Recombinant Human Receptor-type tyrosine-protein phosphatase alpha (PTPRA), partial

Code CSB-YP019047HU1
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Source Yeast
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Code CSB-EP019047HU1
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Source E.coli
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Code CSB-EP019047HU1-B
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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-BP019047HU1
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Source Baculovirus
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Code CSB-MP019047HU1
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
PTPRA
Uniprot No.
Alternative Names
PTPRA; PTPA; PTPRL2; Receptor-type tyrosine-protein phosphatase alpha; Protein-tyrosine phosphatase alpha; R-PTP-alpha
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.

Customer Reviews and Q&A

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Target Background

Function
Tyrosine protein phosphatase which is involved in integrin-mediated focal adhesion formation. Following integrin engagement, specifically recruits BCAR3, BCAR1 and CRK to focal adhesions thereby promoting SRC-mediated phosphorylation of BRAC1 and the subsequent activation of PAK and small GTPase RAC1 and CDC42.
Gene References into Functions
  1. Multivariate Cox regression analysis suggested that PTPRA expression was an independent prognostic factor in SCC patients. In the cellular models, PTPRA promotes SCC cell proliferation through modulating Src activation as well as cell cycle progression. In conclusion, higher PTPRA level was associated with worse prognosis of SCC patients and PTPRA could promote the cell cycle progression PMID: 28656243
  2. VacA mediates CagA phosphorylation through RPTPalpha in AZ-521 cells. PMID: 27935824
  3. A receptor type-protein tyrosine phosphatase alpha-Src family kinase-Rap1 pathway was identified as responsible for recruiting myosin IIB to the zonula adherens in epithelial cells and supporting contractile tension. PMID: 25631816
  4. no evidence was seen for the association of rare, missense mutations in the PTPRA gene with schizophrenia or autism spectrum disorders PMID: 25393624
  5. Data indicate that scaffold protein RACK1 plays a role in IGF-1-mediated protein-tyrosine phosphatase alpha (PTPalpha) tyrosine phosphorylation in MCF-7 Cells. PMID: 25694432
  6. recruited to epithelial adherens junctions for cadherin-dependent cell adhesion and tissue architecture formation PMID: 24652832
  7. Results suggest that inhibition of PTPalpha can have a beneficial effect on HER2-positive breast cancers, but that inhibition of additional targets is needed to block breast tumorigenesis. PMID: 23318421
  8. results suggest that PTPalpha links activation of epidermal growth factor receptor (EGFR) signaling with Src activation and may provide a novel therapeutic target for treatment of breast cancer. PMID: 23532252
  9. A single-nucleotide polymorphism (rs6138953) on the PTPRA gene in the 20p13 region was found to be associated with elevated fasting glucose level. PMID: 23487342
  10. The extracellular proteolytic processing is a novel mechanism for PTPalpha regulation. PMID: 22647903
  11. our results suggest that plasma PTPalpha and fibronectin may be associated with opisthorchiasis. PMID: 23029023
  12. convergent evidence reported here links RPTP to schizophrenia. PMID: 21831360
  13. The transformed cells were tumourigenic in nude mice, suggesting that RPTPalpha245-induced activation of Src in the human tumours may have contributed to carcinogenesis. PMID: 21725282
  14. the PTPalpha-mediated increase of NB-3 level at the cell surface represents a novel function of PTPalpha in NB-3 signaling in neural development PMID: 21622556
  15. a novel role for E-loop residue Lys182 in enhancing HePTP catalytic activity through its interaction with Asp236 of the WPD loop was revealed. PMID: 21094165
  16. force-responsive proteins such as RPTPalpha can influence cancer-cell behavior and identify potential targets for cancer therapy. PMID: 20208566
  17. In entering mitosis the cell cycle-specific regulation of c-Src by RPTPalpha can occur by dephosphorylation of phospho-Tyr527 that activates c-Src in a reaction catalyzed by the transmembrane receptor-like protein tyrosine phosphatase RPTPalpha. PMID: 11796915
  18. interactions between RPTP-domain1s and RPTP-domain 2s are a common but specific mechanism that is likely to be regulated- domain2s and the wedge structures are crucial determinants of binding specificity, thus regulating cross-talk between RPTPs PMID: 12376545
  19. RPTPs have the capacity for inside-out signaling PMID: 12582170
  20. This protein regulates nuclear translocation of ERK2 and can modulate megakaryocytic differentiation of K562 cells. PMID: 12592337
  21. data suggest that receptor-like protein tyrosine phosphatase alpha acts as a receptor for Helicobacter pylori VacA toxin in G401 cells PMID: 12626515
  22. Receptor protein tyrosine phosphatase alpha signaling has a role in androgen depletion-induced neuroendocrine differentiation of prostate tumor cells PMID: 14555984
  23. These data reveal a functional relevance of PTP alpha for insulin secretion. PMID: 14592422
  24. PTPRA and PTPRZ may have roles in gastric cancer progression including lymphovascular invasion and liver/peritoneal dissemination PMID: 16338072
  25. the two splice variants of PTPalpha are expressed differentially and regulate c-Src activity in different ways. PMID: 17212655
  26. siRNA-mediated suppression of protein tyrosine phosphatase alpha (PTP alpha) reduces Src activity 2 to 4-fold in breast, colon and other human cancer cell lines. PMID: 18183590
  27. CD63 plays a role in the regulation of ROMK channels through its association with RPTPalpha, which in turn interacts with and activates Src family PTK, thus reducing ROMK activity. PMID: 18211905
  28. This study showed that PTPalpha is required for remodeling of focal adhesion during cell spreading via a pathway involving Rac1. PMID: 18216165
  29. report a statistically significant lower expression intensity of PTEN and HePTP PMID: 18728972
  30. RPTPalpha plays a critical role in HCN channel function via tyrosine dephosphorylation PMID: 18768480
  31. PTPalpha acts as an adaptor to mediate functional links between focal adhesions and the endoplasmic reticulum that enable IL-1-induced Ca2+ signaling. PMID: 19497848

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Subcellular Location
Cell membrane; Single-pass type I membrane protein. Cell junction, focal adhesion.
Protein Families
Protein-tyrosine phosphatase family, Receptor class 4 subfamily
Database Links

HGNC: 9664

OMIM: 176884

STRING: 9606.ENSP00000369756

UniGene: Hs.269577

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