Recombinant Human Tyrosine-protein phosphatase non-receptor type 23 (PTPN23), partial

Code CSB-YP872490HU
MSDS
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Source Yeast
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Code CSB-EP872490HU
MSDS
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Source E.coli
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Code CSB-EP872490HU-B
MSDS
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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.
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Code CSB-BP872490HU
MSDS
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Source Baculovirus
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Code CSB-MP872490HU
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
PTPN23
Uniprot No.
Alternative Names
DKFZP564F0923; EC 3.1.3.48; HD PTP; HD-PTP; His domain containing protein tyrosine phosphatase; His domain protein tyrosine phosphatase; His domain-containing protein tyrosine phosphatase; KIAA1471; Protein tyrosine phosphatase non receptor type 23; Protein tyrosine phosphatase TD 14; Protein tyrosine phosphatase TD14; PTN23_HUMAN; PTP TD14; PTP-TD14; PTPN 23; PTPN23; Tyrosine protein phosphatase non receptor type 23; Tyrosine-protein phosphatase non-receptor type 23
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.

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Target Background

Function
Plays a role in sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs) via its interaction with the ESCRT-I complex (endosomal sorting complex required for transport I), and possibly also other ESCRT complexes. May act as a negative regulator of Ras-mediated mitogenic activity. Plays a role in ciliogenesis.
Gene References into Functions
  1. Mutations in PTPN23 gene is associated with developmental and epileptic encephalopathy. PMID: 29090338
  2. HD-PTP/PTPN23 as a prominent haploinsufficient tumor suppressor gene preventing tumor progression through control of integrin trafficking. PMID: 27210750
  3. the underlying mechanism of PTPN23 function in breast tumorigenesis as that of a key phosphatase that normally suppresses the activity of FYN PMID: 29066500
  4. The role of HD-PTP/PTPN23 in cancer and tumorigenesis is reviewed. PMID: 28620046
  5. Results present crystal structures of the coiled-coil domain of the HD-PTP phosphatase and its complex with UBAP1. The coiled-coil domain adopts an unexpected open and rigid conformation. The HD-PTP:UBAP1 structure identifies the molecular determinants of the interaction and provides a molecular basis for the specific functional cooperation between HD-PTP and UBAP1. PMID: 27839950
  6. HD-PTP acts as an alternative to ESCRT-II and VPS20/CHMP6 as a link between the ESCRT-I and those ESCRT-III protein(s) necessary for ILV formation. PMID: 26221024
  7. Data indicate a regulatory function of non-receptor-type tyrosine phosphatase PTPN23 in maintaining a highly phosphorylated state of survival motor neuron complex protein SMN. PMID: 25392300
  8. PTPN23 is a tumor suppressor and that repression of PTPN23 expression by miR-142-3p plays an important role in the pathogenesis of testicular germ cell tumors. PMID: 23843459
  9. The ESCRT accessory protein HD-PTP/PTPN23 associates with epidermal growth factor receptor (EGFR) and combines with the deubiquitinating enzyme UBPY/USP8 to transfer EGFR from ESCRT-0 to ESCRT-III and drive EGFR sorting to intralumenal vesicles. PMID: 23477725
  10. our findings suggest an evolutionarily conserved function of HDPTP-Rab4 in the regulation of endocytic trafficking, cell adhesion and migration PMID: 22825871
  11. HD-PTP degradation by calpains might result in the acquisition of a more aggressive phenotype in neoplastic cells. PMID: 22510412
  12. loss of PTPN23 may increase the activity of SRC and the phosphorylation status of the E-cadherin/beta-catenin signaling complex to promote tumor growth and invasive behavior in breast cancer PMID: 21724833
  13. Histidine domain-protein tyrosine phosphatase interacts with Grb2 and GrpL PMID: 21179510
  14. These results suggest that HD-PTP amounts might be regulated both at the transcriptional and post-transcriptional levels. PMID: 16408268
  15. data suggest that HD-PTP might participate in modulating endothelial response to angiogenic factors and play a role in regulating the complex events leading to the formation of new vessels PMID: 16720300
  16. We suggest that HD-PTP contributes to the regulation of endothelial motility by modulating the tyrosine phosphorylation of FAK. PMID: 17959146
  17. contributes to the regulation of endothelial migration; may play a role in angiogenesis PMID: 18762272
  18. in Epidermal Growth Factor (EGF) stimulated cells, Src binds to and phosphorylates HD-PTP on tyrosine residues PMID: 18835089
  19. demonstrate that HD-PTP is a catalytically inactive protein tyrosine phosphatase. As such, we identify one residue involved in its inactivation and show that colony growth reduction activity is independent of its PTP activity status in cancer cell lines PMID: 19340315

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Subcellular Location
Nucleus. Cytoplasm. Cytoplasmic vesicle. Endosome. Cytoplasm, cytoskeleton, cilium basal body. Early endosome.
Protein Families
Protein-tyrosine phosphatase family, Non-receptor class subfamily
Database Links

HGNC: 14406

OMIM: 606584

KEGG: hsa:25930

STRING: 9606.ENSP00000265562

UniGene: Hs.25524

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