Auxin

 CAS No.: 87-51-4  Cat No.: BP-900057  Purity: ≥ 98 % (HPLC) 4.5  

Auxin is a versatile Molecular Glue that plays a pivotal role in targeted protein degradation research. This compound specifically targets the SCF TIR1 E3 ubiquitin ligase complex, facilitating the recruitment and subsequent ubiquitination of proteins tagged with an auxin-inducible degron (AID). The binding site of Auxin is located at the interface between TIR1 and the AID-tagged substrate, promoting substrate recognition and degradation. Auxin's molecular characteristics include its small size and ability to modulate protein-protein interactions, making it an invaluable tool in the study of protein dynamics and cellular processes. The primary mechanism of Auxin involves the promotion of proximity between the E3 ligase and the protein of interest, effectively marking it for proteasomal degradation. This targeted approach is instrumental in dissecting protein function, investigating cellular signaling pathways, and exploring the therapeutic potential of protein degradation. Auxin's application in experimental research provides a robust platform for elucidating protein roles in various biological contexts, advancing our understanding of molecular and cellular biology.

Auxin

Structure of 87-51-4

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Category
Molecular Glue
Molecular Formula
C10H9NO2
Molecular Weight
175.18
Appearance
Solid powder

* For research and manufacturing use only. Not for human or clinical use.

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Popular Publications Citing BOC Sciences Products
Purity
≥ 98 % (HPLC)
Solubility
DMSO : 17.52mg/mL
Appearance
Solid powder
Application
Plant Growth Regulators
ShelfLife
Limited shelf life, expiry date on the label
Storage
Store at -20 °C
Shipping
Room temperature in continental US; may vary elsewhere.
IUPACName
2-(1H-indol-3-yl)acetic acid
Synonyms
Auxin; IAA; 3-Indoleacetic acid
Boiling Point
164-165 °C
Melting Point
168.5 °C
Density
1.576 g/cm<sup>3</sup>
Chemical Name
1H-Indole-3-acetic acid
InChI Key
InChI=1S/C10H9NO2/c12-10(13)5-7-6-11-9-4-2-1-3-8(7)9/h1-4,6,11H,5H2,(H,12,13)
InChI
SEOVTRFCIGRIMH-UHFFFAOYSA-N
SMILES
OC(CC1=CNC2=C1C=CC=C2)=O
Stability
Stable. Incompatible with strong oxidizing agents. Light sensitive.
Biological Activity
Chemical dimerizer used in auxin-inducible degron (AID) systems. Induces degradation of a target protein tagged with the auxin-receptor F-box protein Tir1 E3 ligase AID in human colorectral cancer and mouse ES cells or tagged with AFB2 in A431 cells. Endogenous plant hormone.
Mechanism

E3 Ligase: Auxin functions as a molecular glue in plants by recruiting the TIR1/AFB family of E3 ligases. This stabilizes interactions with Aux/IAA transcriptional repressors to promote ubiquitination.

Target Protein: Auxin primarily targets Aux/IAA proteins, transcriptional repressors regulating plant growth and development. Binding to TIR1 enables selective ubiquitination of these repressors.

Degradation Mechanism: Auxin mediates proteasomal degradation through the ubiquitin–proteasome system. The TIR1–Aux/IAA ternary complex promotes polyubiquitination, leading to recognition and clearance by the 26S proteasome.

Applications

• Molecular Glue in Protein Degradation: Auxin is employed as a molecular glue to facilitate the targeted degradation of proteins by promoting the interaction between specific proteins and the ubiquitin-proteasome system. This application is pivotal in exploring protein function and regulation, providing insights into cellular processes and potential therapeutic targets.

• Targeted Degradation in Plant Biology: In plant research, Auxin serves as a molecular glue to degrade proteins involved in growth and development. By manipulating protein stability, researchers can investigate gene function and signaling pathways, enhancing our understanding of plant physiology and adaptive responses.

• Auxin-Induced Protein Interaction: Utilizing Auxin as a molecular glue enables the study of protein-protein interactions by inducing the proximity of proteins that are otherwise non-interacting. This approach is instrumental in mapping interaction networks and elucidating the dynamic nature of cellular signaling pathways.

• Conditional Protein Degradation: Auxin allows for the conditional degradation of target proteins, enabling researchers to precisely control protein levels in experimental systems. This capability is essential for dissecting complex biological processes and validating the roles of specific proteins in various cellular contexts.

