SOMAmer reagents are selected using the SELEX (Systematic Evolution of Ligands using Exponential Enrichment) method, starting with libraries of 1015 molecules and iteratively narrowing that number based on affinity of the rounds of SELEX. Usually about 100 sequences are available after 6 – 8 rounds of SELEX that have acceptable affinity to the target. While all of the SOMAmer reagent candidates will bind the target to varying degrees, the properties of these reagents will vary, including their performance in any given application. While one sequence might perform well in one set of conditions, another sequence may perform better in another. SomaLogic has not tested all SOMAmer reagents in all applications. Please contact technical support at techsupport@somalogic.com or by telephone at 1-800-324-0783 or 303-625-9000 for any questions regarding our reagents.
Do I need to add a carrier to my SOMAmer reagent solution?
Protein carriers, such as bovine serum albumin (BSA), are not necessary for most applications. Addition of detergent, such as 0.001-0.05% Tween-20, will help prevent loss of SOMAmer reagent material to tube walls in very dilute solutions (< 100 pM total DNA). Precise conditions should be determined for each application before use.
What are reasonable storage and handling conditions for SOMAmer reagents? What is known about the stability as a function of temperatures, pH, and buffer conditions?

SOMAmer reagents are stable (e.g., 2 years at -20 °C, 3 months at 4 °C) in solution. SOMAmer reagents should be stored at -20 °C when not in use. They will degrade slowly due to routine sample handling at room temperature, and therefore aliquoting is a highly recommended strategy for long term use to avoid repeated freeze/thaw cycles. Some variation between individual SOMAmer reagents is to be expected.
Most typical buffers for biological applications (e.g., HEPES, Tris, PBS) will not adversely affect SOMAmer reagent stability. They are resistant to basic conditions, but will degrade rapidly at pH < 4. The presence of functional groups must also be considered. The standard SOMAmer reagent contains a biotin, which is susceptible to oxidation, especially under unbuffered and/or oxidative conditions.

Do I need to use a competitor in my assay?
Polyanionic competitors can reduce non-specific binding due to the modest affinities some proteins have for random DNA. We recommend using 1 μM SomaLogic Polyanionic Competitor (SomaLogic P/N 910-00001) or 1 mM dextran sulfate as a starting concentration for reducing artifacts for many applications. Higher competitor concentrations can be utilized post-equilibration to selectively enrich for specific binding. Precise conditions should be optimized for each application and SOMAmer reagent. See the Application Note on Polyanionic Competitor use for more details.
Why is a “heat/cool” protocol recommended for SOMAmer reagents?
Some SOMAmer reagent sequences have a tendency to aggregate, or become kinetically trapped in alternative inactive structures, and a heat/cool protocol will restore the correctly folded, monomeric
form. We recommend 5 minutes at 95 °C in a low salt buffer such as 5 mM HEPES, 1 mM EDTA, pH 7.5, followed by cooling to room temperature.
Can I use a SOMAmer reagent as an antagonist?
SOMAmer reagents generally bind conformational epitopes across large contact surface areas, and therefore often inhibit the activities of protein targets by competing with natural binding partners. For this reason, SOMAmer reagents antagonize many functions of their target proteins. If the catalog SOMAmer reagent binds your protein of interest but does not block a function of interest, a custom SOMAmer reagent with these properties may be developed through our SOMAmer Discovery Services business or by obtaining candidate SOMAmer reagents from the original SELEX experiments, called Rapid SOMAmer Candidate Discovery Service. Please contact SomaLogic Technical Support at techsupport@somalogic.com or by telephone at 1-800-324-0783 or 303-625-9000 for more information.
Can SOMAmer reagents be immobilized to solid supports?
SOMAmer reagents are supplied with a biotin moiety on the 5’ end. The biotin will bind to streptavidin coated resins, (i.e. streptavidin, NeutrAvidin, Avidin, CaptAvidin and other streptavidin conjugates) beads, plates and planar surfaces.
Can SOMAmer reagents be used in sandwich assays?
Many SOMAmer reagents have been successfully paired with an antibody for sandwich assays in plate-based (e.g. ELISA) and bead-based (e.g. Luminex) applications. SOMAmer-SOMAmer reagent sandwich pairs have been generated via sandwich SELEX to favor SOMAmer reagent binding to distinct epitopes, and they have also been shown to work in bead-based and plate-based sandwich assays (see Rohloff et al.). If you are interested in developing custom sandwich reagents, please see our application note on that topic and/or contact Technical Support at techsupport@somalogic.com or by telephone at 1-800-324-0783 or 303-625-9000.
Can SOMAmer reagents be used in vivo?

