February 14th, 2013
Monoclonal Antibody to Polyhistidine (HIS)-tag
MAB230P, a monoclonal antibody specific for the polyhistidine (HIS) tag, is part of a growing list of MBS products aimed at assisting our customers in the detection of recombinant proteins. HIS-tag is the most popular recombinant protein tag and MAB230P is being widely sampled and used by customers with need for a high affinity, highly specific HIS-tag antibody. MBS R&D developed the murine antibody using 6X-His-KLH. The internal development and production of MAB230P allows MBS to maintain the highest quality standards and the ability to offer the lowest possible price.
Click here to read more about the Forte Bio Dip and Read™ Anti-HIS (HIS2) Biosensors and MAB230P
Monoclonal Antibody to Maltose Binding Protein (MBP)
Maltose Binding Protein (MBP) tags have demonstrated utility to increase expression and proper folding of proteins expressed in bacteria leading to improved solubility of the partner protein.
Maine Biotechnology Services Inc has developed a monoclonal antibody specific for Maltose Binding Protein (MBP) to optimize detection and purification of recombinant proteins utilizing MBP tags. MAB231P has been confirmed by Western Blot and ELISA to recognize MBP irrespective of the vector used for expression.
Several recent publications bring to light the superior performance of maltose binding protein in a variety of applications including, the ability of MBP to improve soluble expression(1), act as a carrier and delivery system for fused proteins to target antigens(2), increasing the solubility of drug candidates(3), and even experimental therapeutic uses(4).
1.The ability to enhance the solubility of its fusion partners is an intrinsic property
of maltose-binding protein but their folding is either spontaneous or chaperone-mediated.
Raran-Kurussi S, Waugh DS.
2. Maltose-binding protein is a potential carrier for
oral immunizations, Veterinary Immunology and Immunopathology,
P.Bellot,P.Tiels, V.Melkebeek, B.Devriendt, B.M.Goddeeris, E. Cox,
3. A chromatography-focused bioprocess that eliminates soluble aggregation
for bioactive production of a new antimicrobial peptide candidate,
Xiang Li, Susanna Su Jan Leong,
4. Synergistic antitumor effects of Escherichia coli maltose
binding protein and Bacillus Calmette–Guerin in a mouse lung carcinoma model
Qingyong Zhang, Weihua Ni, Xiaoxia Zhao, Fengli Wang, Zhuo Gao, Guixiang Tai,
December 12th, 2013
Portland, Maine- In July 2012, Maine Biotechnology Services entered into a partnership with Dr. Scott McVey, supervisor of the USDA-Agricultural Research Service (USDA-ARS) Arthropod Borne Animal Disease Research Unit, with the objective of developing monoclonal antibodies to support ongoing research efforts to advance adequate vaccine and rapid detection methods for Rift Valley Fever Virus in Africa. MBS is announcing the release of the first two antibodies resulting from that partnership; a functioning matched pair demonstrating specificity to the nucleocapsid protein of the virus. These antibodies have applications as detection reagents for circulating antigen, mosquito carriers, or as components of differentiation of infected and vaccinated animals (DIVA) assays. In the final phase of validation for the antibodies, Dr. McVey intends to deliver them to USDA-ARS partnered laboratories in South Africa and other endemic African nations for assay development with clinical samples. Future goals of the MBS-USDA-ARS Rift Valley Fever program include the development of antibodies to the Gn and NSs proteins to support vaccine programs.
About Rift Valley Fever Virus: Rift Valley Fever is a devastating virus transmitted by mosquitoes that affects both animals and humans. The disease results in significant economic losses due to death and abortion in RVFV infected livestock. Originating in the Rift Valley of Kenya, outbreaks of the virus now occur in all areas of sub-Saharan and North Africa. Cases have also been confirmed in Yemen and Saudi Arabia, causing widespread concern about the vulnerability of parts of Asia and Europe involved in livestock trade with Africa.
