CAC Antibody Collection
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Plant-related
Plant hormones / Plant autophagy and apoptosis / Plant stress response / CatechinPlant hormones
Because plants have a sessile lifestyle, they must adjust to numerous external stimuli and coordinate their growth and development accordingly. The plant hormones, a group of structurally unrelated small molecules, are central to the integration of diverse environmental cues with a plant’s genetic program. The ‘classical’ phytohormones, identified during the first half of the twentieth century, are auxin, abscisic acid, cytokinin, gibberellin and ethylene. More recently, several additional compounds have been recognized as hormones, including brassinosteroids, jasmonate, salicylic acid, nitric oxide and strigolactones. Plants also use several peptide hormones to regulate various growth responses, but this class of hormones is beyond our scope here. With the application of genetic approaches, mainly in Arabidopsis thaliana, many aspects of hormone biology have been elucidated. Most hormones are involved in many different processes throughout plant growth and development. This complexity is reflected by the contributions of hormone synthesis, transport and signaling pathways, as well as by the diversity of interactions among hormones to control growth responses.
Genetic screens resulted in the identification of many of the proteins involved in hormone signaling and the analysis of these proteins has contributed significantly to our current models of hormone action. One particularly exciting outcome is the recent identification of receptors for auxin, gibberellin, jasmonate and abscisic acid. Though far from complete, our improved understanding of hormone perception and signaling has allowed for comparisons between hormones. From these it is clear that some hormones (cytokinins, ethylene and the brassinosteroids) use well-characterized signaling mechanisms. On the other hand, the identification and characterization of the auxin and jasmonate receptors, as well as proteins in gibberellin signaling, have highlighted a novel mechanism for hormone perception in which the ubiquitin–proteasome pathway has a central role. [from: Santner A., Mark E., Recent advances and emerging trends in plant hormone signalling (2009) Nature 459: 1071-1078]
Abscisic acid (ABA), a type of plant hormone, is thought to be involved in the induction of dormancy, stomatal closure, and physiological functions such as flower falling and leaf falling. The biosynthesis of this substance is carried out by oxidation of abscisin aldehyde, and it is suggested that a specific aldehyde oxidase (AO) catalyzes the reaction. The CosmoBio Antibody Collection (CAC) has prepared three antibodies for detecting AO gene products cloned from Arabidopsis thaliana, and an antibody for detection of corn ascorbic acid peroxidase (APT)
Genetic screens resulted in the identification of many of the proteins involved in hormone signaling and the analysis of these proteins has contributed significantly to our current models of hormone action. One particularly exciting outcome is the recent identification of receptors for auxin, gibberellin, jasmonate and abscisic acid. Though far from complete, our improved understanding of hormone perception and signaling has allowed for comparisons between hormones. From these it is clear that some hormones (cytokinins, ethylene and the brassinosteroids) use well-characterized signaling mechanisms. On the other hand, the identification and characterization of the auxin and jasmonate receptors, as well as proteins in gibberellin signaling, have highlighted a novel mechanism for hormone perception in which the ubiquitin–proteasome pathway has a central role. [from: Santner A., Mark E., Recent advances and emerging trends in plant hormone signalling (2009) Nature 459: 1071-1078]
