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Mouse Anti-ATP13A2 Recombinant Antibody (CBYC-A872) (CBMAB-A4003-YC)

Provided herein is a Mouse monoclonal antibody against Human ATPase 13A2. The antibody can be used for immunoassay techniques, such as ELISA, WB.
See all ATP13A2 antibodies
Published Data
Mouse Anti-ATP13A2 Recombinant Antibody (CBYC-A872) (CBMAB-A4003-YC) in IHC
Representative photomicrographs of submandibulary gland sections in patients with idiopathic Parkinson's disease and controls, after immunostaining against ATP13A2 and DEHAL1. ...View More
Fernández-Espejo, E., Gavito, A. L., Suárez, J., Tolosa, E., Vilas, D., Aldecoa, I., ... & de Fonseca, F. R. (2022). Salivary ATP13A2 is a potential marker of therapy-induced motor complications and is expressed by inclusions in submandibulary glands in Parkinson´ s disease. Clinical Parkinsonism & Related Disorders, 7, 100163.

Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat
Clone
CBYC-A872
Antibody Isotype
IgG2a, κ
Application
ELISA, WB, IP

Basic Information

Immunogen
Amino acids 68-154 of ATP13A2 of human origin.
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG2a, 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)
ELISA1:100-1:1,000

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

Format
Liquid
Buffer
PBS, 0.1% gelatin
Preservative
< 0.1% sodium azide
Concentration
0.1 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 type 13A2
Introduction
ATP13A2 is a member of the P5 subfamily of ATPases which transports inorganic cations as well as other substrates. Mutations in this gene are associated with Kufor-Rakeb syndrome (KRS), also referred to as Parkinson disease 9. Multiple transcript variants
Entrez Gene ID
23400
UniProt ID
Q9NQ11
Alternative Names
ATPase 13A2; ATPase Type 13A2; PARK9; Parkinson Disease (Autosomal Recessive) 9 (Kufor-Rakeb Syndrome); Probable Cation-Transporting ATPase 13A2; Cation-Transporting ATPase 13A2; EC 3.6.3.5; EC 3.6.3.8;
Function
ATPase which acts as a lysosomal polyamine exporter with high affinity for spermine (PubMed:31996848).
Also stimulates cellular uptake of polyamines and protects against polyamine toxicity (PubMed:31996848).
Plays a role in intracellular cation homeostasis and the maintenance of neuronal integrity (PubMed:22186024).
Contributes to cellular zinc homeostasis (PubMed:24603074).
Confers cellular protection against Mn2+ and Zn2+ toxicity and mitochondrial stress (PubMed:26134396).
Required for proper lysosomal and mitochondrial maintenance (PubMed:22296644, PubMed:28137957).
Regulates the autophagy-lysosome pathway through the control of SYT11 expression at both transcriptional and post-translational levels (PubMed:27278822).
Facilitates recruitment of deacetylase HDAC6 to lysosomes to deacetylate CTTN, leading to actin polymerization, promotion of autophagosome-lysosome fusion and completion of autophagy (PubMed:30538141).
Promotes secretion of exosomes as well as secretion of SCNA via exosomes (PubMed:25392495, PubMed:24603074).
Plays a role in lipid homeostasis (PubMed:31132336).
Biological Process
Autophagosome-lysosome fusion Source: UniProtKB
Autophagosome organization Source: ParkinsonsUK-UCL
Autophagy Source: UniProtKB
Cellular calcium ion homeostasis Source: ParkinsonsUK-UCL
Cellular cation homeostasis Source: ParkinsonsUK-UCL
Cellular iron ion homeostasis Source: ParkinsonsUK-UCL
Cellular response to manganese ion Source: ParkinsonsUK-UCL
Cellular response to oxidative stress Source: ParkinsonsUK-UCL
Cellular response to zinc ion Source: ParkinsonsUK-UCL
Cellular zinc ion homeostasis Source: ParkinsonsUK-UCL
Extracellular exosome biogenesis Source: ParkinsonsUK-UCL
Ion transmembrane transport Source: Reactome
Lipid homeostasis Source: UniProtKB
Lysosomal transport Source: UniProtKB
Negative regulation of lysosomal protein catabolic process Source: ParkinsonsUK-UCL
Negative regulation of neuron death Source: ParkinsonsUK-UCL
Peptidyl-aspartic acid autophosphorylation Source: ParkinsonsUK-UCL
Polyamine transmembrane transport Source: ParkinsonsUK-UCL
Positive regulation of exosomal secretion Source: ParkinsonsUK-UCL
Positive regulation of gene expression Source: UniProtKB
Positive regulation of protein secretion Source: ParkinsonsUK-UCL
Protein autophosphorylation Source: ParkinsonsUK-UCL
Protein localization to lysosome Source: UniProtKB
Regulation of autophagosome size Source: ParkinsonsUK-UCL
Regulation of autophagy of mitochondrion Source: ParkinsonsUK-UCL
Regulation of chaperone-mediated autophagy Source: ParkinsonsUK-UCL
Regulation of endopeptidase activity Source: ParkinsonsUK-UCL
Regulation of glucosylceramidase activity Source: Ensembl
Regulation of intracellular protein transport Source: ParkinsonsUK-UCL
Regulation of lysosomal protein catabolic process Source: ParkinsonsUK-UCL
Regulation of macroautophagy Source: ParkinsonsUK-UCL
Regulation of mitochondrion organization Source: ParkinsonsUK-UCL
Regulation of protein localization to nucleus Source: UniProtKB
Regulation of ubiquitin-specific protease activity Source: UniProtKB
Spermine transmembrane transport Source: UniProtKB
Zinc ion homeostasis Source: ParkinsonsUK-UCL
Cellular Location
Late endosome membrane; Multivesicular body membrane; Lysosome membrane; Autophagosome membrane
Involvement in disease
Kufor-Rakeb syndrome (KRS): The disease is caused by variants affecting the gene represented in this entry. KRS has also been referred to as neuronal ceroid lipofuscinosis 12 (CLN12), due to neuronal and glial lipofuscin deposits detected in the cortex, basal nuclei and cerebellum of some patients. A rare form of autosomal recessive juvenile or early-onset, levodopa-responsive parkinsonism. In addition to typical parkinsonian signs, clinical manifestations of Kufor-Rakeb syndrome include behavioral problems, facial tremor, pyramidal tract dysfunction, supranuclear gaze palsy, and dementia.
Spastic paraplegia 78, autosomal recessive (SPG78): A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body.
Topology
Cytoplasmic: 1-44 aa
Intramembrane: 45-65 aa
Cytoplasmic: 66-235 aa
Helical: 236-253 aa
Lumenal: 254-256 aa
Helical: 257-276 aa
Cytoplasmic: 277-427 aa
Helical: 428-448 aa
Lumenal: 449-463 aa
Helical: 464-484 aa
Cytoplasmic: 485-930 aa
Helical: 931-951 aa
Lumenal: 952-957 aa
Helical: 958-978 aa
Cytoplasmic: 979-994 aa
Helical: 995-1015 aa
Lumenal: 1016-1048 aa
Helical: 1049-1069 aa
Cytoplasmic: 1070-1080 aa
Helical: 1081-1101 aa
Lumenal: 1102-1117 aa
Helical: 1118-1138 aa
Cytoplasmic: 1139-1180 aa
PTM
Autophosphorylated (PubMed:26134396, PubMed:28137957). Accumulates in an inactive autophosphorylated state and autophosphorylation is stimulated by phosphatidic acid and phosphatidylinositol 3,5-bisphosphate but not by Mn2+ or Zn2+ (PubMed:26134396). The presence of spermine results in a dose-dependent reduction in autophosphorylation (PubMed:31996848).