SOMAmer reagents can be used in vivo research purposes but are not intended for use in humans in vivo (i.e. clinical use).  SOMAmer reagents are nucleic acids; therefore, they are sensitive to degradation by plasma and tissue nucleases over time. While the chemical modifications on a SOMAmer reagent offer significant resistance to endonuclease degradation, additional modifications are often necessary for in vivo applications. SomaLogic recommends the addition of a 40 kDa PEG to the 5′ terminus to prevent renal elimination. In our experience, some SOMAmer reagents do show a partial loss in function upon PEG addition, but the majority do not. However, this modification (or one of similar size) is required for in vivo use in order to increase half-life values from minutes to hours. Phosphodiester backbone protection at nuclease-sensitive sites, including 2′-methoxy and phosphorothioate groups, will provide additional stability. With these modifications, plasma half-life values of 3-6 hours can be achieved in vivo. Cell culture media can contain nucleases, and therefore SOMAmer stability in culture media should be tested empirically.

Please contact SomaLogic Technical Support at techsupport@somalogic.com or by telephone at 1-800- 324-0783 or 303-625-9000 to discuss custom SOMAmer reagent optimization opportunities for optimal SOMAmer reagent performance in your application.

Has this product ever been used for an application that is not listed?
SOMAmer reagents are versatile reagents for use in many affinity-based applications and SOMAmer reagents have been shown to work in most applications that typically use antibodies to bind proteins. SOMAmer reagents have been shown to work in flow cytometry, ELISA-like experiments, sandwich assays with a paired antibody, histochemistry and protein affinity purification applications. Several application notes and references are available here. We encourage users to try SOMAmer reagents in novel applications. We welcome you to share your results and protocols with SomaLogic by contacting us at techsupport@somalogic.com.
How can I confirm SOMAmer reagent concentration?
SOMAmer reagents can be quantified by conjugation of the SOMAmer reagent to a fluorophore (streptavidin phycoerythrin for example), by measuring the absorbance at 260 nm, or by labeling the SOMAmers with a radioactive moiety. SOMAmer reagents are provided with a package insert containing the molar mass of the reagent.
How do I reduce the occurrence of non-specific binding with SOMAmer reagents?
Non-specific binding of SOMAmer reagents may be diminished by adding polyanionic competitors such as herring sperm DNA, yeast tRNA or the SomaLogic Polyanionic Competitor (SomaLogic P/N 910- 00001). After binding, the addition of low molecular weight dextran sulfate can also prevent re-binding of non-specific SOMAmers. Please refer to our application note on use of polyanionic competitors.
How do I release SOMAmer Reagents from solid supports?
Any strategy that releases biotin from streptavidin can be used, but caution is advised in low pH buffers, as SOMAmer reagents degrade rapidly at pH <4.
How do I release SOMAmer reagents from their cognate proteins?
SOMAmer reagents can be released from their targets by denaturation of the protein or denaturation of the SOMAmer reagent. Basic solutions (pH=10 or higher), elevated temperatures or chaotropic salts have successfully been employed.
How stable is the SOMAmer reagent in cell culture?
SOMAmer reagents contain modified nucleotides and a 3’ cap (inverted dT) and are more resistant to both endonuclease and exonuclease degradation than traditional aptamers. Even in as high as 90% human serum, SOMAmer reagents have a nine-fold longer half-life than unmodified DNAs of the same sequence (t 1⁄2 > 48 hours). SomaLogic has found SOMAmer reagents to be functional in cell culture assays for 24- 48 hours.
In which biological matrices will SOMAmer reagents work?
SOMAmer reagents are capable of measuring proteins in a wide array of biological matrices including human serum, plasma, cerebral spinal fluid (CSF), bronchoalveolar lavage (BAL), synovial fluid, nasal lavage, sputum, etc. In addition, many SOMAmer reagents generated to pure human proteins cross- react with non-human orthologues and therefore can be used in SOMAscan to identify differential expression of these analytes in non-human samples. (Please see SomaLogic’s SOMAscan Proteomic Assay Technical White Paper for more information.)
What buffers can I use when working with SOMAmer reagents?
It is recommended to use 40 mM HEPES, 100 mM NaCl, 5 mM KCl, 5 mM MgCl2, 1 mM EDTA, pH 7.5 (total NaCl of approximately 120 mM after pH adjustment with NaOH), as a working buffer.  Reagents are likely to perform well in buffers of similar ionic strength and pH, but activity should be tested empirically.
What do I do if the SOMAmer reagent does not work in my application of interest?
While each SOMAmer reagent is tested for affinity to its target, not all SOMAmer reagents have been tested in all applications. Contact technical support at techsupport@somalogic.com or by telephone at 1-800-324-0783 or 303-625-9000 for guidance on how to optimize your protocol for best results.
What is the optimal SOMAmer reagent working concentration?
SOMAmer reagent working concentrations are dependent on the application of interest, but generally range from 10 pM to 1 μM. Please refer to the application notes for guidelines on starting concentrations for various applications.
What kind of functional groups or fluorophores can I put on a SOMAmer reagent?
As synthetic oligonucleotides, SOMAmer reagents can be readily prepared with one or more of numerous functional groups for conjugation to beads or surfaces, as well as for detection in various applications. Our current SOMAmer reagent offering contains a biotin modification. Other typical modifications include an amine, thiol, and/or fluorophores. Custom functionalized SOMAmer reagents are available on request. For more information, please contact SomaLogic Sales at orders@somalogic.com or by telephone at 1-844-SOMAMER (1-844-766-2637) or the main number at 303-625-9000.
What level of multiplexing can be achieved with SOMAmer reagents?
SomaLogic currently offers commercial measurements of 1,310 unique human proteins in the SOMAscan assay. In proprietary testing, the multiplexing of over 4,000 SOMAmer reagents has been demonstrated with the SOMAscan assay.
Can I get a SOMAmer reagent for a protein not on the list?