Abscisic acid (ABA), a type of plant hormone, is thought to be involved in the induction of dormancy, stomatal closure, and physiological functions such as flower falling and leaf falling. The biosynthesis of this substance is carried out by oxidation of abscisin aldehyde, and it is suggested that a specific aldehyde oxidase (AO) catalyzes the reaction. The CosmoBio Antibody Collection (CAC) has prepared three antibodies for detecting AO gene products cloned from Arabidopsis thaliana, and an antibody for detection of corn ascorbic acid peroxidase (APT)
| Plant-related: Plant hormones | |||
| Product name (click for order info) | Cat No (click for datasheet) |
Host | Species specificity |
| Anti Indole-3-Acetaldehyde Oxidase (AAO1/Aldehyde Oxidase 1) pAb (Rabbit, Ammonium Sulfate Purified) | CAC-SDT-01-AO1 | RAB | Plant Arabidopsis Pea |
| Anti Indole-3-Acetaldehyde Oxidase (Aldehyde Oxidase 2) pAb (Rabbit, Ammonium Sulfate Purified) | CAC-SDT-01-AO2 | RAB | Plant Arabidopsis Pea |
| Anti Abscisic-Aldehyde Oxidase (Aldehyde Oxidase 3) pAb (Rabbit, Ammonium Sulfate Purified) | CAC-SDT-01-AO3 | RAB | Plant Arabidopsis Pea |
| Anti L-Ascorbate Peroxidase 1, Cytosolic (AP/AtAPx01) pAb (Rabbit, Ammonium Sulfate Purified) | CAC-SDT-01-APX | RAB | Plant Maize Rice |
| Plant-related: Plant autophagy and apoptosis | |||
| Product name (click for order info) | Cat No (click for datasheet) |
Host | Species specificity |
| Anti Autophagy-Related Protein 8i (ATG8i) pAb (Rabbit, Antiserum) | CAC-KYU-TY-P01 | RAB | Plant Soybean Arabidopsis |
| Plant-related: Plant stress response | |||
| Product name (click for order info) | Cat No (click for datasheet) |
Host | Species specificity |
| Anti Calcineurin B-Like Protein 4 (CBL4/SOS3) pAb (Rabbit, Antiserum) | CAC-KYU-TY-P02 | RAB | Plant Tomato Soybean Cowpea |
| Plant-related: Catechin | |||
| Product name (click for order info) | Cat No (click for datasheet) |
Host | Species specificity |
| Anti Catechin mAb (Clone b-1058) | CAC-KYU-TM-M001 | MS | Plant |
| Product name | Anti Indole-3-Acetaldehyde Oxidase (AAO1/Aldehyde Oxidase 1) pAb (Rabbit, Ammonium Sulfate Purified) |
| Cat No | CAC-SDT-01-AO1 |
| Description | In higher plants aldehyde oxidases (AO) appear to be homo- and heterodimeric assemblies of AO subunits with probably different physiological functions. AO-alpha may be involved in the biosynthesis of auxin, and in biosynthesis of abscisic acid (ABA) in seeds. In vitro, AO-alpha uses heptaldehyde, protocatechualdehyde, benzaldehyde, indole-3-aldehyde (IAld), indole-3-acetaldehyde (IAAld), cinnamaldehyde and citral as substrates; AO-beta uses IAAld, IAld and naphtaldehyde as substrates. Source: Professor Koichi Koshiba, Tokyo Metropolitan University Graduate School of Science and Technology Department of Life Science. References: Akaba, S., Seo, M., Dohmae, N., Takio, K., Sekimoto, H., Kamiya, Y., Furuya, N., Komano, T. and Koshiba, T. (1999) Production of homo -and hetero-dimeric isozymes from two aldehyde oxidase genes of Arabidopsis thaliana. J Biochem (Tokyo) 126: 395-401. |
| Host | Rabbit |
| Species specificity | Plant Arabidopsis Pea |
| Product name | Anti Indole-3-Acetaldehyde Oxidase (Aldehyde Oxidase 2) pAb (Rabbit, Ammonium Sulfate Purified) |
| Cat No | CAC-SDT-01-AO2 |
| Description | In higher plant aldehyde oxidases (AO) appear to be homo- and heterodimeric assemblies of AO subunits with probably different physiological functions. In vitro, AO-gamma uses heptaldehyde, benzaldehyde, 1-naphthaldehyde and cinnamaldehyde as substrates; AO-beta uses indole-3-acetaldehyde (IAAld), indole-3-aldehyde (IAld) and naphtaldehyde; the AAO2-AAO3 dimer uses abscisic aldehyde. Source: Professor Koichi Koshiba, Tokyo Metropolitan University Graduate School of Science and Technology Department of Life Science. References: Akaba, S., Seo, M., Dohmae, N., Takio, K., Sekimoto, H., Kamiya, Y., Furuya, N., Komano, T. and Koshiba, T. (1999) Production of homo -and hetero-dimeric isozymes from two aldehyde oxidase genes of Arabidopsis thaliana. J Biochem (Tokyo) 126: 395-401. |
| Host | Rabbit |
| Species specificity | Plant Arabidopsis Pea |
| Product name | Anti Abscisic-Aldehyde Oxidase (Aldehyde Oxidase 3) pAb (Rabbit, Ammonium Sulfate Purified) |
| Cat No | CAC-SDT-01-AO3 |
