosome loss. There are two major pathways for repairing DSBs: non-homologous end joining (NHEJ) and homologous recombination (HR). Both pathways are critical to the maintenance of genomic stability and involve a variety of proteins that play particular functional roles in the response to DNA damage. In HR, the functional groups include the DNA damage sensors, cell cycle checkpoint enforcers, and the catalyzers of HR repair itself. Additionally, the HR repair pathway requires proteins that function as adaptors and transducers, effector kinases, regulatory proteins, and structural components (1). There a re several diseases associated with genetic defects in proteins involved in HR. These genetic diseases are characterized by a predisposition to cancer indicating the importance of intact HR pathways to circumvent cancer (2). Although deficiencies in HR lead to cancer development, these deficiencies also allow for the selective treatment of cancer cells. Anti-cancer drugs mainly kill cancer cells by inducing toxic DSBs and defects in HR can increase the sensitivity of cancer cells to these drugs (3). Therefore, a better understanding of the factors and pathways involved in HR will further advancements in the development of therapies for cancer.

Selected Reviews

1. Lisby, M. & Rothstein, R. (2009). Choreography of recombination proteins during the DNA damage response. DNA Repair (Amst), 8, 1068-1076.

2. Thompson, L. H. & Schild, D. (2002). Recombinational DNA repair and human disease. Mutat.Res., 509, 49-78.

3. Helleday, T. (2010). Homologous recombination in cancer development, treatment and development of drug resistance. Carcinogenesis, 31, 955-960.

Homologous Recombination Antibody Portfolio

53BP1, Abraxas, ATM, ATR, ATRIP, BARD1, BLM, BRCA1, BRCA2, BRCC36, cAbl, Chk1, Chk2, Claspin, CtIP, FANCA, FANCD2, FANCE, H2AX, Mre11, NBS1, PALB2, Rad17, Rad50, RAD51C, Rad52, Rad9, RAP80, RFC1, RFC2, RFC3, RFC4, RFC5, SMC1, SMC3, SMC5, TopBP1, WRN.

Focusing on CML

Chronic Myelogenous Leukemia (CML) is a hematopoietic stem-cell neoplasm of myeloid origin. A common method for the diagnosis of CML is based on the detection of a chromosomal translocation, first discovered in 1960 by Peter C. Nowell at the University Of Pennsylvania School Of Medicine in Philadelphia. The presence of the translocation was termed the Philadelphia chromosome and was the first chromosomal abnormality positively linked to cancer. Because it is present in over 90% of patients with CML, the Philadelphia chromosome is recognized as the genetic hallmark of CML. The translocation in the Philadelphia chromosome results in the juxtaposition of a portion of the BCR (breakpoint cluster region) gene located on chromosome 22 next to the ABL (Abelson leukemia virus) gene on chromosome 9 [t(9:22)]. Following the discovery of the Philadelphia chromosome came the finding that the product of the ABL gene function ed as a protein tyrosine kinase and that inappropriate regulation of kinase enzymes can be oncogenic. The BCR-ABL fusion protein was shown to be oncogenic and exhibit constitutive kinase activity. Constitutive kinase activity promotes the activation of a number of signaling pathways that support the uncontrolled growth and survival of hematopoietic cells resulting in neoplastic disease. These findings prompted a search for agents that could selectively target the activity of the BCR-Abl fusion protein and resulted in the identification of imatinib mesylate (Gleevec), the first tyrosine kinase inhibitor successfully and effectively used as a molecularly-targeted treatment for cancer. Thus, the discovery that began in Philadelphia with CML has served as a prime example of the successful translation of knowledge gained at the bench of basic scientists into treatments at the bedside of cancer patients.

Selected Reviews

Bumbea, H., Vladareanu, A. M., Voican, I., Cisleanu, D., Barsan, L., & Onisai, M. (2010). Chronic myeloid leukemia therapy in the era of tyrosine kinase inhibitors--the first molecular targeted treatment. J. Med. Life, 3, 162-166.

Koretzky, G. A. (2007). The legacy of the Philadelphia chromosome. J. Clin. Invest, 117, 2030-2032.

Sawyers, C. L. (1999). Chronic myeloid leukemia. N. Engl. J. Med., 340, 1330-1340.