Zheng, K., & Li, T. (2021). Prediction of ATPase cation transporting 13A2 molecule in Petromyzon marinus and pan-cancer analysis into human tumors from an evolutionary perspective. Immunogenetics, 1-13.

Fernández-Espejo, E., de Fonseca, F. R., Suárez, J., González-Aparicio, R., & Santurtún, A. (2021). ATP13A2 levels in serum and cerebrospinal fluid in patients with idiopathic Parkinsons disease. Parkinsonism & Related Disorders.

Chen, Q., Zhong, L., Zhou, C., Feng, Y., Liu, Q. X., Zhou, D., ... & Qiu, Y. (2020). Knockdown of Parkinson’s disease-related gene ATP13A2 reduces tumorigenesis via blocking autophagic flux in colon cancer. Cell & bioscience, 10(1), 1-12.

Moriya, S., Tan, V. P., Yee, A. K., & Parhar, I. S. (2019). pink1, atp13a2 and uchl1 expressions are affected by inflammation in the brain. Neuroscience letters, 708, 134330.

Fleming, S. M., Santiago, N. A., Mullin, E. J., Pamphile, S., Karkare, S., Lemkuhl, A., ... & Schultheis, P. J. (2018). The effect of manganese exposure in Atp13a2-deficient mice. Neurotoxicology, 64, 256-266.

Dirr, E. R., Ekhator, O. R., Blackwood, R., Holden, J. G., Masliah, E., Schultheis, P. J., & Fleming, S. M. (2018). Exacerbation of sensorimotor dysfunction in mice deficient in Atp13a2 and overexpressing human wildtype alpha-synuclein. Behavioural brain research, 343, 41-49.

Shen, T., Pu, J., Lai, H. Y., Xu, L., Si, X., Yan, Y., ... & Zhang, B. (2018). Genetic analysis of ATP13A2, PLA2G6 and FBXO7 in a cohort of Chinese patients with early-onset Parkinson’s disease. Scientific reports, 8(1), 1-10.

M Sue, C., & Park, J. S. (2017). Hereditary parkinsonism-associated genetic variations in PARK9 locus Lead to functional impairment of ATPase type 13A2. Current Protein and Peptide Science, 18(7), 725-732.

Abbas, M. M., Govindappa, S. T., Sheerin, U. M., Bhatia, K. P., & Muthane, U. B. (2017). Exome sequencing identifies a novel homozygous missense ATP13A2 mutation. Movement disorders clinical practice, 4(1), 132.

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

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