1.Auxin response under osmotic stress.
Naser V1, Shani E2. Plant Mol Biol. 2016 Apr 6. [Epub ahead of print]
The phytohormone auxin (indole-3-acetic acid, IAA) is a small organic molecule that coordinates many of the key processes in plant development and adaptive growth. Plants regulate the auxin response pathways at multiple levels including biosynthesis, metabolism, transport and perception. One of the most striking aspects of plant plasticity is the modulation of development in response to changing growth environments. In this review, we explore recent findings correlating auxin response-dependent growth and development with osmotic stresses. Studies of water deficit, dehydration, salt, and other osmotic stresses point towards direct and indirect molecular perturbations in the auxin pathway. Osmotic stress stimuli modulate auxin responses by affecting auxin biosynthesis (YUC, TAA1), transport (PIN), perception (TIR/AFB, Aux/IAA), and inactivation/conjugation (GH3, miR167, IAR3) to coordinate growth and patterning. In turn, stress-modulated auxin gradients drive physiological and developmental mechanisms such as stomata aperture, aquaporin and lateral root positioning.
2.Hydrolases of the ILR1-like family of Arabidopsis thaliana modulate auxin response by regulating auxin homeostasis in the endoplasmic reticulum.
Sanchez Carranza AP1, Singh A1, Steinberger K1, Panigrahi K2, Palme K1,3,4,5, Dovzhenko A1, Dal Bosco C1. Sci Rep. 2016 Apr 11;6:24212. doi: 10.1038/srep24212.
Amide-linked conjugates of indole-3-acetic acid (IAA) have been identified in most plant species. They function in storage, inactivation or inhibition of the growth regulator auxin. We investigated how the major known endogenous amide-linked IAA conjugates with auxin-like activity act in auxin signaling and what role ILR1-like proteins play in this process in Arabidopsis. We used a genetically encoded auxin sensor to show that IAA-Leu, IAA-Ala and IAA-Phe act through the TIR1-dependent signaling pathway. Furthermore, by using the sensor as a free IAA reporter, we followed conjugate hydrolysis mediated by ILR1, ILL2 and IAR3 in plant cells and correlated the activity of the hydrolases with a modulation of auxin response. The conjugate preferences that we observed are in agreement with available in vitro data for ILR1. Moreover, we identified IAA-Leu as an additional substrate for IAR3 and showed that ILL2 has a more moderate kinetic performance than observed in vitro.
3.MicroRNAs, polyamines, and the activities antioxidant enzymes are associated with in vitro rooting in white pine (Pinus strobus L.).
Fei Y1, Xiao B1, Yang M1, Ding Q1, Tang W2. Springerplus. 2016 Apr 6;5:416. doi: 10.1186/s40064-016-2080-1. eCollection 2016.
Molecular mechanism of in vitro rooting in conifer is not fully understood. After establishment of a regeneration procedure in eastern white pine (Pinus strobus L.) using mature embryos as explants to induce shoot formation on medium containing 3 μM IAA, 6 μM BA and 6 μM TDZ and induce root formation on medium containing 0.001-0.05 μM IAA, 0.001-0.05 μM IBA, 0.001-0.05 μM TDZ, we have investigated the changes of polyamine content and the activities of antioxidant enzymes during in vitro rooting in P. strobus. Our results demonstrated that putrescine (Put), spermidine (Spd), and spermine (Spm) did not increase in P. strobus during the first week of rooting on medium supplemented with 0.01 μM indole-3-acetic acid (IAA), whereas the levels of Put, Spd, and Spm increased during the 1st-3rd week of culture on medium with IAA, and then decreased on medium with IAA. No such a change in Put, Spd, and Spm was observed on medium without IAA. Measurement of antioxidant enzyme activity demonstrated that the activities of polyphenol oxidase, catalase, and peroxidase slightly increased in the first week of culture and reached to the highest peak in the 3rd-5th week of culture.
4.Molecular Characterization of MaCCS, a Novel Copper Chaperone Gene Involved in Abiotic and Hormonal Stress Responses in Musa acuminata cv. Tianbaojiao.
Feng X1, Chen F2, Liu W3, Thu MK4, Zhang Z5, Chen Y6, Cheng C7, Lin Y8, Wang T9, Lai Z10. Int J Mol Sci. 2016 Mar 24;17(4). pii: E441. doi: 10.3390/ijms17040441.
Copper/zinc superoxide dismutases (Cu/ZnSODs) play important roles in improving banana resistance to adverse conditions, but their activities depend on the copper chaperone for superoxide dismutase (CCS) delivering copper to them. However, little is known about CCS in monocots and under stress conditions. Here, a novel CCS gene (MaCCS) was obtained from a banana using reverse transcription PCR and rapid-amplification of cDNA ends (RACE) PCR. Sequence analyses showed that MaCCS has typical CCS domains and a conserved gene structure like other plant CCSs. Alternative transcription start sites (ATSSs) and alternative polyadenylation contribute to the mRNA diversity of MaCCS. ATSSs in MaCCS resulted in one open reading frame containing two in-frame start codons to form two protein versions, which is supported by the MaCCS subcellular localization of in both cytosol and chloroplasts. Furthermore, MaCCS promoter was found to contain many cis-elements associated with abiotic and hormonal responses.

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