Creative Biolabs

Last updated
Creative Biolabs, Inc.
Company type Corporation
Industry Biotechnology
Founded2005
Headquarters45-1 Ramsey Road, Shirley, New York 11967,
US
ProductsPremade antibody, peptide libraries
ServicesAntibody discovery services, antibody engineering services, bio-manufacturing
Website www.creative-biolabs.com/aboutus.html

Creative Biolabs, Inc. is a life-science company which produces and supplies biotech products and services for early drug discovery and development, including various phage display libraries [1] such as pre-made libraries, [2] phage display services, [3] [4] antibody sequencing, [5] and antibody humanization. [6] Customers include pharmaceutical companies, academic institutions, government agencies, clinical research organizations and biotechnology companies.

Contents

History

Creative Biolabs Inc. was founded in 2005 by a group of scientists researching on the treatment and prevention of intractable diseases like cancer. The company has distributors in Australia, New Zealand, Japan and other countries in Europe, Asia, and America. Its headquarter is in Shirley, New York. [7] In June 2017, Creative Biolabs set up its first scholarship program. [8]

Services

Fab construction [9] is a complex technique as Fab fragments contain both variable domains and constant regions. The same heavy and light variable chains used for scFv construction can be used in the construction of Fab.

Construction of pre-made phage display libraries. Pre-made phage display library [10] is a laboratory technique for the study of protein–protein, protein–peptide, and protein–DNA interactions that uses bacteriophages (viruses that infect bacteria) to connect proteins with the genetic information that encodes them.

Sequencing services [11] such as Database Assisted Shotgun Sequencing (DASS) technology

Analysis of microarray hybridization data [12]

Yeast two-hybrid screen [13]

Products

Monoclonal antibodies such as mouse anti-human Duox2 monoclonal antibody S-40 [14]

Immunoglobulin Y (IgY) such as Anti-ADP3 chicken IgY [15]

Antibody libraries such as HuSdLTM phage display human single domain antibody library [16]

Response to COVID-19

Creative Biolabs offers SARS-CoV-2 S antibodies that come from common hosts like human, mouse, and rabbit, and apply to various lab tests, like ELISA, FC, ICC/IF, etc. Apart from S protein antibodies, Creative Biolabs also provides a comprehensive list of anti-SARS-CoV-2 antibodies to assist with the research and development of drug and vaccine candidates, including but not limited to antibodies targeting genes like N, S1/S2, and ORF7a. [17]

Creative Biolabs Scholarship Program

Since the first scholarship program in 2017, Creative Biolabs has released scholarship every year. The scholarship award of $1,000 is given to one student of freshman, undergraduate, graduate or Ph.D. level majoring in science-related fields such as Biology, Biochemistry, Chemistry and Molecular Biology. [18]

Related Research Articles

<span class="mw-page-title-main">Antibody</span> Protein(s) forming a major part of an organisms immune system

An antibody (Ab), also known as an immunoglobulin (Ig), is a large, Y-shaped protein used by the immune system to identify and neutralize foreign objects such as pathogenic bacteria and viruses. The antibody recognizes a unique molecule of the pathogen, called an antigen. Each tip of the "Y" of an antibody contains a paratope that is specific for one particular epitope on an antigen, allowing these two structures to bind together with precision. Using this binding mechanism, an antibody can tag a microbe or an infected cell for attack by other parts of the immune system, or can neutralize it directly.

<span class="mw-page-title-main">Monoclonal antibody</span> Antibodies from clones of the same blood cell

A monoclonal antibody is an antibody produced from a cell lineage made by cloning a unique white blood cell. All subsequent antibodies derived this way trace back to a unique parent cell.

<span class="mw-page-title-main">Phage display</span> Biological technique to evolve proteins using bacteriophages

Phage display is a laboratory technique for the study of protein–protein, protein–peptide, and protein–DNA interactions that uses bacteriophages to connect proteins with the genetic information that encodes them. In this technique, a gene encoding a protein of interest is inserted into a phage coat protein gene, causing the phage to "display" the protein on its outside while containing the gene for the protein on its inside, resulting in a connection between genotype and phenotype. The proteins that the phages are displaying can then be screened against other proteins, peptides or DNA sequences, in order to detect interaction between the displayed protein and those of other molecules. In this way, large libraries of proteins can be screened and amplified in a process called in vitro selection, which is analogous to natural selection.

