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Marker Gene Monthly Newsletter

February, 2005

Volume 5, Number 2

© Copyright MGT, Inc., 2007. Published by Marker Gene Technologies, Inc., The University of Oregon Riverfront Research Park, 1850 Millrace Drive, Eugene, Oregon 97403-1992 USA. All rights reserved. For information on the use or copying of the material contained in this document, please contact us at techservice@markergene.com. Please see below for subscription information and updates. This newsletter is labeled as an ADVERTISEMENT in accordance with the CAN-SPAM act of 2003, S.877 Public Law: 108-187.

Leaky RNAi Targeting.

Recent reports of non-specific RNAi interactions may complicate the interpretation of experimental data, particularly when used in high-throughput assays, microarray analyses or for diagnostic or therapeutic applications. RNA silencing using small interfering RNA’s (RNAi) is a sequence specific RNA degradation process that is triggered by the formation of double stranded RNA in the cell. Complementary sequences of single stranded RNA (21 bp) are introduced by viral methods or as transgenes in vector constructs. When duplexes form, cellular degradation processes mediate the degradation of the target mRNA, and result in loss of target gene expression. The method seems to take advantage of a natural defense mechanism in cells that is used to prevent viral infection. But specificity of binding is paramount for targeting. In recent reports, RNAi targeted toward luciferase, a firefly protein with no close relatives in the human genome, was introduced into a human HeLa cell line, but exhibited effects on over 1800 genes. Similarly, two different RNAi’s targeted toward GFP caused differential effects on expression of both GFP and endogenous proteins. There have also been experiments in which RNAi’s have been constructed with slight mismatches for their intended target, but have still worked better than expected. In addition, RNAi’s have been found to initiate an interferon response, suggesting that the technique may cause cells to respond as if they're

Bridge, A.J. et al. (2003) Induction of an interferon response by RNAi vectors in mammalian cells. Nat. Genet. 34: 263–264.

Scacheri,P.C.et al. (2004) Short interfering RNAs can induce unexpected and divergent changes in the levels of untargeted proteins in mammalian cells. Proc. Natl. Acad. Sci. U. S. A. 101: 1892–1897.

Persengiev, S.P. et al. (2004) Nonspecific, concentration-dependent stimulation and repression of mammalian gene expression by small interfering RNAs (siRNAs). RNA 10: 12–18.

A. L. Jackson and P. S. Linsley (2004) “Noise amidst the silence: off-target effects of siRNAs?” TRENDS in Genetics 20(11): 521-524.

Gaucher’s Disease – a Lysosomal Storage Disorder.

People with Gaucher’s disease lack the normal form of the enzyme glucocerebrosidase and are unable to break down glucocerebroside glycolipids. Instead, the glucocerebrosides remain stored within macrophage lysosomes, preventing the macrophages from functioning normally. Enlarged macrophages containing undigested glucocerebroside are called Gaucher cells. These cells are the hallmark of the disease. Gaucher disease is the most common of so-called "storage" disorders, with an occurrence of about 2 newborns of every 100,000 live births. The most widely known of these disorders is Tay-Sachs disease. The fluorogenic substrate fluorescein di-b-D-glucopyranoside (FDGlc, M0881) is one of the most sensitive substrates for detecting glucocerebrosidase and general -glucosidase activity in both cells and cell extracts.

This substrate has also been used to demonstrate the utility of Saccharomyces cerevisiae and Candida albicans exo-1,3--glucanase genes as reporter genes. Because these reporter genes encode secreted proteins, assays for reporter gene expression do not require cell permeabilization. Marker Gene also provides the red fluorogenic resorufin b-D-glucopyranoside (M0569) substrate, which is a more stable, long-wavelength analog for detection of these important enzymes. Please see our website or the references below for more information.

Kohen E., Kohen C., Hirschberg J.G., Santus R., Grabowski G., Mangel W., Gatt S., Prince J., (1993) "An in situ study of beta-glucosidase activity in normal and Gaucher fibroblasts with fluorogenic probes." Cell Biochem. Funct. 11: 167-177.

Cid V.J., Alvarez A.M., Santos A.I., Nombela C., Sanchez M., (1994) "Yeast exo-beta-glucanases can be used as efficient and readily detectable reporter genes in Saccharomyces cerevisiae." Yeast 10: 747-756.

van Es H.H., Veldwijk M., Havenga M., Valerio D. (1997) "A flow cytometric assay for lysosomal glucocerebrosidase" Anal. Biochem.247:268-271.