About Maine Biotechnology Services: Maine Biotechnology Services is a premier provider of antibody services, from design and development to production and characterization. MBS extends the creativity and experience necessary for the most complex hybridoma development projects. A wide variety of tools are utilized by MBS to allow customers the opportunity to refine clone selection early in a project, and to support prototype assay validation. Collaboration opportunities combine 25 years of custom hybridoma development experience at MBS with academic expertise on a target of shared interest.
For more information contact:
Maine Biotechnology Services
1037R Forest Ave.
Portland, Maine 04103
November 7th, 2013
Two monoclonal antibodies to the nucleocapsid protein of Rift Valley Fever Virus (RVFV) are now available for sampling from MBS R&D. The clones are a result of a partnership between MBS and the USDA-Agricultural Research Service (USDA-ARS) to develop detection reagents for RVFV assays.
For this project, mice were immunized with RVFV lysates and screened for recognition of recombinant nucleocapsid protein (rNP). The clones were screened by USDA-ARS by indirect ELISA against native virus to confirm specificity. A sandwich ELISA against rNP demonstrated a sensitivity level of at least 6 ng/ml.
In the final phase of validation for the antibodies, Dr. Scott McVey, supervisor of the USDA Arthropod Borne Animal Disease Research Unit (ABADRU), intends to deliver them to the USDA-ARS partnered laboratories in South Africa and other endemic African nations for assay development with clinical samples. Future goals of the MBS-USDA-ARS Rift Valley Fever program include the development of antibodies to the Gn and NSs proteins to support vaccine programs.
Link to the USDA Project Description
October 4th, 2013
MBS has long used Protein A with pH gradient elution for the purification of murine monoclonal IgG antibodies. By providing the gentlest conditions possible we have been able to offer our customers consistent monomer IgG purity of ~95%. When circumstances warrant, we also offer the highest quality standards in Protein G and Immunoaffinity Chromatography techniques. Increasingly, however, our custom antibody development customers have therapeutic research goals that may require an even higher level of antibody purity.
To meet those customer’s needs, MBS is now offering an additional Size Exclusion Chromatography polishing step to be added to one of our standard purification protocols. Removal of misfolded and confounding IgG dimers and higher molecular weight aggregates consistently results in antibody preparations >99% pure. Soluble aggregates can cause non-specific background problems, loss of sensitivity and variability in immunoassays that can severely confound clinical studies.
Increasing Your Antibody Purity
Industry Standard MBS Protein A Purified MBS Protein A with
Protein A Purified Antibody Antibody SEC Polishing
(80-90% Purity) (~95% Purity) (>99% Purity)
Applications that customers have requested ~99% purity for:
- Clinical Assays
- Bridging Assays
- Gold Conjugations
September 13th, 2013
MBS R&D began a Cystatin C monoclonal antibody development project with the goal of developing a diagnostic grade, matched pair capable of detecting human Cystatin C in clinical samples. The resultant monoclonal antibodies; MAB236P, MAB237P and MAB238P, far exceed that development goal, recognizing Cystatin C in ng/mL concentrations. The two best matched pairs detect Cystatin C present in normal human serum and purified from urine.
Now widely used for diagnostic applications, these monoclonals are the affordable, highly sensitive solution you are looking for in your assay. Backed by extensive product support and produced under cGMP conditions, MAB236P, MAB237P and MAB238P provide customers with the best value in the marketplace.
Sandwich ELISA Data
A sandwich ELISA was performed using MAB236P or MAB237P as capture and MAB238P-biotin as tracer. Cystatin C purified from human urine was spiked into sample diluent and serially diluted from 3.12ng/ml to 0.025ng/ml.
A second sandwich ELISA was run using normal human serum as the sample to demonstrate that the two matched pairs are able to detect Cystatin C present in serum. The data indicates that both matched pairs are able to detect and measure Cystatin C in the serum matrix.
*Although Cystatin C circulates in serum at μg/ml range, the MBS Cystatin C matched pair antibodies function in the ng/ml range.
July 18th, 2013
MBS MAB230P, monoclonal antibody to (His) tag has now been incorporated into Forte Bio Anti-HIS biosensors for rapid quantitative measurement. The antibody is identified by the kit insert as being high affinity and highly specific. MBS is proud to offer MAB230P according to the highest quality standards and at a bulk manufacturing friendly price.