<span class="mw-page-title-main">Single-chain variable fragment</span> Fragment

A single-chain variable fragment (scFv) is not actually a fragment of an antibody, but instead is a fusion protein of the variable regions of the heavy (VH) and light chains (VL) of immunoglobulins, connected with a short linker peptide of ten to about 25 amino acids. The linker is usually rich in glycine for flexibility, as well as serine or threonine for solubility, and can either connect the N-terminus of the VH with the C-terminus of the VL, or vice versa. This protein retains the specificity of the original immunoglobulin, despite removal of the constant regions and the introduction of the linker. The image to the right shows how this modification usually leaves the specificity unaltered.

<span class="mw-page-title-main">Gregory Winter</span> English biochemist (born 1951)

Sir Gregory Paul Winter is a Nobel Prize-winning English molecular biologist best known for his work on the therapeutic use of monoclonal antibodies. His research career has been based almost entirely at the MRC Laboratory of Molecular Biology and the MRC Centre for Protein Engineering, in Cambridge, England.

<span class="mw-page-title-main">Single-domain antibody</span> Antibody fragment

A single-domain antibody (sdAb), also known as a Nanobody, is an antibody fragment consisting of a single monomeric variable antibody domain. Like a whole antibody, it is able to bind selectively to a specific antigen. With a molecular weight of only 12–15 kDa, single-domain antibodies are much smaller than common antibodies which are composed of two heavy protein chains and two light chains, and even smaller than Fab fragments and single-chain variable fragments.

<span class="mw-page-title-main">Immunoglobulin heavy chain</span> Large polypeptide subunit of an antibody

The immunoglobulin heavy chain (IgH) is the large polypeptide subunit of an antibody (immunoglobulin). In human genome, the IgH gene loci are on chromosome 14.

<span class="mw-page-title-main">CD40 (protein)</span> Mammalian protein found in Homo sapiens

Cluster of differentiation 40, CD40 is a type I transmembrane protein found on antigen-presenting cells and is required for their activation. The binding of CD154 (CD40L) on TH cells to CD40 activates antigen presenting cells and induces a variety of downstream effects.

Humanized antibodies are antibodies from non-human species whose protein sequences have been modified to increase their similarity to antibody variants produced naturally in humans. The process of "humanization" is usually applied to monoclonal antibodies developed for administration to humans. Humanization can be necessary when the process of developing a specific antibody involves generation in a non-human immune system. The protein sequences of antibodies produced in this way are partially distinct from homologous antibodies occurring naturally in humans, and are therefore potentially immunogenic when administered to human patients. The International Nonproprietary Names of humanized antibodies end in -zumab, as in omalizumab.

<span class="mw-page-title-main">Protein A</span>

Protein A is a 42 kDa surface protein originally found in the cell wall of the bacteria Staphylococcus aureus. It is encoded by the spa gene and its regulation is controlled by DNA topology, cellular osmolarity, and a two-component system called ArlS-ArlR. It has found use in biochemical research because of its ability to bind immunoglobulins. It is composed of five homologous Ig-binding domains that fold into a three-helix bundle. Each domain is able to bind proteins from many mammalian species, most notably IgGs. It binds the heavy chain within the Fc region of most immunoglobulins and also within the Fab region in the case of the human VH3 family. Through these interactions in serum, where IgG molecules are bound in the wrong orientation, the bacteria disrupts opsonization and phagocytosis.

<span class="mw-page-title-main">Monoclonal antibody therapy</span> Form of immunotherapy

Monoclonal antibodies (mAbs) have varied therapeutic uses. It is possible to create a mAb that binds specifically to almost any extracellular target, such as cell surface proteins and cytokines. They can be used to render their target ineffective, to induce a specific cell signal, to cause the immune system to attack specific cells, or to bring a drug to a specific cell type.

A bispecific monoclonal antibody is an artificial protein that can simultaneously bind to two different types of antigen or two different epitopes on the same antigen. Naturally occurring antibodies typically only target one antigen. BsAbs can be manufactured in several structural formats. BsAbs can be designed to recruit and activate immune cells, to interfere with receptor signaling and inactivate signaling ligands, and to force association of protein complexes. BsAbs have been explored for cancer immunotherapy, drug delivery, and Alzeimer's disease.

<span class="mw-page-title-main">IGHG1</span> Gene in the species Homo sapiens

Ig gamma-1 chain C region is a protein that in humans is encoded by the IGHG1 gene.