CML Antibody Portfolio
 
Axl, BCR, cAbl, NUP98, SMARCB1/SNF5

Focusing on Ribosomes

Ribosomes are large macromolecules that are constructed of both RNA and protein components and play a fundamental role in decoding genetic information. The RNA component of ribosomes has been shown to provide the enzymatic activities required for protein translation, while the protein components are thought to serve largely in a structural manner.  The human 80S ribosome is made up of a 60S and 40S subunit. The 60S subunit is composed of a 5S rRNA, 5.8S rRNA, 28S rRNA and approximately 49 proteins and functions to catalyze peptide bond formation. The 40S subunit is composed of an 18S rRNA and approximately 33 proteins and functions to bring together the mRNA codon and the tRNA anticodon. Evolutionarily speaking, ribosomal proteins represent some of the oldest proteins, and their evolutionary development is considered to be the spark that facilitated a transition from a mainly DNA/RNA world to a DNA/RNA/protein wo rld. As a link between the RNA and protein world, ribosomes fulfill a critical element of the “central dogma” which hypothesizes that for all living things, DNA is transcribed into RNA which is then translated to protein.  Ribosomal structure and function is highly conserved across archaea, bacteria, and eukaryotes and it is suggested that along with RNA and DNA, modern ribosomal macromolecules were present among the last common ancestor (LUCA). Because of their ancient beginnings and macromolecular complexity, studies of  ribosome structure, function, and assembly will provide clues to the origins of life and the evolutionary history of modern species.

Selected Reviews

Crick, F. (1970). Central dogma of molecular biology. Nature, 227, 561-563.

Fox, G. E. (2010). Origin and evolution of the ribosome. Cold Spring Harb. Perspect. Biol., 2, a003483.

Moore, P. B. & Steitz, T. A. (2002). The involvement of RNA in ribosome function. Nature, 418, 229-235.

Ribosome Antibody Portfolio

AATF/Che-1, BOP1, DAP3, DjC21, Drosha, GCN1L1, GCN2, NPM1, NUFIP2, PRMT3, RACK1, RPL26, RPL7, rpL7a/SURF3, RPLP0, RPS6, RPS6 (S235), RPS6 (S235/S236), Ubiquitin.

Rabbit IL-8 (CXCL8) ELISA Kit

Interleukin-8 (IL-8), renamed CXCL8, is a chemokine produced by macrophages and other cell types such as epithelial cells and endothelial cells. IL-8 can be secreted by any cell with toll-like receptors which are involved in the innate immune response. The most frequently studied receptors of IL-8 are the G protein coupled serpentine receptors CXCR1 (previously named IL-8 receptor α) and CXCR2 (previously named IL-8 receptor β). Both monomer and homodimer forms of IL-8 were reported as potent inducers of CXCR1 and CXCR2.

IL-8 is one of the first major mediators of the inflammatory response. The primary function of IL-8 is the induction of chemotaxis in its target cells (e.g. neutrophil granulocytes). Initially, macrophages phagocytose the antigen. Upon processing the antigen, macrophages release chemokines, such as IL-8, to signal other immune cells to come to the site of inflammation. IL-8 serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as neutrophil chemotactic factor.

While neutrophil granulocytes are the primary target cells of IL-8, there is a relative wide range of cells (endothelial cells, macrophages, mast cells, keratinocytes) responding to this chemokine, too. IL-8 is believed to play a role in the pathogenesis of bronchiolitis, a common respiratory tract disease caused by viral infection.

Standard range is 320 - 5 pg/ml

Rabbit IL-8 ELISA Kit  Catalog No. E121-800

CCL2 ELISA Kits for Pig and Bovine

Chemokine (C-C motif) ligand 2 (CCL2) is a small cytokine belonging to the CC chemokine family that is also known as monocyte chemotactic protein-1 (MCP-1). CCL2 recruits monocytes, memory T cells, and dendritic cells to sites of tissue injury and infection.1-2 This chemokine is produced as a protein precursor containing signal peptide of 23 amino acids and a mature peptide of 76 amino acids.3-4 It is a monomeric polypeptide, with a molecular weight of approximately 13kDa. The cell surface receptors that bind CCL2 are CCR2 and CCR4.5.