Please contact SomaLogic regarding the availability of a reagent to your target of interest or about our SOMAmer Discovery Service. You may contact us or call us by telephone at 1-844-SOMAMER (1-844-766-2637) or the main number at 303-625-9000.

Can I have the sequence of the SOMAmer reagent that I am using?
The sequence is proprietary to SomaLogic and this information is not disclosed.
Can orders be expedited?
Yes, in most cases we can expedite orders for SOMAmer reagents that are in-stock. Please contact SomaLogic sales at orders@somalogic.com or by telephone at 1-844-SOMAMER (1-844-766-2637) or the main number at 303-625-9000 to discuss expedited orders.
Can I submit a bulk order?
SomaLogic will accept bulk orders for SOMAmer reagents and a discount may be available depending on the quantity ordered. Please contact Customer Service at orders@somalogic.com or by telephone at 1-844-SOMAMER (1-844-766-2637) or the main number at 303-625-9000 to place a bulk order.
Can SOMAmer reagents be ordered in different amounts?
We offer 500 pmoles of SOMAmer reagent stocks. If you would like to order in bulk amounts, please contact SomaLogic Sales directly at orders@somalogic.com or by telephone at 1-844-SOMAMER (1-844-766-2637) or the main number at 303-625-9000.
How long does it take to receive my order?
Most SOMAmer reagents are available in-stock at the time of your order, and your order will be processed within 5 business days, depending on quantity. You may expedite the shipping of your order by choosing overnight or the 2-day/Priority shipping option at check-out. Please note however, that international and bulk orders may take longer to process and that overnight delivery is not available to international orders.
How much variability is there between lots of SOMAmer reagents?
As synthetic oligonucleotides, the automated solid phase synthesis process followed by HPLC purification is robust and yields low variability between lots of a given SOMAmer reagent. Typical CVs for purity are 5.0%.
Is there another SOMAmer reagent available for my protein of interest?
Our goal is to provide you with the best reagent for your application. As such, SomaLogic can work with you on a SOMAmer Discovery Service project to deliver multiple SOMAmer reagents from a given SELEX to test in your application. Please contact SomaLogic Sales at orders@somalogic.com or by telephone at 1-844-SOMAMER (1-844-766-2637) or the main number at 303-625-9000 for more information.
What do I do if I am missing a tube or my package arrives damaged?
Contact SomaLogic at orders@somalogic.com or by telephone at 1-844-SOMAMER (1-844-766-2637) or the main number at 303-625-9000. Please be prepared with your order number, the name of the SOMAmer reagent, and a description of the condition in which the product was received.
What shall I do if the SOMAmer doesn’t work in my application?
While each SOMAmer reagent is tested for affinity to its target, not all SOMAmer reagents have been tested in all applications and as such, SomaLogic cannot guarantee that a SOMAmer Reagent will work in your specific application. Contact Technical Support at techsupport@somalogic.com or by telephone at 1-800-324-0783 or 303-625-9000 for ideas on how to optimize your protocol for best results.
Where can I find copies of documents, protocols, and publications?
Documents may be found on the SomaLogic website. If you cannot find a document, please contact Customer Service at orders@somalogic.com or by telephone at 1-844-SOMAMER (1-844-766- 2637) or the main number at 303-625-9000.
Whom do I contact with questions?