Chan KW; Waire J; Simons B., (2004) "Measurement of lysosomal glucocerebrosidase activity in mouse liver using a fluorescence-activated cell sorter assay." Anal Biochem 334(2): 227-33.

Rudensky B., Paz E., Altarescu G., (2003) "Fluorescent flow cytometric assay: a new diagnostic tool for measuring beta-glucocerebrosidase activity in Gaucher disease." Blood Cells Mol. Dis. 30(1): 97-9.

Barnase expression utilizes negative selection.

The barnase gene codesfor a highly active RNase from Bacillus amyloliquefaciens. It has been utilized in plant molecular biology for decades as a method of selection for recombinant plant species. The bacteria Bacillus amyloliquefaciens manufactures this cytotoxic 110-residue extracellular ribonuclease, which cleaves single-stranded RNA through hydrolysis of phosphodiester bonds. The complete system typically utilizes two components, the enzyme barnase, which kills cells expressing it, and a ‘site-specific’ recombinase, which is used to block the action of barnase until it is required. A third component, the barstar gene, codes for the barstar protein, a 90-residue polypeptide that’s a steric inhibitor of barnase, useful in neutralizing its activity. Co-expression of barnase and barstar allow continued growth and development. In addition to its use in plant molecular biology, the barnase gene has recently been incorporated into mammalian expression vectors for use in selection of recombinant cells, either under control of a tetracycline inducible promoter system, or by including a multiple cloning site within the barnase gene sequence. In the latter case, subcloning a gene of interest within the barnase sequence, destroys its activity, and allows recombinant cells to grow, while untransfected cells are ablated. For more information about these new techniques, see the references below.

Hartley,R.W. (1989) “Barnase and Barstar: Two small small proteins to fold and fit together.” Trends Biochem. Sci., 14: 450–454.

S. Leuchtenberger, A. Perz, C. Gatz , J. W. Bartsch (2001) “Conditional cell ablation by stringent tetracycline-dependent regulation of barnase in mammalian cells.” Nucleic Acids Research 29(16): 76-80.

Yazynin S., Lange H., Mokros T., Deyev S., Lemke H., (1999) “A new phagemid vector for positive selection of recombinants based on a conditionally lethal barnase gene.” FEBS Lett. 452(3): 351-4.

Yazynin S.A., Deyev S.M., Jucovic M., Hartley R.W., (1996) “A plasmid vector with positive selection and directional cloning based on a conditionally lethal gene.” Gene 169(1): 131-2.

Fluorescent Glutathione Transferase Assay.
Glutathione (GSH), is a tripeptide (g-glutamyl-cysteinyl-glycine) that represents the major free thiol in most living cells. It is involved in many biological processes including detoxification of xenobiotics, removal of hydroperoxides, and maintenance of the oxidation state of protein sulfhydryls. It is the key antioxidant present in animal tissues, and diminished glutathione levels have been observed in the early stages of apoptosis. Older methods for determining glutathione utilize 5,5’-dithiobis(2-nitrobenzoic acid) (DTNB or Ellman’s reagent) in an oxidation or oxidation-reduction scheme. But these methods have been largely replaced by a widely used method for determining GSH in living cells. By simply adding monochlorobimane (M1045) to cell culture medium and allowing intracellular glutathione S-transferases to form GSH-mCB complexes, levels of GSH can be measured fluorometrically. Unlike other bimanes such as monobromobimane, monochlorobimane appears to form an adduct exclusively with GSH. The membrane-permeant monochlorobimane has been used to measure GSH in live cells and in flow cytometry systems. This procedure has been used to measure GSH content of cultured neural cells and in tissue homogenates and, indeed, several laboratories have used this approach to measure the GSH content of the cytosolic fraction liver and intact tissues. It has been found that monochlorobimane readily enters cells to form a fluorescent GSH–mono-chlorobimane adduct that can be measured fluorometrically and that this reaction is catalyzed by glutathione S-transferase. Please see our website for more information about these techniques, and look for new products from Marker Gene in this area. Additional information is available in the references below.

Fernandez-Checa, J. C., Kaplowitz, N. (1990) “The use of monochlorobimane to determine hepatic GSH levels and synthesis.” Anal. Biochem. 190: 212–219.

H. Kamencic, A. Lyon, P. G. Paterson, B. H. J. Juurlink (2000) “Monochlorobimane Fluorometric Method to Measure Tissue Glutathione” Analytical Biochemistry 286: 35–37.