2F5 is a broadly neutralizing human monoclonal antibody (mAb) that has been shown to bind to and neutralize HIV-1 in vitro, making it a potential candidate for use in vaccine synthesis. 2F5 recognizes an epitope in the membrane-proximal external region (MPER) of HIV-1 gp41. 2F5 then binds to this epitope and its constant region interacts with the viral lipid membrane, which neutralizes the virus.

<span class="mw-page-title-main">Cambridge Antibody Technology</span> Defunct British biotechnology company

Cambridge Antibody Technology was a biotechnology company headquartered in Cambridge, England, United Kingdom. Its core focus was on antibody therapeutics, primarily using Phage Display and Ribosome Display technology.

Avimers are artificial proteins that are able to specifically bind to certain antigens via multiple binding sites. Since they are not structurally related to antibodies, they are classified as a type of antibody mimetic. Avimers have been developed by the biotechnology company Avidia, now part of Amgen, as potential new pharmaceutical drugs.

Eldelumab is a fully human monoclonal antibody that targets chemokine ligand 10 (CXCL10)/Interferon-γ-inducible protein-10 (IP-10) designed for the treatment of Crohn's disease and ulcerative colitis.

Synthetic antibodies are affinity reagents generated entirely in vitro, thus completely eliminating animals from the production process. Synthetic antibodies include recombinant antibodies, nucleic acid aptamers and non-immunoglobulin protein scaffolds. As a consequence of their in vitro manufacturing method the antigen recognition site of synthetic antibodies can be engineered to any desired target and may extend beyond the typical immune repertoire offered by natural antibodies. Synthetic antibodies are being developed for use in research, diagnostic and therapeutic applications. Synthetic antibodies can be used in all applications where traditional monoclonal or polyclonal antibodies are used and offer many inherent advantages over animal-derived antibodies, including comparatively low production costs, reagent reproducibility and increased affinity, specificity and stability across a range of experimental conditions.

Tse Wen Chang is an immunology researcher, whose career spans across academia and industry. His early research involving the Immunoglobulin E (IgE) pathway and antibody-based therapeutics lead to the development of omalizumab, a medication that has been approved for the treatment of severe allergic asthma and severe chronic spontaneous urticaria. Chang is a cofounder of Tanox, a biopharmaceutical company specialized in anti-IgE therapies for the treatment of allergic diseases. After Tanox's tripartite partnership with Genentech and Novartis was forged in 1996, Chang returned to his alma mater, the National Tsing Hua University in Taiwan and served as the Dean (1996–1999) of the College of Life Sciences. Chang was appointed by the Taiwanese government as President of the Development Center for Biotechnology (DCB) in 2000, and served as a Science and Technology Advisor of the Executive Yuan from 2002 to 2006. From 2006 to 2016, he was tenured as Distinguished Research Fellow at the Genomics Research Center, Academia Sinica. He founded Immunwork, Inc. in 2014.

Recombinant antibodies are antibody fragments produced by using recombinant antibody coding genes. They mostly consist of a heavy and light chain of the variable region of immunoglobulin. Recombinant antibodies have many advantages in both medical and research applications, which make them a popular subject of exploration and new production against specific targets. The most commonly used form is the single chain variable fragment (scFv), which has shown the most promising traits exploitable in human medicine and research. In contrast to monoclonal antibodies produced by hybridoma technology, which may lose the capacity to produce the desired antibody over time or the antibody may undergo unwanted changes, which affect its functionality, recombinant antibodies produced in phage display maintain high standard of specificity and low immunogenicity.