Please contact us via email, telephone, or the website.
Customer Service: orders@somalogic.com or 1-844-SOMAMER (1-844-766-2637)
Technical Support: techsupport@somalogic.com or 1-800-324-0783
Main Phone Number: 303-625-9000
Contact Form

Will you discontinue a SOMAmer reagent?
Through our process of continuous quality improvement, SomaLogic works to improve the affinity and specificity of existing SOMAmer reagents. Over time, SomaLogic may replace the currently available SOMAmer reagent for a given target with a new and improved reagent. Please contact SomaLogic Sales to for more information about a custom synthesis of a reagent at orders@somalogic.com or by telephone at 1-844-SOMAMER (1-844-766-2637) or the main number at 303-625-9000.
Do I need gloves to handle SOMAmer reagents? Are SOMAmer reagents biohazardous? How do I dispose of SOMAmer reagents?
Although SomaLogic has not thoroughly investigated the specific toxicity of each individual SOMAmer reagent, synthetic oligonucleotides are generally considered non-hazardous. SOMAmer reagents do contain functional groups, trace organic salts, and modified nucleic acid bases; therefore, all products should be handled with proper protective equipment (gloves, lab coats, etc.) and universal precautions. Always follow the safety and disposal guidelines for your institution.
Can matrices, high abundance proteins, or other substances interfere with SOMAmer reagent binding?
Binding characteristics of protein-binding reagents, whether SOMAmer reagents or antibodies, will vary depending on the matrix, relative protein concentrations of the target and related proteins, and other factors. Some proteins known to bind to DNA can lead to non-specific binding. Any substance that alters the structure of folded DNA (intercalating dyes for example) could alter the binding properties of SOMAmer reagents. A competitor or blocking reagent may be required, depending on the application.
Can SOMAmer reagents be selected against both non-glycosylated and glycosylated target proteins?
SOMAmer reagents may be selected against non-glycosylated or glycosylated target proteins, and generally binds both forms. However, exceptions may exist, for example if a sugar group sterically blocks the epitope of a SOMAmer reagent selected against a non-glycosylated form, or if glycosylation causes a conformational change in the protein.
Do SOMAmer reagents recognize denatured proteins or linear epitopes?
SOMAmer reagents bind large, conformational epitopes and, therefore, generally do not bind fully denatured target protein or linear epitopes.  However, SOMAmer reagents may bind partially denatured target proteins if the epitope retains enough tertiary structure.  Please see Jarvis et al. 2015 Structure 23:1-12, Gelinas et al 2014 JBC 289:8720-8734 and Davies et al 2012 PNAS USA 109: 19971-19976 for additional details.
Do SOMAmer reagents recognize post-translational modifications (PTMs)?
SOMAmer reagents typically bind a structure defined by the polypeptide chain. The effect of various PTMs on the binding of a given SOMAmer-protein pair have not been determined for each reagent. SOMAmer reagents that recognize a specific form of a protein with or without a PTM may be identified through our SOMAmer Discovery Service business.
How do I improve specificity in my assay?
Addition of a competitor into a given assay will generally improve specificity. Please refer to the application note on Polyanionic Competitor (P/N 910-00001) use for more details. If you are interested in developing a reagent with unique specificity requirements (e.g. binds one form of a protein and not another or binds all proteins in a given class), please contact SomaLogic at orders@somalogic.com or by telephone at 1-844-SOMAMER (1-844-766-2637) or the main number at 303-625-9000.
How do you define the purity of a SOMAmer reagent?