CCL2 is found at the site of tooth eruption and bone degradation. In the bone, CCL2 is expressed by mature osteoclasts and osteoblasts and is under the control of nuclear factor κB (NFκB). CCL2 causes the degranulation of basophils and mast cells, an effect potentiated by pre-treatment with IL-3 and other cytokines.6-7

Pig CCL2 ELISA Kit  E101-800

Bovine CCL2 ELISA Kit E11-800



Background References

 

1. Carr MW, Roth SJ, Luther E, Rose SS, Springer TA (April 1994). "Monocyte chemoattractant protein 1 acts as a T-lymphocyte chemoattractant". Proc. Natl. Acad. Sci. U.S.A. 91 (9): 3652–6.

2. Xu LL, Warren MK, Rose WL, Gong W, Wang JM (01 September 1996). "Human recombinant monocyte chemotactic protein and other C-C chemokines bind and induce directional migration of dendritic cells in vitro". J. Leukoc. Biol. 60 (3): 365–71.

3. Yoshimura T, Yuhki N, Moore SK, Appella E, Lerman MI, Leonard EJ (February 1989). "Human monocyte chemoattractant protein-1 (MCP-1). Full-length cDNA cloning, expression in mitogen-stimulated blood mononuclear leukocytes, and sequence similarity to mouse competence gene JE". FEBS Lett. 244 (2): 487–93.

4. Furutani Y, Nomura H, Notake M, Oyamada Y, Fukui T, Yamada M, Larsen CG, Oppenheim JJ, Matsushima K (February 1989). "Cloning and sequencing of the cDNA for human monocyte chemotactic and activating factor (MCAF)". Biochem. Biophys. Res. Commun. 159 (1): 249–55.

5. Craig MJ, Loberg RD (December 2006). "CCL2 (Monocyte Chemoattractant Protein-1) in cancer bone metastases". Cancer Metastasis Rev. 25 (4): 611–9.

6. Conti P, Boucher W, Letourneau R, Feliciani C, Reale M, Barbacane RC, Vlagopoulos P, Bruneau G, Thibault J, Theoharides TC (November 1995). "Monocyte chemotactic protein-1 provokes mast cell aggregation and [3H]5HT release". Immunology 86 (3): 434–40.

7. Bischoff SC, Krieger M, Brunner T, Dahinden CA (May 1992). "Monocyte chemotactic protein 1 is a potent activator of human basophils". J. Exp. Med. 175 (5): 1271–5.

Chicken IL-16 ELISA Kit

Interleukin 16 (IL-16) is a pleiotropic cytokine that has been characterized as a chemoattractant for certain immune cells expressing the cell surface molecule CD4, and has effects on mixed lymphocyte reaction and inhibition of HIV viral replication. Because this cytokine was discovered in 1982 for its T lymphocyte chemotactic activity, it was named “Lymphocyte Chemoattractant Factor (LCF)” until it was designated interleukin-16 in 1995. The product of this gene is generated as a precursor molecule, pro-IL-16, which is then processed to yield two functional proteins. IL-16 forms homotetramers and this structure is required for its bioactivity. The cytokine function is exclusively attributed to the secreted C-terminal peptide, while the N-terminal product may play a role in cell cycle control. Caspase 3 is reported to be involved in the proteolytic processing of this protein. IL-16 is released by a variety of immune (T cells, esinophils, and dendritic cells) and non-immune (fibroblasts, epithelial, and neurona) cells (Center et al., 1997; Cruikshank et al., 2000). In the non-diseased state, IL-16 mRNA is almost exclusively expressed on lymphatic tissue, and high levels in T cells. During inflammation, IL-16 is synthesized in a number of other tissues (Smith and Humphries, 2009). The sequence, structure, and function of IL-16 are highly conserved in all species examined. Thus far, all species of IL-16 tested induce similar bioactivities on CD4+ T cells. Chicken IL-6 has been cloned by Min et al. (2004) and shows 86% sequence identity to duct pro-IL-16, and 49-52% to various mammalian homologues. The recombinant chicken IL-16 showed chemoattractive activity to splenic lymphocytes.

Chicken IL-16 ELISA Kit  E33-800

Representative Data