Reichelt, W., Stabel-Burow, J., Pannicke, T., Weichert, H., Heinemann, U. (1997) “The glutathione level of retinal Müller glial cells is dependent on the high-affinity sodium-dependent uptake of glutamate.” Neuroscience 77: 1213–1224.

Devesa, A., Oconnor, J. E., Garcia, C., Puertes, I. R., Vina, J. R. (1993) “Glutathione metabolism in primary astrocyte cultures: flow cytometric evidence of heterogeneous distribution of GSH content.” Brain Res. 618: 181–189.

Kannan, R., Tang, D., Mackic, J. B., Zlokovic, B. V., Fernandez-Checa, J. C. (1993) “A simple technique to determine glutathione (GSH) levels and synthesis in ocular tissues as GSH-bimane adduct: application to normal and galactosemic guinea-pigs.” Exp. Eye Res. 56: 45–50.

The DAAO Selection Marker Technology described in our July, 2004 WebNewsletter (SELDA^TM Technology) is available for license from BASF Plant Sciences GmbH. Please contact Dr. Andreas Ranz, BPS – Li 444, D-67117 Linburgerhof, Germany (e-mail: andreas.renz@basf-ag-de) for more information.

Compare Our Quality.
Marker Gene strives to offer our customers products of the highest quality and at the best possible prices. Our years of experience allow us to provide timely products for less cost to you. See our latest Price Comparison Chart that compares our prices with those from several alternate sources, to see if you can save money by switching to Marker Gene (http://www.markergene.com/crossref.htm). Or visit our website at www.markergene.com and click on the link “COMPARE”. We think you will appreciate our efforts to keep costs low and maintain excellent quality of our products for your research. For more information about any of our products, simply telephone us toll free at 1-888-218-4062 or contact us by e-mail at techservice@markergene.com. We will be happy to send you more about our products and their specifications.

New 2005-2006 Catalog Now Available.

The 2005 edition of the Marker Gene catalog is now available. Visit our website or use the link www.markergene.com/catalog2005-2006.pdf for an electronic version. Many new products and kits, additional literature references, data and protocols have been included, as well as new information about our old products. Ifyou haven’t already received yours, be sure to add your name to our mailing list. Visit our Customer Information Form, or e-mail us at techservice@markergene.com and we will have a copy sent out to you post-haste. Sign up now!

CONTRACT RESEARCH@markergene.com

Marker Gene Technologies, Inc. has the expertise to perform contract research with you on your project. We have worked with many biotechnology and pharmaceutical companies on successful, proprietary and patented projects.

Contract Research and Development Capabilities in the following areas:

Established in 1993 at the University of Oregon Riverfront Research Park.

Screening Assay Development for HTS and uHTS

Chemical and Cellular Assays – High-Content Screening.

DNA/RNA (genomics) and protein (proteomics) labeling and assay development.

Pharmaceutical Intermediates - design, synthesis, and in vitro testing in mammalian cell culture.

Specializing in Carbohydrate, Lipid, Peptide, and Nucleic Acid Chemistries.

Fully equipped laboratories (Biochemistry, Chemical Synthesis, Tissue Culture, Analytical).

Confidentiality, help in patent preparation and filings.

Contact us by telephone at (888) 218-4062 or (541) 342-3760 or FAX us at (541) 342-1960 or you can write to us at Contract Research, Marker Gene Technologies, Inc., 1850 Millrace Drive, Eugene, Oregon 97403-1992 or contact us by e-mail at: techservice@markergene.com

Marker Gene Accepts Major Credit Cards.

Place your orders now, using Master Card or Visa and save time and money! Our Customer Assistance Staff can now accept either Master Card or Visa Credit Card orders, securely by telephone (toll-free) at 1-888-218-4062 (Domestic orders only). We will continue to accept Institutional Purchase Orders for our products, online or by FAX at 1-541-342-1960. International customers should contact us by e-mail, post or telephone for more information about International Distributors and ordering. For information on pricing for individual products, or for a quote on bulk quantities of our products or kits, please contact our technical assistance staff at techservice@markergene.com. We will be happy to assist you.

To add your name to our WebNewsletter mailing list, please use the following link: subscribe@markergene.com.

To unsubscribe from our mailing list, please use the following link: unsubscribe@markergene.com. Your e-mail address will be deleted in 2-3 business days.


