I think my claim that they are working with recombinant spider silk proteins, just as KBLB is, can be justified.
LOL, who is arguing they aren't? They are coming back to it now, with KBLB's news, but guess what, they are going to go with the cheap version. I am telling you now.
The methods and technologies Spiber has developed for the production and utilization of our materials are based on a multitude of interdisciplinary research initiatives. Many important questions crucial to structural protein development and production remain unanswered, particularly in the frontier research topic that forms Spiber’s core competency—understanding the mechanism that drives the expression of our specially-designed proteins.
We believe that pioneering the new technologies and knowledge required by our endeavour will require a coordinated fusion of the best solutions that academia and industry have to offer.
By applying the latest academic developments to the cyclical research and development process that drives our efforts to commercialize structural proteins, we believe that we can contribute to the global scientific endeavor to bring about a more sustainable future. It is this belief that inspires our research into a wide range of natural protein materials and their properties, from the incredible softness of premium luxury cashmere to the tough and tensile spider silk that inspired our company’s name.
Protein materials are unmatched in terms of their potential for diversity across both form and function, and we are confident that their impact on humanity and the world will only continue to grow as our knowledge and ability to utilize them increases through the combined efforts of industry and academia.
International Journal of Biological Macromolecules
February 23, 2022 The solubility of N-acetyl amino acid amides in organic acid and alcohol solutions: Mechanistic insight into structural protein solubilization Atsushi Hirano, Momoyo Wada, Takehiro K.Sato, Tomoshi Kameda -> Abstract Molecules | January 14, 2022 Presence of ß-Turn Structure in Recombinant Spider Silk Dissolved in Formic Acid Revealed with NMR Yu Suzuki, Takanori Higash, Takahiro Yamamoto, Hideyasu Okamura, Takehiro K. Sato and Tetsuo Asakura -> Abstract Open Biology | December 22, 2021 Darwin’s bark spider shares a spidroin repertoire with Caerostris extrusa but achieves extraordinary silk toughness through gene expression Nobuaki Kono, Rintaro Ohtoshi, Ali D. Malay, Masaru Mori, Hiroyasu Masunaga, Yuki Yoshida, Hiroyuki Nakamura, Keiji Numata and Kazuharu Arakawa -> Abstract Engineering Biology | December 10, 2021 Fuelling the future of sustainable sugar fermentation across generations David Lips -> Abstract Data in Brief | September 20, 2021 Transcriptomic data during development of a two-spotted cricket Gryllus bimaculatus Nobuaki Kono, Hiroyuki Nakamura, Rintaro Ohtoshi, Kazuharu Arakawa -> Abstract Perspective | Emerging Topics in Life Sciences | September 08, 2021 Practical considerations for delivering on the sustainability promise of fermentation-based biomanufacturing David Lips -> Abstract Proceedings of the National Academy of Science of the United States of America | August 06, 2021 Multicomponent nature underlies the extraordinary mechanical properties of spider dragline silk Nobuaki Kono, Hiroyuki Nakamura, Masaru Mori, Yuki Yoshida, Rintaro Ohtoshi, Ali D. Malay, Daniel A. Pedrazzoli Moran, Masaru Tomita, Keiji Numata, and Kazuharu Arakawa -> Abstract Zoological Letters | July 26, 2021 The balance of crystalline and amorphous regions in the fibroin structure underpins the tensile strength of bagworm silk Nobuaki Kono, Hiroyuki Nakamura, Ayaka Tateishi, Keiji Numata and Kazuharu Arakawa -> Abstract Mitochondrial DNA Part B | July 26, 2021 The complete mitochondrial genome of Trichonephila clavipes (Araneae: Araneidae) Nobuaki Kono, Hiroyuki Nakamura and Kazuharu Arakawa -> Abstract Biomolecules | April 12, 2021 Xanthurenic Acid Is the Main Pigment of Trichonephila clavata Gold Dragline Silk Masayuki Fujiwara, Nobuaki Kono, Akiyoshi Hirayama, Ali D. Malay, Hiroyuki Nakamura, Rintaro Ohtoshi, Keiji Numata, Masaru Tomita and Kazuharu Arakawa -> Abstract Scientific Reports | January 08, 2021 Environmental biodegradability of recombinant structural protein Yuya Tachibana, Sunita Darbe, Senri Hayashi, Alina Kudasheva, Haruna Misawa, Yuka Shibata & Ken-ichi Kasuya -> Abstract Polymer Journal | October 01, 2020 Aqueous spinning system with a citrate buffer for highly extensible silk fibers Jianming Chen, Yoshinori Ohta, Hiroyuki Nakamura, Hiroyasu Masunaga, Keiji Numata -> Abstract Scientific Reports | September 24, 2020 Spidroin profiling of cribellate spiders provides insight into the evolution of spider prey capture strategies Nobuaki Kono, Hiroyuki Nakamura, Masaru Mori, Masaru Tomita & Kazuharu Arakawa -> Abstract Molecular Biology and Evolution | August 14, 2019 Sequenceserver: a modern graphical user interface for custom BLAST databases Anurag Priyam, Ben J Woodcroft, Vivek Rai, Ismail Moghul, Alekhya Munagala, Filip Ter, Hiten Chowdhary, Iwo Pieniak, Lawrence J Maynard, Mark Anthony Gibbins, HongKee Moon, Austin Davis-Richardson, Mahmut Uludag, Nathan S Watson-Haigh, Richard Challis, Hiroyuki Nakamura, Emeline Favreau, Esteban A Gómez, Tomás Pluskal, Guy Leonard, Wolfgang Rumpf, Yannick Wurm -> Abstract Scientific Reports | June 10, 2019 Orb-weaving spider Araneus ventricosus genome elucidates the spidroin gene catalogue Nobuaki Kono, Hiroyuki Nakamura, Rintaro Ohtoshi, Daniel A. Pedrazzoli Moran, Asaka Shinohara, Yuki Yoshida, Masayuki Fujiwara, Masaru Mori, Masaru Tomita & Kazuharu Arakawa -> Abstract Communications Biology | April 29, 2019 The bagworm genome reveals a unique fibroin gene that provides high tensile strength Nobuaki Kono, Hiroyuki Nakamura, Rintaro Ohtoshi, Masaru Tomita, Keiji Numata & Kazuharu Arakawa -> Abstract Mitochondrial DNA Part B | August 01, 2018 The complete mitochondrial genome of Eumeta variegata (Lepidoptera: Psychidae) Kazuharu Arakawa, Nobuaki Kono, Rintaro Ohtoshi, Hiroyuki Nakamura, Masaru Tomita -> Abstract Polymer Degradation and Stability | April 12, 2018 Stabilization of recombinant spider silk in thermo-oxidative degradation: High-throughput screening for antioxidants Anh T.N. Dao, Jun'ichi Shimokata, Kengo Takeuchi, Koyuru Nakayama, Toshiaki Taniike -> Abstract Scientific Reports | January 29, 2018 Reconstruction of cysteine biosynthesis using engineered cysteine-free enzymes Kosuke Fujishima, Kendrick M. Wang, Jesse A. Palmer, Nozomi Abe, Kenji Nakahigashi, Drew Endy & Lynn J. Rothschild -> Abstract Macromolecules | October 13, 2017 NMR Investigation about Heterogeneous Structure and Dynamics of Recombinant Spider Silk in the Dry and Hydrated States Yugo Tasei, Akio Nishimura, Yu Suzuki, Takehiro K. Sato, Junichi Sugahara, and Tetsuo Asakura -> Abstract Polymer Degradation and Stability | August 12, 2017 Chemiluminescence from recombinant spider silk under thermo-oxidative degradation Koyuru Nakayama, Anh T.N. Dao, Kengo Takeuchi, Junichi Shimokata, Toshiaki Taniike -> Abstract Polymer Chemistry | January 02, 2017 Multilateral characterization of recombinant spider silk in thermal degradation Anh T. N. Dao, K. Nakayama, J. Shimokata and T. Taniike -> Abstract Biomacromolecules | February 02, 2016 Influence of Water Content on the ß-Sheet Formation, Thermal Stability, Water Removal, and Mechanical Properties of Silk Materials Kenjiro Yazawa, Kana Ishida, Hiroyasu Masunaga, Takaaki Hikima and Keiji Numata -> Abstract Molecular Ecology Resources | November 12, 2015 Evaluation of the impact of RNA preservation methods of spiders for de novo transcriptome assembly Nobuaki Kono, Hiroyuki Nakamura, Yusuke Ito, Masaru Tomita, Kazuharu Arakawa -> Abstract Polymer | October 23, 2015 Crystal structure and physical properties of Antheraea yamamai silk fibers: Long poly(alanine) sequences are partially in the crystalline region Keiji Numata, Ryota Sato, Kenjiro Yazawa, Takaaki Hikima, Hiroyasu Masunaga -> Abstract Soft Matter | June 30, 2015 Use of extension-deformation-based crystallisation of silk fibres to differentiate their functions in nature Keiji Numata, Hiroyasu Masunaga, Takaaki Hikima, Sono Sasaki, Kazuhide Sekiyama and Masaki Takata -> Abstract
IN RESPONSE TO:
Proteins are made from long chains of amino acids that may have been modified during protein formation. There are only 20 normal amino acids in most proteins. At an atomic level, lots of carbon atoms, oxygen, nitrogen, and hydrogen being the most common.
To say that something is ‘molecularly identical’ means each of these amino acids appears in the same position in the larger protein structure. Companies are now synthesizing whey protein from cow milk. It is the same protein.