| Description | In higher plants aldehyde oxidases (AO) appear to be homo- and heterodimeric assemblies of AO subunits with probably different physiological functions. AO-delta seems to be involved in the last step of abscisic acid biosynthesis, at least in leaves and seeds. In vitro, AO-delta oxidizes abscisic aldehyde to abscisic acid (ABA). In vitro, AO-delta also uses indole-3-aldehyde (IAld), benzaldehyde, 1-naphthaldehyde and cinnamaldehyde as substrate; the AAO2-AAO3 dimer also uses abscisic aldehyde as substrate. Source: Professor Koichi Koshiba, Tokyo Metropolitan University Graduate School of Science and Technology Department of Life Science. References: Seo, M., Koiwai, H., Akaba, S., Komano, T., Oritani, T., Kamiya, Y. and Koshiba, T. (2000) Abscisic aldehyde oxidase in leaves of Arabidopsis thaliana. Plant J. 23:481-488. |
| Host | Rabbit |
| Species specificity | Plant Arabidopsis Pea |
| Product name | Anti L-Ascorbate Peroxidase 1, Cytosolic (AP/AtAPx01) pAb (Rabbit, Ammonium Sulfate Purified) |
| Cat No | CAC-SDT-01-APX |
| Description | Ascorbate peroxidase (or APX) is a member of the family of heme-containing peroxidases. Ascorbate-dependent peroxidase activity was first reported in 1979, more than 150 years after the first observation of peroxidase activity in horseradish plants and almost 40 years after the discovery of the closely related cytochrome c peroxidase enzyme. Peroxidases have been classified into three types (class I, class II and class III). Ascorbate peroxidase is a class I peroxidase enzyme. APXs catalyse the H2O2-dependent oxidation of ascorbate in plants, algae and certain cyanobacteria. APX has high sequence identity to cytochrome c peroxidase, which is also a class I peroxidase enzyme. Under physiological conditions, the immediate product of the reaction, the monodehydroascorbate radical, is reduced back to ascorbate by a monodehydroascorbate reductase (monodehydroascorbate reductase (NADH)) enzyme. APX is an integral component of the glutathione-ascorbate cycle. Source: Professor Koichi Koshiba, Tokyo Metropolitan University Graduate School of Science and Technology Department of Life Science. References: Koshiba, T. (1993) Cytosolic ascorbate peroxidase in seeds and leaves of maize (Zea mays). Plant Cell Physiol. 34: 713-721. |
| Host | Rabbit |
| Species specificity | Plant Maize Rice |
| Plant autophagy and apoptosis |
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| Programmed cell death (PCD) in plants is a crucial component of development and defense mechanisms. In animals, different types of cell death (apoptosis, autophagy, and necrosis) have been distinguished morphologically and discussed in these morphological terms. PCD is largely used to describe the processes of apoptosis and autophagy (although some use PCD and apoptosis interchangeably) while necrosis is generally described as a chaotic and uncontrolled mode of death. In plants, the term PCD is widely used to describe most instances of death observed. At present, there is a vast array of plant cell culture models and developmental systems being studied by different research groups and it is clear from what is described in this mass of literature that, as with animals, there does not appear to be just one type of PCD in plants. It is fundamentally important to be able to distinguish between different types of cell death for several reasons. For example, it is clear that, in cell culture systems, the window of time in which ‘PCD’ is studied by different groups varies hugely and this can have profound effects on the interpretation of data and complicates attempts to compare different researcher’s data. In addition, different types of PCD will probably have different regulators and modes of death. For this reason, in plant cell cultures an apoptotic-like PCD (AL-PCD) has been identified that is fairly rapid and results in a distinct corpse morphology which is visible 4–6 h after release of cytochrome and other apoptogenic proteins. This type of morphology, distinct from autophagy and from necrosis, has also been observed in examples of plant development. [from: Reape TJ, Molony EM, and McCabe PF. (2008) Programmed cell death in plants: distinguishing between different modes. Journal of Experimental Botany. 59(3): 435–444.] | |
