Recombinant Human Telomeric repeat-binding factor 2-interacting protein 1 (TERF2IP)

Code CSB-YP878922HU
MSDS
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Source Yeast
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Code CSB-EP878922HU
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Source E.coli
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Code CSB-EP878922HU-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-BP878922HU
MSDS
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Source Baculovirus
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Code CSB-MP878922HU
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
TERF2IP
Uniprot No.
Alternative Names
Dopamine receptor interacting protein 5; Dopamine receptor-interacting protein 5; DRIP 5; DRIP5; hRap1; MGC105533; RAP 1; RAP1 homolog; RAP1, yeast, homolog if; RAP1, yeast, homolog of; Repressor/activator protein 1 homolog; TE2IP_HUMAN; Telomeric Repeat Binding Factor 2 Interacting Protein; Telomeric repeat-binding factor 2-interacting protein 1; TERF2-interacting protein; TERF2-interacting telomeric protein 1; TERF2IP; TRF2 Interacting Telomeric Protein RAP1; TRF2 interacting telomeric RAP1 protein; TRF2-interacting telomeric protein 1; TRF2-interacting telomeric protein
Species
Homo sapiens (Human)
Expression Region
2-399
Target Protein Sequence
AEAMDLGKD PNGPTHSSTL FVRDDGSSMS FYVRPSPAKR RLSTLILHGG GTVCRVQEPG AVLLAQPGEA LAEASGDFIS TQYILDCVER NERLELEAYR LGPASAADTG SEAKPGALAE GAAEPEPQRH AGRIAFTDAD DVAILTYVKE NARSPSSVTG NALWKAMEKS SLTQHSWQSL KDRYLKHLRG QEHKYLLGDA PVSPSSQKLK RKAEEDPEAA DSGEPQNKRT PDLPEEEYVK EEIQENEEAV KKMLVEATRE FEEVVVDESP PDFEIHITMC DDDPPTPEED SETQPDEEEE EEEEKVSQPE VGAAIKIIRQ LMEKFNLDLS TVTQAFLKNS GELEATSAFL ASGQRADGYP IWSRQDDIDL QKDDEDTREA LVKKFGAQNV ARRIEFRKK
Protein Length
Full Length of Mature Protein
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
Acts both as a regulator of telomere function and as a transcription regulator. Involved in the regulation of telomere length and protection as a component of the shelterin complex (telosome). In contrast to other components of the shelterin complex, it is dispensible for telomere capping and does not participate in the protection of telomeres against non-homologous end-joining (NHEJ)-mediated repair. Instead, it is required to negatively regulate telomere recombination and is essential for repressing homology-directed repair (HDR), which can affect telomere length. Does not bind DNA directly: recruited to telomeric double-stranded 5'-TTAGGG-3' repeats via its interaction with TERF2. Independently of its function in telomeres, also acts as a transcription regulator: recruited to extratelomeric 5'-TTAGGG-3' sites via its association with TERF2 or other factors, and regulates gene expression. When cytoplasmic, associates with the I-kappa-B-kinase (IKK) complex and acts as a regulator of the NF-kappa-B signaling by promoting IKK-mediated phosphorylation of RELA/p65, leading to activate expression of NF-kappa-B target genes.
Gene References into Functions
  1. These data reveal a MAPK pathway-independent switch in response to cAMP signaling during melanoma progression.Implications: The prosurvival mechanism involving the cAMP-EPAC-RAP1 signaling pathway suggest the potential for new targeted therapies in melanoma. PMID: 28851815
  2. Rap1 telomeric and non-telomeric functions and potential implications in diabetic cardiomyopathy have been discussed. (Review) PMID: 28853973
  3. the cytoplasmic RAP1-NF-kappaB-BCL2 axis represents a key pathway to cisplatin resistance in non-small cell lung cancer cells. PMID: 28518145
  4. Rap1GAP functions as a novel suppressor of epithelial mesenchymal transformation and tumor metastasis in gastric cancer, and loss of Rap1GAP predicts poor prognosis. PMID: 28009991
  5. The formation of the Rap1-TRF2 complex restored DNA unwinding. PMID: 28981702
  6. Rap1 may induce hepatic ischemia reperfusion injury (IRI) through promoting neutrophils inflammatory response. Rap1 may be the potential therapeutic target of attenuating hepatic IRI. PMID: 27050284
  7. The Rap1-RIAM-talin axis of integrin activation and blood cell function PMID: 27207789
  8. Rap1 activation was dependent on PKA and required Src family kinases and the Rap1 exchanger C3G. PMID: 27531745
  9. RAP1 promotes colorectal cell migration through the regulation of Vimentin and RAP1 may act as a potential target for the diagnosis and therapy of CRC. PMID: 28381157
  10. Data show that isoform beta2 of the heregulin (HRGbeta2) localizes at telomeres with the telomere-associated proteins TRF2 and RAP1. PMID: 26318724
  11. Data indicate telomere-binding protein RAP1 as an interacting partner of isoform beta2 of the heregulin (HRGbeta2). PMID: 26327598
  12. In pro-inflammatory macrophages, Rap1 promotes cytokine production via NFkappaB activation favoring a pro-inflammatory environment which may contribute to the development and progression of atherosclerosis. PMID: 26505215
  13. Through a combination of biochemical, biophysical and structural approaches, we unveiled a unique mode of assembly between RAP1 and TRF2 PMID: 26748096
  14. the conservation of Rap1 reflects its role in transcriptional regulation rather than a function at telomeres. PMID: 25453752
  15. These findings reveal Pkp3 as a coordinator of desmosome and adherens junction assembly and maturation through its functional association with Rap1. PMID: 25208567