Click here to read more about the Forte Bio Dip and Read™ Anti-HIS (HIS2) Biosensors and MAB230P
May 14th, 2013
MAB234P and MAB235P, monoclonal antibodies to progesterone, are now ready for sampling.
The most accurate formats for measurement of progesterone in clinical samples are competition and/or inhibition assays since the molecule is only 314 daltons. Progesterone in a clinical sample competes with a carefully chosen conjugated progesterone reagent for available binding sites on a capture antibody specific for progesterone. The signal seen in a competitive immunoassay is inversely proportional to the amount of progesterone present in a sample.
Progesterone Molecular Structure and Numbering of Positions
MAB234P – Generated using progesterone-6-KLH immunogen
MAB235P – Generated using progesterone-11-KLH immunogen
A successful, specific clinical progesterone competition assay is dependent on the optimized pairing of a competition progesterone reagent with the anti-progesterone antibody. It is critical to understand the compatibility of the competition reagents used. Knowing the attachment point used in the chosen progesterone conjugate is important, as steric interactions can play a role in confounding an assay if the epitopes on the conjugate are blocked by the attached detection enzyme. The conjugation ratio used to develop the progesterone competition reagent can also have an effect on assay sensitivity and should be considered.
For the validation of MAB234P and MAB235P as capture antibodies, MBS used internally developed competition progesterone conjugates in a series of competitive ELISAs to look at antibody sensitivity and specificity. A limited supply of those progesterone conjugates are available for sampling with MAB234P and 235P while supplies last. MBS R&D assays demonstrated sensitivity levels within the normal clinical range for detection of progesterone.
April 29th, 2013
Amid a wave of acquisitions and outsourced manufacturing by antibody service providers, MBS wants to reassure our customers that they can count on the stability and longevity of our organization. MBS has been privately owned and operated in New England since 1990. We have stayed true to our core proficiency and quality standards in antibody development, while continuously striving to add to our expertise and tools to assure the highest quality project outcomes.
The cornerstones of our success have always been customer communication and in-house project management. In 2013, MBS plans to add electrofusion to our hybridoma development services which also include innovative purification protocols and Octet kinetic analysis. Investing in our technical capabilities to meet evolving customer needs signals our commitment to remaining your partner in antibody development well into the future.
Browse our site to learn more about the cGMP antibody services offered by MBS:
Custom Monoclonal Antibody Development
Interaction Analysis via Octet
Prototype Assay Development
Polyclonal Antibody Development and Affinity Purification
Ascites and In Vitro Antibody Production
Optimized Antibody Purification
Antibody Characterization Services
Growing Catalog of MBS Produced Antibodies
February 27th, 2013
MBS is now offering two antibodies specific for lactoferrin, MAB232P, and MAB233P. Lactoferrin is part of the transferrin family of proteins, an iron binding glycoprotein involved in host defense against infection and is a modulator of inflammatory reactions.
The antibodies were evaluated for their ability to work as matched pairs in a mono-mono sandwich ELISA format. Biotin conjugates of both antibodies were prepared for use as tracers. The antibodies demonstrated the ability to work in both capture/tracer configurations.
Both monoclonal antibodies were evaluated by indirect ELISA and sandwich ELISA (data not shown) for cross-reactivity to transferrin, both Apo (iron-free) and Holo (iron-saturated) forms. The results suggest that neither antibody cross-reacts with transferrin to a significant degree.
January 16th, 2013
In response to customer inquiries, MBS announces the expansion of contract services offered to include ELISA development. The assay development service will provide customers with refined, R&D use assays at the end of hybridoma development. Optimization of reagents for assay applications has long been an area of core competency for MBS, used heavily in the development of internal products and services. It is with great excitement that we will, for the first time, be extending the benefit of that experience to our hybridoma development customers.
Included in the service will be the development of an optimized ELISA using your predicted matrices, transfer of protocols, and training support; making our lab an extension of yours.