FKHRL1 (Phospho-Ser253) ELISA Kit

Name: FKHRL1 (Phospho-Ser253) ELISA Kit
SKU: DEIA-XYA667
Rating: 5 (1 reviews)

Regulatory status: For research use only, not for use in diagnostic procedures.

COA

SDS

Datasheet

Summary

Sample

Nuclear and Cell Lysates

Species Reactivity

Human; Mouse

Intended Use

The FKHRL1 (Phospho-Ser253) ELISA Kit is intended for the qualitative determination of Activated Transcription Factors in Nuclear and Cell Lysates.

Contents of Kit

1. dsDNA Oligonucleotide Coated Microstrips: 96-Well, 4°C
2. 100x Anti-Phospho Target Primary Antibody: 100μL, 4°C
3. 100x Anti-Target Primary Antibody: 100μL, 4°C
4. HRP-Conjugated Anti-Rabbit IgG Secondary Antibody: 2x 6 ml, 4°C
5. Nuclear Lysate Positive Control: Lyophilized, 4°C/-80°C
6. Wild-Type Consensus dsDNA Oligonucleotide: 20μL, -20°C
7. Mutant Consensus dsDNA Oligonucleotide: 20μL, -20°C
8. 10x Wash Buffer: 50 mL, 4°C
9. 2x Binding Buffer: 12 ml, -20°C
10. Primary Antibody Diluent: 12 ml, 4°C
11. 100x Protease and Phosphatase Inhibitors: 100μL, -20°C
12. Nuclear Wash Buffer: 12 ml, -20°C
13. Cytoplasmic Extraction Buffer: 6 ml, -20°C
14. Nuclear Extraction Buffer: 6 ml, -20°C
15. Ready-to-Use Substrate: 12 ml, 4°C
16. Stop Solution: 12 ml, 4°C
17. Adhesive Plate Seals: 4 Sheets
18. Technical Manual: 1

Storage

After receiving the kit, please open and store the kit components at the indicated temperature. If used frequently, reagents may be stored at 4°C. Reconstituted Nuclear Lysate Positive Control must be aliquoted and stored at -80°C.

Citations

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Documents

pdf COA

pdf SDS

pdf Datasheet

QA & Reviews

Customer Reviews

References

Skeletal muscle-specific Prmt1 deletion causes muscle atrophy via deregulation of the PRMT6-FOXO3 axis

AUTOPHAGY

Authors: Choi, Seri; Jeong, Hyeon-Ju; Kim, Hyebeen; Choi, Dahee; Cho, Sung-Chun; Seong, Je Kyung; Koo, Seung-Hoi; Kang, Jong-Sun

Abstract

Protein arginine methyltransferases (PRMTs) have emerged as important regulators of skeletal muscle metabolism and regeneration. However, the direct roles of the various PRMTs during skeletal muscle remodeling remain unclear. Using skeletal muscle-specific prmt1 knockout mice, we examined the function and downstream targets of PRMT1 in muscle homeostasis. We found that muscle-specific PRMT1 deficiency led to muscle atrophy. PRMT1-deficient muscles exhibited enhanced expression of a macroautophagic/autophagic marker LC3-II, FOXO3 and muscle-specific ubiquitin ligases, TRIM63/MURF-1 and FBXO32, likely contributing to muscle atrophy. The mechanistic study reveals that PRMT1 regulates FOXO3 through PRMT6 modulation. In the absence of PRMT1, increased PRMT6 specifically methylates FOXO3 at arginine 188 and 249, leading to its activation. Finally, we demonstrate that PRMT1 deficiency triggers FOXO3 hyperactivation, which is abrogated by PRMT6 depletion. Taken together, PRMT1 is a key regulator for the PRMT6-FOXO3 axis in the control of autophagy and protein degradation underlying muscle maintenance.Abbreviations: Ad-RNAi: adenovirus-delivered small interfering RNA; AKT: thymoma viral proto-oncogene; AMPK: AMP-activated protein kinase; Baf A1: bafilomycin A(1); CSA: cross-sectional area; EDL: extensor digitorum longus; FBXO32: F-box protein 32; FOXO: forkhead box O; GAS: gatrocnemieus; HDAC: histone deacetylase; IGF: insulin-like growth factor; LAMP: lysosomal-associated membrane protein; MAP1LC3B/LC3B: microtubule-associated protein 1 light chain 3 beta; mKO: Mice with skeletal muscle-specific deletion of Prmt1; MTOR: mechanistic target of rapamycin kinase; MYH: myosin heavy chain; MYL1/MLC1f: myosin, light polypeptide 1; PRMT: protein arginine N-methyltransferase; sgRNA: single guide RNA; SQSTM1: sequestosome 1; SOL: soleus; TA:tibialis anterior; TRIM63/MURF-1: tripartite motif-containing 63; YY1: YY1 transcription factor

In vitro protective effects of marine-derived Aspergillus puulaauensis TM124-S4 extract on H2O2-stressed primary human fibroblasts

TOXICOLOGY IN VITRO

Authors: Letsiou, Sophia; Bakea, Artemis; Le Goff, Geraldine; Lopes, Philippe; Gardikis, Konstantinos; Alonso, Carolina; Alvarez, Pedro A.; Ouazzani, Jamal

Abstract

Nowadays, there is a huge interest in natural products obtained from marine organisms that can promote human health.The aim of the present study is to evaluate for the first time, the in vitro effects of marine Aspergillus puulaauensis TM124-S4 extract against oxidative stress in human fibroblasts, and its potential as a cosmetic ingredient. The strain was isolated from the Mediterranean Sea star, Echinaster sepositus, and identified according to ITS molecular sequence homology as a member of Aspergillus section versicolores.To gain insight on the bioactivity underpinning the effects of TM124-S4 extract on oxidative stress, we examined a panel of a hundred genes as well as cell viability. Initially, Aspergillus puulaauensis TM124-S4 promoted cell viability.The change in gene transcripts revealed that Aspergillus puulaauensis TM124-S4 extracts exhibited skin protection properties by mediating cell proliferation (EPS8, GDF15, CASP7, VEGFA), antioxidant response (CAT, SOD1, TXN, GPX1), skin hydration (CD44, CRABP2, SERPINE) and DNA repair (PCNA, P21). The extract also modulated the expression of genes involved in skin pigmentation and aging (TYR, FOXO3).These findings indicate that Aspergillus puulaauensis TM124-S4 extract possesses significant in-vitro skin protection activity against induced oxidative stress.Furthermore, new insights are provided into the beneficial role of fungal bioactive compounds in skin related research.