	If you are having trouble viewing this email, click on this link. To order any of our products, please go to our ORDER FORM or visit one of our distributors:
	Marker Gene Monthly Newsletter February, 2005 Volume 5, Number 2 © Copyright MGT, Inc., 2007. Published by Marker Gene Technologies, Inc., The University of Oregon Riverfront Research Park, 1850 Millrace Drive, Eugene, Oregon 97403-1992 USA. All rights reserved. For information on the use or copying of the material contained in this document, please contact us at techservice@markergene.com. Please see below for subscription information and updates. This newsletter is labeled as an ADVERTISEMENT in accordance with the CAN-SPAM act of 2003, S.877 Public Law: 108-187.
	Leaky RNAi Targeting. Recent reports of non-specific RNAi interactions may complicate the interpretation of experimental data, particularly when used in high-throughput assays, microarray analyses or for diagnostic or therapeutic applications. RNA silencing using small interfering RNA’s (RNAi) is a sequence specific RNA degradation process that is triggered by the formation of double stranded RNA in the cell. Complementary sequences of single stranded RNA (21 bp) are introduced by viral methods or as transgenes in vector constructs. When duplexes form, cellular degradation processes mediate the degradation of the target mRNA, and result in loss of target gene expression. The method seems to take advantage of a natural defense mechanism in cells that is used to prevent viral infection. But specificity of binding is paramount for targeting. In recent reports, RNAi targeted toward luciferase, a firefly protein with no close relatives in the human genome, was introduced into a human HeLa cell line, but exhibited effects on over 1800 genes. Similarly, two different RNAi’s targeted toward GFP caused differential effects on expression of both GFP and endogenous proteins. There have also been experiments in which RNAi’s have been constructed with slight mismatches for their intended target, but have still worked better than expected. In addition, RNAi’s have been found to initiate an interferon response, suggesting that the technique may cause cells to respond as if they're Bridge, A.J. et al. (2003) Induction of an interferon response by RNAi vectors in mammalian cells. Nat. Genet. 34: 263–264. Scacheri,P.C.et al. (2004) Short interfering RNAs can induce unexpected and divergent changes in the levels of untargeted proteins in mammalian cells. Proc. Natl. Acad. Sci. U. S. A. 101: 1892–1897. Persengiev, S.P. et al. (2004) Nonspecific, concentration-dependent stimulation and repression of mammalian gene expression by small interfering RNAs (siRNAs). RNA 10: 12–18. A. L. Jackson and P. S. Linsley (2004) “Noise amidst the silence: off-target effects of siRNAs?” TRENDS in Genetics 20(11): 521-524.
	Gaucher’s Disease – a Lysosomal Storage Disorder. People with Gaucher’s disease lack the normal form of the enzyme glucocerebrosidase and are unable to break down glucocerebroside glycolipids. Instead, the glucocerebrosides remain stored within macrophage lysosomes, preventing the macrophages from functioning normally. Enlarged macrophages containing undigested glucocerebroside are called Gaucher cells. These cells are the hallmark of the disease. Gaucher disease is the most common of so-called "storage" disorders, with an occurrence of about 2 newborns of every 100,000 live births. The most widely known of these disorders is Tay-Sachs disease. The fluorogenic substrate fluorescein di-b-D-glucopyranoside (FDGlc, M0881) is one of the most sensitive substrates for detecting glucocerebrosidase and general -glucosidase activity in both cells and cell extracts. This substrate has also been used to demonstrate the utility of Saccharomyces cerevisiae and Candida albicans exo-1,3--glucanase genes as reporter genes. Because these reporter genes encode secreted proteins, assays for reporter gene expression do not require cell permeabilization. Marker Gene also provides the red fluorogenic resorufin b-D-glucopyranoside (M0569) substrate, which is a more stable, long-wavelength analog for detection of these important enzymes. Please see our website or the references below for more information. Kohen E., Kohen C., Hirschberg J.G., Santus R., Grabowski G., Mangel W., Gatt S., Prince J., (1993) "An in situ study of beta-glucosidase activity in normal and Gaucher fibroblasts with fluorogenic probes." Cell Biochem. Funct. 11: 167-177. Cid V.J., Alvarez A.M., Santos A.I., Nombela C., Sanchez M., (1994) "Yeast exo-beta-glucanases can be used as efficient and readily detectable reporter genes in Saccharomyces cerevisiae." Yeast 10: 747-756. van Es H.H., Veldwijk M., Havenga M., Valerio D. (1997) "A flow cytometric assay for lysosomal glucocerebrosidase" Anal. Biochem.247:268-271. Chan KW; Waire J; Simons B., (2004) "Measurement of lysosomal glucocerebrosidase activity in mouse liver using a fluorescence-activated cell sorter assay." Anal Biochem 334(2): 227-33. Rudensky B., Paz E., Altarescu G., (2003) "Fluorescent flow cytometric assay: a new diagnostic tool for measuring beta-glucocerebrosidase activity in Gaucher disease." Blood Cells Mol. Dis. 30(1): 97-9.
