Recombinant Human Probable cation-transporting ATPase 13A2 (ATP13A2), partial

Code CSB-YP889076HU
Size Pls inquire
Source Yeast
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-EP889076HU
Size Pls inquire
Source E.coli
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-EP889076HU-B
Size Pls inquire
Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-BP889076HU
Size Pls inquire
Source Baculovirus
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-MP889076HU
Size Pls inquire
Source Mammalian cell
Have Questions? Leave a Message or Start an on-line Chat

Product Details

Purity
>85% (SDS-PAGE)
Target Names
ATP13A2
Uniprot No.
Alternative Names
AT132_HUMAN; Atp13a2; ATPase type 13A2; CLN12; FLJ26510; HSA9947; KRPPD; PARK9; Probable cation transporting ATPase 13A2; Probable cation-transporting ATPase 13A2; Putative ATPase; RP1-37C10.4
Species
Homo sapiens (Human)
Protein Length
Partial
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

Related Products

Customer Reviews and Q&A

 Customer Reviews

There are currently no reviews for this product.

Submit a Review here

Target Background

Function
ATPase which acts as a lysosomal polyamine exporter with high affinity for spermine. Also stimulates cellular uptake of polyamines and protects against polyamine toxicity. Plays a role in intracellular cation homeostasis and the maintenance of neuronal integrity. Contributes to cellular zinc homeostasis. Confers cellular protection against Mn(2+) and Zn(2+) toxicity and mitochondrial stress. Required for proper lysosomal and mitochondrial maintenance. Regulates the autophagy-lysosome pathway through the control of SYT11 expression at both transcriptional and post-translational levels. Facilitates recruitment of deacetylase HDAC6 to lysosomes to deacetylate CTTN, leading to actin polymerization, promotion of autophagosome-lysosome fusion and completion of autophagy. Promotes secretion of exosomes as well as secretion of SCNA via exosomes. Plays a role in lipid homeostasis.
Gene References into Functions
  1. This study showed that Lysosomal defects in ATP13A2 associated familial Parkinson's disease. PMID: 28894968
  2. Hereditary Parkinsonism-associated genetic variations in PARK9 locus lead to functional impairment in the ion transport function of this protein. (Review) PMID: 26965689
  3. Study unravels a novel activity-independent scaffolding role of ATP13A2 in trafficking/export of intracellular cargo in response to proteotoxic stress. PMID: 28334751
  4. we describe, for the first time, the deleterious effect arising from the interaction between the ATP13A2 familial mutant Dup22 with a-Syn. We show that this ATP13A2 mutant can enhance a-Syn oligomerization and aggregation in cell culture PMID: 27282395
  5. ATP13A2 inhibition by hsa-miR-4306 efficiently restored manganese-induced cytotoxicity in cultured neurons. PMID: 28302480
  6. This study demonstrated that loss of ATP13A2 function causes a combination of lysosomal and mitochondrial dysfunction that affects multiple neuronal populations. PMID: 28137957
  7. The ATP13A2 A746T variant is rare in Han Chinese patients and controls and is not associated with PD susceptibility in this ethnic group. PMID: 26000924
  8. This study showed that LRRK2, PARK2 and ATP13A2 are under copy number variations influence in patient with Parkinson disease. PMID: 27399248
  9. tre results of this study suggests that the expression of ATP13A2 regulated by the PHD2-HIF1alpha signaling pathway,and this is instrumental in maintaining cellular iron homeostasis and cell viability in mitochondrially compromised DAergic neurons. PMID: 26818499
  10. that ATP13A2 contains a unique N-terminal hydrophobic extension that lies on the cytosolic membrane surface of the lysosome, where it interacts with the lysosomal signaling lipids phosphatidic acid and phosphatidylinositol(3,5)bisphosphate. PMID: 26134396
  11. ATP13A2 overexpression improves the lysosome membrane integrity and protects against iron-induced cell damage. PMID: 25912790
  12. A review of recent advances in the emerging association of ATP13A2 mutations with Parkinsonism and neuronal ceroid lipofuscinoses. PMID: 25197640
  13. The mutation rates of Thr12Met and Ala1144Thr of ATP13A2 in the Uygur and Han Parkinson's disease patients in the Xinjiang region are low. PMID: 25374329
  14. This study demonistrated that loss of ATP13A2 causes a specific protein trafficking defect, and that Atp13a2 null mice develop age-related motor dysfunction that is preceded by neuropathological changes. PMID: 25855184
  15. Data show that patients with Lewy body diseases have an overall deficit in ATP13A2 protein levels, with the remaining protein being more insoluble and partially redistributing towards Lewy bodies PMID: 24252509
  16. Present results of homozygosity mapping in two siblings affected with early onset Parkinson's disease (EOPD) and mutation screening of ATP13A2. The variation identified represents the 13th known disease causing mutation in ATP13A2. PMID: 24949580
  17. these data suggest the involvement of PARK9 in the biogenesis of exosomes and alpha-synuclein secretion. PMID: 25392495
  18. Reduced ATP13A2 expression significantly decreased vesicular zinc levels, indicating ATP13A2 facilitates transport of zinc. PMID: 24603074
