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Mouse Anti-ATP7B Recombinant Antibody (S62-29) (CBMAB-A4119-YC)


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Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat
Clone
S62-29
Antibody Isotype
IgG1
Application
WB, IHC, IP, IF

Basic Information

Immunogen
Synthetic peptide amino acids 3-21 (cytoplasmic N-terminus) of human Copper-transporting ATPase2.
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:1,000
IF(ICC)1:100

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

Format
Liquid
Buffer
PBS, pH7.4, 50% glycerol
Preservative
0.09% sodium azide
Concentration
1 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
ATPase Copper Transporting Beta
Introduction
ATP7B belongs to the P-type cation transport ATPase family and encodes a protein with several membrane-spanning domains, an ATPase consensus sequence, a hinge domain, a phosphorylation site, and at least 2 putative copper-binding sites. This protein funct
Entrez Gene ID
Human540
Mouse11979
Rat24218
UniProt ID
HumanP35670
MouseQ64446
RatQ64535
Alternative Names
ATPase Copper Transporting Beta; Copper Pump 2; ATPase, Cu++ Transporting, Beta Polypeptide; Wilson Disease-Associated Protein; Copper-Transporting ATPase 2; WND; PWD; WC1;
Function
Copper ion transmembrane transporter involved in the export of copper out of the cells. It is involved in copper homeostasis in the liver, where it ensures the efflux of copper from hepatocytes into the bile in response to copper overload.
Biological Process
Cellular copper ion homeostasis Source: GO_Central
Copper ion export Source: GO_Central
Copper ion import Source: UniProtKB
Copper ion transport Source: UniProtKB
Ion transmembrane transport Source: Reactome
Response to copper ion Source: UniProtKB
Sequestering of calcium ion Source: UniProtKB
Xenobiotic detoxification by transmembrane export across the plasma membrane Source: GO_Central
Cellular Location
Late endosome; Trans-Golgi network membrane. Predominantly found in the trans-Golgi network (TGN). Localized in the trans-Golgi network under low copper conditions, redistributes to cytoplasmic vesicles when cells are exposed to elevated copper levels, and then recycles back to the trans-Golgi network when copper is removed (PubMed:10942420).
Isoform 1: Golgi apparatus membrane
Isoform 2: Cytoplasm
WND/140 kDa: Mitochondrion
Involvement in disease
Wilson disease (WD): An autosomal recessive disorder of copper metabolism in which copper cannot be incorporated into ceruloplasmin in liver, and cannot be excreted from the liver into the bile. Copper accumulates in the liver and subsequently in the brain and kidney. The disease is characterized by neurologic manifestations and signs of cirrhosis.
Topology
Cytoplasmic: 1-653 aa
Helical: 654-675 aa
Extracellular: 676-697 aa
Helical: 698-717 aa
Cytoplasmic: 718-724 aa
Helical: 725-745 aa
Extracellular: 746-764 aa
Helical: 765-785 aa
Cytoplasmic: 786-919 aa
Helical: 920-942 aa
Extracellular: 943-972 aa
Helical: 973-994 aa
Cytoplasmic: 995-1322 aa
Helical: 1323-1340 aa
Extracellular: 1341-1351 aa
Helical: 1352-1371 aa
Cytoplasmic: 1372-1465 aa
PTM
Isoform 1 may be proteolytically cleaved at the N-terminus to produce the WND/140 kDa form.
More Infomation

Mamoor, S. (2021). ATP7B is a differentially expressed gene in brain metastatic human breast cancer.

Li, J., Lu, Q., Yu, J., Ji, M., & Lu, L. (2021). Osteoarticular manifestations as initial symptoms of WD with novel compound heterozygote mutations in the ATP7B gene: a case report. Translational Pediatrics, 10(4), 1026.

Wang, J., Tang, L., Xu, A., Zhang, S., Jiang, H., Pei, P., ... & Yang, W. (2021). Identification of mutations in the ATP7B gene in 14 Wilson disease children: Case series. Medicine, 100(16).

Abdelmoula, N. (2021). Toxic accumulation of copper and neuropsychiatric symptoms due to a familial tunisian compound heterozygous ATP7B missense mutation. European Psychiatry, 64(S1), S717-S718.

Ryumon, S., Okui, T., Kunisada, Y., Kishimoto, K., Shimo, T., Hasegawa, K., ... & Sasaki, A. (2019). Ammonium tetrathiomolybdate enhances the antitumor effect of cisplatin via the suppression of ATPase copper transporting beta in head and neck squamous cell carcinoma. Oncology reports, 42(6), 2611-2621.

Wang, X., Guo, L., Zhang, S., Chen, Y., Chen, Y. T., Zheng, B., ... & Lu, W. (2019). Copper sulfide facilitates hepatobiliary clearance of gold nanoparticles through the copper-transporting ATPase ATP7B. ACS nano, 13(5), 5720-5730.

Xiao, H., Deng, S., Deng, X., Gu, S., Yang, Z., Yin, H., & Deng, H. (2019). Mutation analysis of the ATP7B gene in seven Chinese families with Wilson’s disease. Digestion, 99(4), 319-326.

Schmidt, K., Ralle, M., Schaffer, T., Jayakanthan, S., Bari, B., Muchenditsi, A., & Lutsenko, S. (2018). ATP7A and ATP7B copper transporters have distinct functions in the regulation of neuronal dopamine-β-hydroxylase. Journal of Biological Chemistry, 293(52), 20085-20098.

Moinuddin, F. M., Hirano, H., Shinsato, Y., Higa, N., Arita, K., & Furukawa, T. (2017). ATP7B expression in human glioblastoma is related to temozolomide resistance. Oncology letters, 14(6), 7777-7782.

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

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