	Barnase expression utilizes negative selection. The barnase gene codesfor a highly active RNase from Bacillus amyloliquefaciens. It has been utilized in plant molecular biology for decades as a method of selection for recombinant plant species. The bacteria Bacillus amyloliquefaciens manufactures this cytotoxic 110-residue extracellular ribonuclease, which cleaves single-stranded RNA through hydrolysis of phosphodiester bonds. The complete system typically utilizes two components, the enzyme barnase, which kills cells expressing it, and a ‘site-specific’ recombinase, which is used to block the action of barnase until it is required. A third component, the barstar gene, codes for the barstar protein, a 90-residue polypeptide that’s a steric inhibitor of barnase, useful in neutralizing its activity. Co-expression of barnase and barstar allow continued growth and development. In addition to its use in plant molecular biology, the barnase gene has recently been incorporated into mammalian expression vectors for use in selection of recombinant cells, either under control of a tetracycline inducible promoter system, or by including a multiple cloning site within the barnase gene sequence. In the latter case, subcloning a gene of interest within the barnase sequence, destroys its activity, and allows recombinant cells to grow, while untransfected cells are ablated. For more information about these new techniques, see the references below. Hartley,R.W. (1989) “Barnase and Barstar: Two small small proteins to fold and fit together.” Trends Biochem. Sci., 14: 450–454. S. Leuchtenberger, A. Perz, C. Gatz , J. W. Bartsch (2001) “Conditional cell ablation by stringent tetracycline-dependent regulation of barnase in mammalian cells.” Nucleic Acids Research 29(16): 76-80. Yazynin S., Lange H., Mokros T., Deyev S., Lemke H., (1999) “A new phagemid vector for positive selection of recombinants based on a conditionally lethal barnase gene.” FEBS Lett. 452(3): 351-4. Yazynin S.A., Deyev S.M., Jucovic M., Hartley R.W., (1996) “A plasmid vector with positive selection and directional cloning based on a conditionally lethal gene.” Gene 169(1): 131-2.
	Fluorescent Glutathione Transferase Assay. Glutathione (GSH), is a tripeptide (g-glutamyl-cysteinyl-glycine) that represents the major free thiol in most living cells. It is involved in many biological processes including detoxification of xenobiotics, removal of hydroperoxides, and maintenance of the oxidation state of protein sulfhydryls. It is the key antioxidant present in animal tissues, and diminished glutathione levels have been observed in the early stages of apoptosis. Older methods for determining glutathione utilize 5,5’-dithiobis(2-nitrobenzoic acid) (DTNB or Ellman’s reagent) in an oxidation or oxidation-reduction scheme. But these methods have been largely replaced by a widely used method for determining GSH in living cells. By simply adding monochlorobimane (M1045) to cell culture medium and allowing intracellular glutathione S-transferases to form GSH-mCB complexes, levels of GSH can be measured fluorometrically. Unlike other bimanes such as monobromobimane, monochlorobimane appears to form an adduct exclusively with GSH. The membrane-permeant monochlorobimane has been used to measure GSH in live cells and in flow cytometry systems. This procedure has been used to measure GSH content of cultured neural cells and in tissue homogenates and, indeed, several laboratories have used this approach to measure the GSH content of the cytosolic fraction liver and intact tissues. It has been found that monochlorobimane readily enters cells to form a fluorescent GSH–mono-chlorobimane adduct that can be measured fluorometrically and that this reaction is catalyzed by glutathione S-transferase. Please see our website for more information about these techniques, and look for new products from Marker Gene in this area. Additional information is available in the references below. Fernandez-Checa, J. C., Kaplowitz, N. (1990) “The use of monochlorobimane to determine hepatic GSH levels and synthesis.” Anal. Biochem. 