  19. human ATP13A2 deficiency results in zinc dyshomeostasis and mitochondrial dysfunction. PMID: 24399444
  20. PARK9 loss of function leads to dyshomeostasis of intracellular Zn(2+) that in turn contributes to lysosomal dysfunction and accumulation of alpha-Syn. PMID: 24334770
  21. No association is found between ATP13A2 Ala746Thr and early onset Parkinson's disease (EOPD) or late onset Parkinson's in a Chinese cohort; this variant is not a strong risk factor in the Chinese population. PMID: 23522931
  22. hypoxia signaling plays a very important role in the regulation of human ATP13A2 gene expression PMID: 22288903
  23. a novel frame-shift mutation in exon 22 of ATP13A2 (c.2473C>AA, p.Leu825AsnfsX32). PMID: 21696388
  24. Mutations in ATP13A2 is often associated with rapidly progressive parkinsonism and with additional features including pyramidal signs, cognitive decline and loss of sustained Levodopa responsiveness. PMID: 23196729
  25. Cathepsin D activity was decreased in ATP13A2-knockdown cells that displayed lysosome-like bodies characterized by fingerprint-like structures PMID: 23499937
  26. ATP13A2 knockout exacerbates apoptosis and autophagy in infarct penumbra of cerebral cortex, with no influence on the infarct size in mice with ischemic stroke. PMID: 23121889
  27. ATP13A2 protects against manganese & nickel toxicity, & proteasomal, mitochondrial, & oxidative stress. ATP13A2 may import a cofactor required for the function of a lysosome enzyme(s). PMID: 22847264
  28. the human P5B-ATPase ATP13A2 is involved in polyamine uptake. PMID: 23205587
  29. ATP13A2 variation may be a risk marker for neurotoxic effects of manganese in humans. PMID: 22285144
  30. ATP13A2 and alpha-syn are functionally linked in neurodegeneration. PMID: 22645275
  31. Our results indicate that ATP13A2 mutations are a rare cause of both NBIA and dystonia-parkinsonism. PMID: 22743658
  32. This study provides support for common loss-of-function effects of homozygous and heterozygous missense mutations in ATP13A2 associated with early-onset forms of parkinsonism. PMID: 22768177
  33. The altered apoptotic pattern of subjects with mutated ATP13A2 suggests a correlation between apoptosis alteration and the mutated ATP13A2 protein PMID: 22117566
  34. These findings collectively suggest that ATP13A2 contributes to the maintenance of a healthy mitochondrial pool, supporting the hypothesis that impaired mitochondrial clearance represents an important pathogenic mechanism underlying KRS. PMID: 22296644
  35. Data show that a family with typical neuronal ceroid lipofuscinoses (NCLs) pathology carried a single homozygous mutation in ATP13A2 that fully segregates with disease. PMID: 22388936
  36. This study demonistrated that contralateral silent period duration was increased in the symptomatic ATP13A2 mutation carriers suggested that compound heterozygous mutation in the ATP13A2 gene is associated with increased intracortical inhibition. PMID: 22104014
  37. results unravel an instrumental role of ATP13A2 deficiency on lysosomal function and cell viability and demonstrate the feasibility and therapeutic potential of modulating ATP13A2 levels in the context of PD PMID: 22647602
  38. results confirm a role for Ypk9 in manganese homeostasis and illuminates cellular pathways and biological processes in which Ypk9 likely functions PMID: 22457822
  39. The SNPs investigated in the BST1, PARK15 and PARK9 genes associated with PD susceptibility are not associated with PD in the northern Han Chinese population. PMID: 22490479
  40. study reveals a number of intriguing neuronal phenotypes due to the loss- or gain-of-function of ATP13A2 that support a role for this protein in regulating intracellular cation homeostasis and neuronal integrity PMID: 22186024
  41. This study demonistrated that restoration of ATP13A2 function may lead to improved lysosomal function and decreased accumulation of alpha-syn. PMID: 22442086
  42. rare variants of ATP13A2 may contribute to Parkinson's disease susceptibility in Taiwan PMID: 21714071
  43. Mutant Atp13a2 proteins are degraded by endoplasmic reticulum-associated degradation and sensitize cells to cell death. PMID: 21665991
  44. A novel frameshift mutation in ATP13A2 causes juvenile dystonia-parkinsonism and dementia. PMID: 21094623
  45. premature degradation of mutant ATP13A2 mRNA contribute to the aetiology of Kufor-Rakeb syndrome (KRS). PMID: 21542062
  46. Regulation of intracellular manganese homeostasis by Kufor-Rakeb syndrome-associated ATP13A2 protein. PMID: 21724849
  47. To see if ATP13A2 mutations could be responsible for some cases of human adult-onset NCL (Kufs disease), we resequenced ATP13A2 from 28 Kufs disease patients. None of these patients had ATP13A2 sequence variants likely to be causal for their disease PMID: 21362476
  48. No clearly pathogenic mutations are identified in ATP13A2 and GIGYF2 in Brazilian patients with early-onset Parkinson's disease. PMID: 20816920
  49. report clinical, instrumental, and genetic findings in an Italian family with novel PARK9 and PARK15 mutations PMID: 20853184
  50. We found no evidence for a correlation between a single heterozygous mutation in the ATP13a2 gene and the development of distinct oculomotor disturbances. PMID: 20842691