| Product name | Anti Autophagy-Related Protein 8i (ATG8i) pAb (Rabbit, Antiserum) |
| Cat No | CAC-KYU-TY-P01 |
| Description | ATG8 is an autophagy-related gene, a homolog protein of LC3. ATG8 is conjugated with phosphatidyl ethanol amine on its COOH terminal glycine via the ATG7 and ATG3 E1-like enzyme system. Higher plants have multiple ATG8 homologs comprising two subfamilies, ATG8a-g and ATG8h-i in Arabidopsis. Anti-soybean ATG8i antibody was raised against GST-fused GmATG8i and cross reacts with plant ATG8h- and ATG8i-related proteins, but not with plant ATG8a-g. References: 1) Nang MPSH, Tanigawa H, Ishibashi Y, Zheng SH, Yuasa T and Iwaya-Inoue M. (2009) Nutrient starvation differentially regulates GmATG8i in soybean seedlings. Plant Biotechnol. 26:317-326. 2) Okuda M, Nang MP, Oshima K, Ishibashi Y, Zheng SH, Yuasa T, Iwaya-Inoue M. (2011) Ethylene signal mediates induction of GmATG8i in soybean plants under starvation stress, Biosci Biotechnol Biochem. 75(7):1408-12. PMID : 21737912 |
| Host | RAB |
| Species specificity | Soybean Arabidopsis |
| Plant stress response (Top) | |
| Plants have to deal with various and complex types of interactions involving numerous environmental factors. In the course of evolution, they have evolved specific mechanisms allowing them to adapt and survive stressful events. Exposure of plants to biotic and abiotic stress induces a disruption in plant metabolism implying physiological costs, and thus leading to a reduction in fitness and ultimately in productivity. Abiotic stress is one of the most important features of and has a huge impact on growth and, consequently, it is responsible for severe losses in the field. The resulting growth reductions can reach >50% in most plant species. Moreover, biotic stress is an additional challenge inducing a strong pressure on plants and adding to the damage through pathogen or herbivore attack. A crucial step in plant defense is the timely perception of the stress in order to respond in a rapid and efficient manner. After recognition, the plants’ constitutive basal defense mechanisms lead to an activation of complex signaling cascades of defense varying from one stress to another. Following exposure to abiotic and/or biotic stress, specific ion channels and kinase cascades are activated, reactive oxygen species (ROS), phytohormones like abscisic acid (ABA), salicylic acid (SA), jasmonic acid (JA), and ethylene (ET) accumulate, and a reprogramming of the genetic machinery results in adequate defense reactions and an increase in plant tolerance in order to minimize the biological damage caused by the stress. [from: Rejeb IB, Pastor V and Mauch-Mani B. (2014) Plant Responses to Simultaneous Biotic and Abiotic Stress: Molecular Mechanisms. Plants. 3:458-475. doi:10.3390/plants3040458] |
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| Product name | Anti Calcineurin B-Like Protein 4 (CBL4/SOS3) pAb (Rabbit, Antiserum) |
| Cat No | CAC-KYU-TY-P02 |
| Description | Application of the Arabidopsis model system has yielded a regulatory pathway for ionic homeostasis under salt stress. The pathway was discovered through the cloning of the salt overly sensitive (SOS) genes. Mutations in the SOS genes render Arabidopsis plants more sensitive to Na+ stress. The pathway begins with SOS3, a myristoylated protein with three EF hands for calcium binding. SOS3 interacts physically with SOS2, which is a serine/threonine protein kinase. One downstream target of SOS3–SOS2 kinase complex is SOS1, which is a plasma membrane Na+–H+ antiporter that exports Na+ from the cell. SOS1 expression is upregulated by salt stress in wild-type Arabidopsis plants but this upregulation is reduced by sos3 or sos2 mutations. It remains to be seen whether or not SOS3–SOS2 directly regulates the activities of SOS1 and other transporter through phosphorylation. Remaining components in the SOS pathway are expected to be identified by cloning additional SOS genes and screening for second site suppressor and enhancer mutations in the sos mutant backgrounds. [from: Zhu JK. (2001) Plant salt tolerance. TRENDS in Plant Science. 