The presence of a variety of low level impurities is an inherent challenge in solid phase phosphoramidite synthesis of long oligonucleotides (e.g., N > 50). The highest abundance impurities are slightly shorter versions of the oligonucleotide, missing the 5’ modification, one or more of the 5’ nucleotides, an internal nucleotide, and some combination thereof. Because these molecules differ very slightly from the parent compound, it is difficult to obtain baseline resolution in the chromatographic analysis. In addition, many of these compounds are fully active, and are more correctly thought of as “product-related compounds” and not as impurities or contaminants.
It is our philosophy to obtain the highest quality analytical data, and we therefore determine chromatographic purity using a UPLC system and a slow reverse phase gradient, and conservatively cut all partially resolved shoulders when determining the purity value. This typically results in reported purity values in the 50-80% range. This conservative approach allows better evaluation of lot-to-lot consistency. The reported purity may seem low to scientists accustomed to small molecule purity values, which are typically much higher. Therefore, this value should be evaluated together with the functional data (e.g., the binding constant) to properly assess performance of the SOMAmer reagent.

How is SOMAmer reagent specificity determined?
SOMAmer reagents are tested in an affinity capture assay to determine cross reactivity to similar proteins using the SOMAmer target protein as well as closely related proteins (50% or greater identity). Affinity curves are generated for any off-target proteins that demonstrate binding to a SOMAmer reagent in order to determine relative affinities compared to target binding. These results are available on the specification sheets for each reagent.
How is the dissociation constant (Kd) determined in functional testing of a particular protein-SOMAmer interaction?
We perform solution-phase affinity measurements using several methods, depending on the nature of the protein being studied. All measurements are performed with purified protein. In the case of proteins with recombinant tags (i.e. poly-Histidine or Fc) we typically use an AlphaScreen® (Perkin Elmer®) proximity method to detect association of the tagged protein with a biotinylated SOMAmer reagent. In the case of untagged proteins, we typically measure the association of radiolabeled SOMAmer reagent with protein and capture the complex using a non-specific protein-capturing chromatography medium. Saturation binding curves are generated by titrating increasing amounts of protein in the presence of a constant amount of SOMAmer reagent. In the event that the protein-SOMAmer complex cannot be captured, we perform an electrophoretic mobility shift assay (EMSA) in which protein-SOMAmer complexes are detected by a shift in electrophoretic mobility of the radiolabeled SOMAmer reagent on a native gel. The Kd is determined to be the protein concentration at which the half maximal binding is observed. The reported Kd and the Kd measured by the end user may differ based on the assay format, assay conditions, protein source, protein sample purity, or protein modification. Please review the Specification Sheet and Certificate of Analysis for more information on the Kd for a specific SOMAmer reagent.
In what pH range do SOMAmer reagents work?
SOMAmer reagent binding is selected for and tested at pH 7.5. Binding at different pH values should be evaluated for each SOMAmer reagent-protein pair since binding is dependent on proper folding of both the SOMAmer reagent and the protein.
Is it known where the SOMAmer reagent binds the target protein?
Crystal structure analyses of a small number of SOMAmer reagent-protein complexes indicate SOMAmer reagents bind large, conformational epitopes, but the exact epitope of each SOMAmer reagent is not known. Please see Jarvis et al. 2015 Structure 23:1-12, Gelinas et al 2014 JBC 289:8720-8734 and Davies et al 2012 PNAS USA 109: 19971-19976 for additional details.
What are the advantages of SOMAmer reagents over antibodies?
SOMAmer reagents  have several distinct advantages over antibodies, including customized in vitro selection conditions, consistent chemical synthesis, superior storage stability, reversible denaturation, and utility in highly multiplexed ligand-binding assays.
What buffers are not compatible with SOMAmer reagents?
Since SOMAmer reagent-protein binding is dependent on proper folding of both the SOMAmer reagent and the protein, denaturing solutions should be avoided. Reducing agents will not affect SOMAmer reagent structure, but are not compatible for proteins containing disulfide bonds. Addition of 1 mM EDTA is acceptable, but higher concentrations should be used with caution since some SOMAmer reagent structures may utilize divalent cations.
Are SOMAmer reagents resistant to nucleases?