Show More

Hide All

Involvement in disease
Kufor-Rakeb syndrome (KRS); Spastic paraplegia 78, autosomal recessive (SPG78)
Subcellular Location
Lysosome membrane; Multi-pass membrane protein. Late endosome membrane; Multi-pass membrane protein. Endosome, multivesicular body membrane; Multi-pass membrane protein. Cytoplasmic vesicle, autophagosome membrane; Multi-pass membrane protein.
Protein Families
Cation transport ATPase (P-type) (TC 3.A.3) family, Type V subfamily
Tissue Specificity
Expressed in brain; protein levels are markedly increased in brain from subjects with Parkinson disease and subjects with dementia with Lewy bodies. Detected in pyramidal neurons located throughout the cingulate cortex (at protein level). In the substanti
Database Links

HGNC: 30213

OMIM: 606693

KEGG: hsa:23400

STRING: 9606.ENSP00000327214

UniGene: Hs.128866

icon of phone
Call us
301-363-4651 (Available 9 a.m. to 5 p.m. CST from Monday to Friday)
icon of address
Address
7505 Fannin St., Ste 610, Room 7 (CUBIO Innovation Center), Houston, TX 77054, USA
icon of social media
Join us with

Subscribe newsletter

Leave a message

* To protect against spam, please pass the CAPTCHA test below.
CAPTCHA verification
© 2007-2024 CUSABIO TECHNOLOGY LLC All rights reserved. 鄂ICP备15011166号-1
webinars: DT3C facilitates antibody internalization X