6(2):66-71] References: 1) Yuasa T, Ishibashi Y. and Iwaya-Inoue M. (2012) A flower specific calcineurin B-like molecule (CBL)-interacting protein kinase (CIPK) homolog in tomato cultivar Micro-Tom (Solanum lycopersicum L.). American Journal of Plant Sciences. 3:753-763. 2) Imamura M, Yuasa T, Takahashi T, Nakamura N, Nang MPSH, Zheng SH, Shimazaki K. and Iwaya-Inoue M. (2008) Isolation and characterization of a cDNA coding cowpea (Vigna unguiculata (L.) Walp.) calcineurin B-like protein interacting protein kinase, VuCIPK1. Plant Biotechnol. 25:437-445. |
| Host | RAB |
| Species specificity | Plant Tomato Soybean |
| Catechin (Top) | |
| Green tea (Camellia sinensis) is one of the most popular beverages worldwide and its habitual consumption has long been associated with health benefit. In Asian countries, where tea drinking is a 4000 year-old cultural phenomenon, epidemiological studies show lower incidences of certain cancers and cardiovascular diseases. Many cancers and cardiovascular diseases are associated with Western lifestyle, especially related to diet on health outcomes (Ziegler et al., 1993; Kolonel et al., 2004). Most of the beneficial effects of green tea are attributed to its polyphenolic flavonoids, known as catechins, including epicatechin (EC), epigallocatechin (EGC), epicatechin-3-gallate (ECG) and the major flavonoid (—)-epigallocatechin-3-gallate (EGCG) (Graham, 1992). These polyphenols account for up to 40% of the dry weight of green tea, and purified EGCG has been the focus of research in recent years. Extensive research on green tea has taken place over the last decade, especially on the isolated catechin EGCG; however, most are based on in vitro and animal experiments. This emerging body of research is providing the basic scientific evidence for the presumed chemopreventative and cardiovascular properties of green tea. Green tea polyphenols are known antioxidants and it is proposed that these phytochemicals modulate biochemical and physiological processes leading to the initiation and propagation of carcinogenesis and cardiovascular diseases. [from: Clement Y. (2009) Can green tea do that? A literature review of the clinical evidence, Preventive Medicine 49(2–3): 83-87] |
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| Product name | Anti Catechin mAb (Clone b-1058) |
| Cat No | CAC-KYU-TM-M001 |
| Description | The world's first Catechin-recognizing antibody has been added to the Cosmobio Antibody Collection (CAC). Catechin is a polyphenol that is abundant in green tea. It has been reported to possess antioxidant, anticancer, antibacterial and antiallergic activities. Catechin comprises the following compounds: Epicatechin gallate (ECg), gallocatechin gallate (GCg), catechin gallate (Cg), epigallocatechin gallate (EGCg), gallocatechin (GC), epigallocatechin (EGC), catechin (C), epicatechin (EC). Cone b-1058 antibody reacts with epigallocatechin (EGC), epicatechin gallete (ECg), epigallocatechin gallete (EGCg), gallocatechin (GC), catechin gallete (Cg) and gallocatechin gallete (GCg). It reacts especially well with gallocatechin gallete (GCg) and epigallocatechin gallete (EGCg). References: Miyamoto T., et al. Development of novel monoclonal antibodies directed against catechins for investigation of antibacterial mechanism of catechins. Journal of Microbiological Methods, Volume 137, June 2017, Pages 6–13. [PubMed ID] 28347725 |
| Host | Mouse |
| Species specificity | Plant |
| Figure 1 |  |
| The concentrations of epigallocatechin gallate (EGCg) and epicatechin (EC) were measured by the direct ELISA method. Anti-catechin antibody (clone b-1058) was diluted 10,000-fold (0.1 ug / mL) and 50 uL was added to each well. |
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| Figure 2 |  |
| The affinity of anti-catechin antibody (clone b-1058) against epigallocatechin gallate (EGCg) and epicatechin (EC) was measured by SPR measurement. | |