190: 212–219. H. Kamencic, A. Lyon, P. G. Paterson, B. H. J. Juurlink (2000) “Monochlorobimane Fluorometric Method to Measure Tissue Glutathione” Analytical Biochemistry 286: 35–37. Reichelt, W., Stabel-Burow, J., Pannicke, T., Weichert, H., Heinemann, U. (1997) “The glutathione level of retinal Müller glial cells is dependent on the high-affinity sodium-dependent uptake of glutamate.” Neuroscience 77: 1213–1224. Devesa, A., Oconnor, J. E., Garcia, C., Puertes, I. R., Vina, J. R. (1993) “Glutathione metabolism in primary astrocyte cultures: flow cytometric evidence of heterogeneous distribution of GSH content.” Brain Res. 618: 181–189. Kannan, R., Tang, D., Mackic, J. B., Zlokovic, B. V., Fernandez-Checa, J. C. (1993) “A simple technique to determine glutathione (GSH) levels and synthesis in ocular tissues as GSH-bimane adduct: application to normal and galactosemic guinea-pigs.” Exp. Eye Res. 56: 45–50.
	The DAAO Selection Marker Technology described in our July, 2004 WebNewsletter (SELDA^TM Technology) is available for license from BASF Plant Sciences GmbH. Please contact Dr. Andreas Ranz, BPS – Li 444, D-67117 Linburgerhof, Germany (e-mail: andreas.renz@basf-ag-de) for more information.
	Compare Our Quality. Marker Gene strives to offer our customers products of the highest quality and at the best possible prices. Our years of experience allow us to provide timely products for less cost to you. See our latest Price Comparison Chart that compares our prices with those from several alternate sources, to see if you can save money by switching to Marker Gene (http://www.markergene.com/crossref.htm). Or visit our website at www.markergene.com and click on the link “COMPARE”. We think you will appreciate our efforts to keep costs low and maintain excellent quality of our products for your research. For more information about any of our products, simply telephone us toll free at 1-888-218-4062 or contact us by e-mail at techservice@markergene.com. We will be happy to send you more about our products and their specifications.
	New 2005-2006 Catalog Now Available. The 2005 edition of the Marker Gene catalog is now available. Visit our website or use the link www.markergene.com/catalog2005-2006.pdf for an electronic version. Many new products and kits, additional literature references, data and protocols have been included, as well as new information about our old products. Ifyou haven’t already received yours, be sure to add your name to our mailing list. Visit our Customer Information Form, or e-mail us at techservice@markergene.com and we will have a copy sent out to you post-haste. Sign up now!
	CONTRACT RESEARCH@markergene.com Marker Gene Technologies, Inc. has the expertise to perform contract research with you on your project. We have worked with many biotechnology and pharmaceutical companies on successful, proprietary and patented projects. Contract Research and Development Capabilities in the following areas: Established in 1993 at the University of Oregon Riverfront Research Park. Screening Assay Development for HTS and uHTS Chemical and Cellular Assays – High-Content Screening. DNA/RNA (genomics) and protein (proteomics) labeling and assay development. Pharmaceutical Intermediates - design, synthesis, and in vitro testing in mammalian cell culture. Specializing in Carbohydrate, Lipid, Peptide, and Nucleic Acid Chemistries. Fully equipped laboratories (Biochemistry, Chemical Synthesis, Tissue Culture, Analytical). Confidentiality, help in patent preparation and filings. Contact us by telephone at (888) 218-4062 or (541) 342-3760 or FAX us at (541) 342-1960 or you can write to us at Contract Research, Marker Gene Technologies, Inc., 1850 Millrace Drive, Eugene, Oregon 97403-1992 or contact us by e-mail at: techservice@markergene.com
	Marker Gene Accepts Major Credit Cards. Place your orders now, using Master Card or Visa and save time and money! Our Customer Assistance Staff can now accept either Master Card or Visa Credit Card orders, securely by telephone (toll-free) at 1-888-218-4062 (Domestic orders only). We will continue to accept Institutional Purchase Orders for our products, online or by FAX at 1-541-342-1960. International customers should contact us by e-mail, post or telephone for more information about International Distributors and ordering. For information on pricing for individual products, or for a quote on bulk quantities of our products or kits, please contact our technical assistance staff at techservice@markergene.com. We will be happy to assist you.
	To add your name to our WebNewsletter mailing list, please use the following link: subscribe@markergene.com. To unsubscribe from our mailing list, please use the following link: unsubscribe@markergene.com. Your e-mail address will be deleted in 2-3 business days.