  16. Data show that full-length repressor activator protein 1 (Rap1) binds to full-length telomeric repeat binding factor 2 (TRF2) with high affinity and equimolar ratio. PMID: 25675958
  17. C3G/RAP1 activity is involved in the metastatic spread of epithelial ovarian cancer. PMID: 25617801
  18. a detailed analysis of individual focal adhesion parameters identified focal adhesion size, sliding and intensity as primary targets of Rap1. PMID: 25447308
  19. Nonsense mutations in the TERF2IP gene in familial melanoma: four families carried TERF2IP variants, which included nonsense mutations in both genes (p.Q320X and p.R364X, respectively). PMID: 25505254
  20. results indicate that Rap1 miRNA can effectively enhance sensitivity of HepG2 cell line to 5-FU chemotherapy PMID: 24549317
  21. Loss of epithelial integrity in tumorigenesis involves activation of RAP1 via exchange protein directly activated by cAMP (EPAC). PMID: 24316969
  22. chemokine unresponsiveness in chronic lymphocytic leukemia lymphocytes results from failure of Arf1/phospholipase D1-mediated translocation of Rap1 to the plasma membrane for GTP loading and may be a specific feature of anergy induced by DNA Ags. PMID: 23804711
  23. results reveal an effector pathway for Rap1 in the modulation of Rho signaling and actin dynamics, through which Rap1 modulates endothelial barrier function PMID: 23798437
  24. These data provide evidence for the involvement of the Epac/Rap1 signaling pathway in cAMP-mediated decidualization of human endometrial stromal cells. PMID: 23352189
  25. these results demonstrate PRL-3 as a novel regulator of NF-kappaB signaling pathway through RAP1. PMID: 23178297
  26. Mesenchymal high-grade glioma is maintained by the ID-RAP1 axis. PMID: 23241957
  27. as hTRF2 recruits hRap1 to telomeric sequences, hRap1 alters the affinity of hTRF2 and its binding preference on telomeric DNA. Moreover, the TRF2-Rap1 complex has higher ability to re-model telomeric DNA PMID: 23086976
  28. Data uncover a new Epac-Rap1-dependent pathway by which endothelial cells can regulate WPB exocytosis in response to agonists that signal through cAMP. PMID: 22511766
  29. Lyn controls spatial activation of Rap1 by recruiting the CrkL-C3G protein complex to the leading edge PMID: 21628423
  30. Study investigated the binding sites of telomeric proteins along human chromosomes; RAP1 and TRF2 could be found on a small number of interstitial sites, including regions that are proximal to genes. PMID: 21423278
  31. Mouse gene deletion experiments revealed DNA-damage-response pathways that threaten chromosome ends and how the components of the telomeric shelterin complex prevent activation of these pathways.[Shelterin] PMID: 21209389
  32. N-terminal myr-tagged SKAP1 for membrane binding facilitated constitutive RapL membrane and Rap1 binding and effectively substituted for PI3K and TCR ligation in the activation of LFA-1 in T cells. PMID: 21669874
  33. Rap1 controls cadherin function to regulate somal translocation in the neocortex. PMID: 21315259
  34. play a role in telomere regulation and may contribute to the telomeric fusions and chromosomal abnormalities observed in ulcerative colitis; a biomarker for associated cancer risk PMID: 20061197
  35. Data found that Rap1 binds to both telomeres and to extratelomeric sites through the (TTAGGG)(2) consensus motif. Extratelomeric Rap1-binding sites were enriched at subtelomeric regions. PMID: 20622869
  36. levels of Rap1 are positively regulated by NF-kappaB, and human breast cancers with NF-kappaB hyperactivity show elevated levels of cytoplasmic Rap1. PMID: 20622870
  37. Data show that actin bundle formation and subsequent linkage between actin bundles and VE-cadherin through alpha- and beta-catenins are important for the stabilization of VE-cadherin at the cell-cell contacts in cAMP-Epac-Rap1 signal-activated cells. PMID: 20032304
  38. TRF2/RAP1 prevents classical-non-homologous end-joining-mediated end fusion at the initial DNA-dependent protein kinase end binding and activation step. PMID: 20407424
  39. Findings provide the first demonstration that the interplay between Rap1 and E-cadherin along the endocytic recycling pathway serves as a timely and efficient mechanism to regulate hESC self-renewal. PMID: 20039365
  40. OZF overexpression in tumours may alter the balance between hRap1 and other telomeric proteins PMID: 15838871
  41. Biochemical fractionation and reconstitution revealed that telomere protection is mediated by a RAP1/TRF2 complex, providing evidence for direct role for human RAP1 in protection of telomeric DNA from nonhomologous end-joining at telomeric DNA ends. PMID: 17499040
  42. Suggest a role for cAMP/Epac1/Rap1 pathway in regulating proliferation of pancreatic carcinoma cells. PMID: 18580452
  43. Rap1-induced activation of both alpha4beta1 and alphaLbeta2 is defective, autocrine VEGF and chemokine are necessary to activate alpha4beta1 for ligand binding. PMID: 18922916

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Subcellular Location
Nucleus. Cytoplasm. Chromosome. Chromosome, telomere.
Protein Families
RAP1 family
Tissue Specificity
Ubiquitous. Highly expressed.
Database Links

HGNC: 19246

OMIM: 605061

KEGG: hsa:54386

STRING: 9606.ENSP00000300086

UniGene: Hs.301419

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