References

  1. ↑ "Creative Biolabs Works with UEC for Commercial Phage Display Technology". PR.com. Retrieved 2017-05-18.
  2. ↑ Fukunaga, K; Taki, M (2012). "Practical Tips for Construction of Custom Peptide Libraries and Affinity Selection by Using Commercially Available Phage Display Cloning Systems". J Nucleic Acids. 2012: 295719. doi: 10.1155/2012/295719 . PMC   3444042 . PMID   22991651.
  3. ↑ "Creative Biolabs Announced Phage Display Technology For Anti-membrane Protein Antibody Production". BioSpace. Retrieved 2017-05-18.
  4. ↑ "Creative Biolabs Announces A Successful Completion Of Virbac's Unique Monoclonal Antibody Discovery Project Through Cooperation With In-Cell-Art". ASK. Retrieved 2017-05-18.
  5. ↑ "Creative Biolabs Introduces Innovative Antibody Sequencing Service with DASS Technology for Quicker Testing and Guaranteed Results". PRWeb. Retrieved 2017-05-18.
  6. ↑ "Creative Biolabs Updates Its Antibody Humanization Service to Further Accelerate Your Monoclonal Antibody Research". EIN Presswire. 8 August 2015. Retrieved 2017-05-18.
  7. ↑ "Company Overview of Creative Biolabs Inc". Bloomberg. Retrieved 2017-05-18.
  8. ↑ "Creative Biolabs Scholarship Program". The Company of Biologists. Retrieved 2017-05-18.
  9. ↑ Wanczyk, Heather; Barker, Tolga; Rood, Debra; Zapata, Daniel I.; Howell, Amy R.; Richardson, Stewart K.; Zinckgraf, John; Marusov, Gregory P.; Lynes, Michael A. (2013-03-19). "Cloning and Characterization of a Hybridoma Secreting a 4-(Methylnitrosamino)-1-(3-pyridyl)-1-butanone (NNK)-Specific Monoclonal Antibody and Recombinant F(ab)". Toxins. 5 (3): 568–589. doi: 10.3390/toxins5030568 . ISSN   2072-6651. PMC   3705279 . PMID   23518474.
  10. ↑ US 9156906,Franco, Alessandra,"Glycopeptides and methods of making and using them",published Oct 13, 2015
  11. ↑ Hammerberg, Bruce; Eguiluz-Hernandez, Sitka (2017-02-01). "Therapeutic anti-IgE monoclonal antibody single chain variable fragment (scFv) safety and immunomodulatory effects after one time injection in four dogs". Veterinary Dermatology. 28 (1): 52–e13. doi:10.1111/vde.12354. ISSN   1365-3164. PMID   27426720. S2CID   22605797.
  12. ↑ Gass, Justin T.; Olive, M. Foster (2008-04-28). "Transcriptional profiling of the rat frontal cortex following administration of the mGlu5 antagonists MPEP and MTEP". European Journal of Pharmacology. 584 (2–3): 253–262. doi:10.1016/j.ejphar.2008.02.032. ISSN   0014-2999. PMC   2386089 . PMID   18346726.
  13. ↑ Horgan, Conor P.; Hanscom, Sara R.; Kelly, Eoin E.; McCaffrey, Mary W. (2012-02-14). "Tumor Susceptibility Gene 101 (TSG101) Is a Novel Binding-Partner for the Class II Rab11-FIPs". PLOS ONE. 7 (2): e32030. Bibcode:2012PLoSO...732030H. doi: 10.1371/journal.pone.0032030 . ISSN   1932-6203. PMC   3279423 . PMID   22348143.
  14. ↑ Wu, Yongzhong; Antony, Smitha; Juhasz, Agnes; Lu, Jiamo; Ge, Yun; Jiang, Guojian; Roy, Krishnendu; Doroshow, James H. (2011-04-08). "Up-regulation and Sustained Activation of Stat1 Are Essential for Interferon-γ (IFN-γ)-induced Dual Oxidase 2 (Duox2) and Dual Oxidase A2 (DuoxA2) Expression in Human Pancreatic Cancer Cell Lines". The Journal of Biological Chemistry. 286 (14): 12245–12256. doi: 10.1074/jbc.M110.191031 . ISSN   0021-9258. PMC   3069428 . PMID   21321110.
  15. ↑ Morimoto, Jumpei; Sarkar, Mohosin; Kenrick, Sophia; Kodadek, Thomas (2014-08-20). "Dextran as a Generally Applicable Multivalent Scaffold for Improving Immunoglobulin-Binding Affinities of Peptide and Peptidomimetic Ligands". Bioconjugate Chemistry. 25 (8): 1479–1491. doi:10.1021/bc500226j. ISSN   1043-1802. PMC   4140544 . PMID   25073654.
  16. ↑ Ma, Lin; Gu, Kai; Zhang, Cheng-hai; Chen, Xue-tao; Jiang, Yi; Melcher, Karsten; Zhang, Juan; Wang, Min; Xu, H Eric (June 2016). "Generation and characterization of a human nanobody against VEGFR-2". Acta Pharmacologica Sinica. 37 (6): 857–864. doi:10.1038/aps.2016.2. ISSN   1671-4083. PMC   4954766 . PMID   27108602.
  17. ↑ "Creative Biolabs Supplies Resourceful Antibodies for Research Use on the COVID-19". MarketWatch. Retrieved 2020-08-10.
  18. ↑ "Creative Biolabs Scholarship Program". scholarships. Retrieved 2020-08-10.
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