SOMAmer reagents are nucleic acids and are sensitive to degradation by endonucleases and exonucleases that recognize DNA substrates. While the chemical groups on a SOMAmer reagent offer significant resistance to endonuclease degradation, additional modifications are often necessary for applications where nucleases may be present. SomaLogic has added an inverted dT to the 3′ terminus of the SOMAmer reagents to block exonuclease degradation. Protection against endonucleases is possible via 2′-methoxyribosesor phosphorothioate groups. Please contact SomaLogic Technical Support at techsupport@somalogic.com or by telephone at 1-800-324-0783 or 303-625-9000 to discuss custom SOMAmer reagent optimization opportunities for optimal SOMAmer reagent performance in applications where nuclease stability is required.
Am I permitted to amplify the SOMAmer reagent instead of purchasing more?
No, the sequence is proprietary to SomaLogic and any attempt to determine the sequence is a violation of the license terms that you agreed to upon purchase of the SOMAmer reagent.   In the event that we determine that you attempted to reverse engineer the SOMAmer reagent, we reserve the right to no longer provide you SOMAmer reagents.
Can I re-use a SOMAmer reagent?
The answer will vary by application, but in general, SOMAmer reagents can be repeatedly denatured by heat or high pH and re-natured to a fully-active form for re-use.
Am I permitted to sequence a SOMAmer reagent?
No, the sequence is proprietary to SomaLogic and any attempt to determine the sequence is a violation of the license terms that you agreed to upon purchase of the SOMAmer reagent.  In the event that we determine that you attempted to reverse engineer the SOMAmer reagent, we reserve the right to no longer provide you SOMAmer reagents.
Do SOMAmer reagents bind their cognate proteins in organic solvents?
SOMAmer reagents are selected to bind their target proteins in an aqueous buffer at pH 7.5 and physiologic ionic strength. In organic solvents, a SOMAmer reagent will likely denature and no longer bind its target protein. However, SOMAmer reagents that have been exposed to organic solvents can be reconstituted in an appropriate aqueous buffer and regain full binding activity after heating to 95°C for 5 minutes and cooling to room temperature, provided the organic solvent did not chemically alter the SOMAmer reagent.
Do SOMAmer reagents run on agarose gels in the same manner as unmodified DNA?
SOMAmer reagents have a phosphodiester backbone and therefore behave much like unmodified DNA or RNA in gel electrophoresis, migrating according to size. The length of a SOMAmer reagent typically ranges from 25-80 nucleotides, and therefore separation can be achieved on 8-20% polyacrylamide Tris-borate-EDTA (TBE) gels containing 8M urea as a denaturant.
How is the extinction coefficient determined?
The extinction coefficients of SOMAmer reagents are determined using the nearest neighbor method for estimation of extinction coefficients of oligonucleotides (Cantor, C.R. et al., Biopolymers, 9, 1059- 1077., Cavaluzzi, M.J. and Borer, P.N., Nucleic Acids Res., 32, e13). The third term in the equation in the references accounts for the proprietary modifications of SOMAmer reagents. Extinction coefficients are determined for each new modified nucleoside (nucleotide) as they are introduced into newly discovered SOMAmer reagents. Sequence-specific extinction coefficients are included on the Certificate of Analysis.
What are the melting temperatures (Tm) of the folded SOMAmer reagent structures?
The selection experiments used to discover SOMAmer reagents were performed at 37°C, so the bound, folded structures of the SOMAmer reagents are stable at this temperature and below. The melting temperatures of the majority of the SOMAmer reagents have been measured in solution without protein present and are 50-65°C. The transitions are typically broader than those observed for double stranded DNA. The bound forms of the SOMAmer reagents are expected to be more stable.
In what buffers are SOMAmer reagents compatible?
SomaLogic recommends reconstitution in deionized water to 50 μL, which will result in 5 mmol HEPES at pH 8.0, 1 mM EDTA, and 10 μM of Reagent. Most buffers near physiological ionic strength and pH should are compatible, but controlled binding experiments in buffers suitable for the intended application are recommended.
What is the composition of SOMAmer reagents?

SOMAmer reagents are synthetic oligonucleotides with standard DNA 2’-deoxynucleotides as well as unique modified nucleotides developed by SomaLogic (see Vaught et. al., JACS, 2010, 132, 4141-4151). In addition, each SOMAmer reagent can be modified with a capture (biotin or amine), conjugation (amine or thiol), or detection moiety (fluorophore) on the 5′ end and an inverted dT on the 3’ end.  Custom orders may be requested by contacting SomaLogic Sales at orders@somalogic.com or by telephone at 1-844-SOMAMER (1-844-766-2637) or the main number at 303-625-9000.)

Why are the SOMAmer reagent quantities reported in nmol instead of mg?

SOMAmers are high-affinity binding reagents and this facilitates determination of the quantities needed for experiments. The molecular mass is provided for those who prefer to convert to mass.