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Mouse Anti-AMD1 Recombinant Antibody (A-8) (CBMAB-A2516-YC)


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Published Data
Mouse Anti-AMD1 Recombinant Antibody (A-8) in WB
The effect of food deprivation on polyamine pathway proteins. Mice allowed ad libitum (AL) access to food or were food deprived (FD) for 48 h. Tibialis anterior muscles were subjected to Western blot analysis for polyamine pathway-associated proteins: Ornithine decarboxylase 1 (Odc1, A). Adenosylmethionine decarboxylase 1 (Amd1, B), spermidine synthase (SpdSyn, C), spermine synthase (SpmSyn, D), spermine oxidase (Smox, E), spermidine/spermine acetyltransferase 1 (Sat1, F) and c-Myc (G). ...View More
Tabbaa, M., Ruz Gomez, T., Campelj, D. G., Gregorevic, P., Hayes, A., & Goodman, C. A. (2021). The regulation of polyamine pathway proteins in models of skeletal muscle hypertrophy and atrophy: A potential role for mTORC1. American Journal of Physiology-Cell Physiology, 320(6), C987-C999.
Mouse Anti-AMD1 Recombinant Antibody (A-8) in WB
Western blot and densitometry analyses showing Amd1expression, normalized to Actin, in TA and triceps of wild type and dy2j/dy2j mice at different ages. ...View More
Kemaladewi, D. U., Benjamin, J. S., Hyatt, E., Ivakine, E. A., & Cohn, R. D. (2018). Increased polyamines as protective disease modifiers in congenital muscular dystrophy. Human molecular genetics, 27(11), 1905-1912.
Mouse Anti-AMD1 Recombinant Antibody (A-8) in WB
(A) Representative blots of vinculin, ODC, AMD1, PAOX, and SMOX in the BEAS-2B, A549, and H1299 cells. (B) Quantitation of ODC, AMD1, PAOX, and SMOX levels in the three cell lines. Protein levels are expressed as the ratio of protein/vinculin in each sample. ...View More
López-Contreras, F., Muñoz-Uribe, M., Pérez-Laines, J., Ascencio-Leal, L., Rivera-Dictter, A., Martin-Martin, A., ... & López-Muñoz, R. (2020). Searching for drug synergy against cancer through polyamine metabolism impairment: insight into the metabolic effect of indomethacin on lung cancer cells. Frontiers in pharmacology, 10, 1670.

Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat
Clone
A-8
Antibody Isotype
IgG1, κ
Application
WB, IP, IF, ELISA

Basic Information

Immunogen
Amino acids 5-219 of AdoMetDC of human origin.
Host Species
Mouse
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG1, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:100-1:1,000
IP1-2 µg per 100-500 µg of total protein (1 ml of cell lysate)
IF(ICC)1:50-1:500
ELISA1:30-1:3,000

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, 0.1% gelatin
Preservative
< 0.1% sodium azide
Concentration
0.2 mg/ml
Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Adenosylmethionine Decarboxylase 1
Introduction
AMD1 is an important intermediate enzyme in polyamine biosynthesis. The polyamines spermine, spermidine, and putrescine are low-molecular-weight aliphatic amines essential for cellular proliferation and tumor promotion. Multiple alternatively spliced tran
Entrez Gene ID
Human262
Mouse11702
Rat81640
UniProt ID
HumanP17707
MouseP0DMN7
RatP17708
Alternative Names
ADOMETDC; AMD; SAMDC
Function
Essential for biosynthesis of the polyamines spermidine and spermine. Promotes maintenance and self-renewal of embryonic stem cells, by maintaining spermine levels.
Biological Process
Polyamine metabolic process Source: Reactome
S-adenosylmethioninamine biosynthetic process Source: UniProtKB-UniPathway
Spermidine biosynthetic process Source: GO_Central
Spermine biosynthetic process Source: GO_Central
Cellular Location
Cytosol
PTM
Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.
More Infomation

Yang, L., Li, X., Luo, Y., Yang, T., Wang, H., Shi, L., ... & Xie, W. (2021). Weighted gene co‑expression network analysis of the association between upregulated AMD1, EN1 and VGLL1 and the progression and poor prognosis of breast cancer. Experimental and therapeutic medicine, 22(3), 1-13.

Bian, X., Shi, D., Xing, K., Zhou, H., Lu, L., Yu, D., & Wu, W. (2021). AMD1 upregulates hepatocellular carcinoma cells stemness by FTO mediated mRNA demethylation. Clinical and translational medicine, 11(3), e352.

Rahim, A. B., Lim, H. K., Tan, C. Y. R., Jia, L., Leo, V. I., Uemura, T., ... & Vardy, L. A. (2021). The polyamine regulator AMD1 up-regulates spermine levels to drive epidermal differentiation. Journal of Investigative Dermatology.

Zhu, X., Shou, Y., Ji, X., Hu, Y., & Wang, H. (2020). S-adenosylmethionine Decarboxylase 1 Participates in PM2. 5 Exposure Induced Neuronal Apoptosis via Mitochondria-Mediated Pathway.

Xu, L., You, X., Cao, Q., Huang, M., Hong, L. L., Chen, X. L., ... & Chen, Y. (2020). Polyamine synthesis enzyme AMD1 is closely associated with tumorigenesis and prognosis of human gastric cancers. Carcinogenesis, 41(2), 214-222.

Yordanova, M. M., Loughran, G., Zhdanov, A. V., Mariotti, M., Kiniry, S. J., O’Connor, P. B., ... & Baranov, P. V. (2018). AMD1 mRNA employs ribosome stalling as a mechanism for molecular memory formation. Nature, 553(7688), 356-360.

Zabala-Letona, A., Arruabarrena-Aristorena, A., Martín-Martín, N., Fernandez-Ruiz, S., Sutherland, J. D., Clasquin, M., ... & Carracedo, A. (2017). mTORC1-dependent AMD1 regulation sustains polyamine metabolism in prostate cancer. Nature, 547(7661), 109-113.

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For research use only. Not intended for any clinical use.

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