Recombinant Human Amyloid beta A4 precursor protein-binding family B member 1 (APBB1)

Code CSB-YP001890HU
MSDS
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Source Yeast
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Code CSB-EP001890HU
MSDS
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Source E.coli
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Code CSB-EP001890HU-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-BP001890HU
MSDS
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Source Baculovirus
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Code CSB-MP001890HU
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
APBB1
Uniprot No.
Alternative Names
Adaptor protein FE65a2; Amyloid beta (A4) precursor protein binding family B member 1; Amyloid beta A4 precursor protein binding family B; Amyloid beta A4 precursor protein binding family B member 1; Amyloid beta A4 precursor protein-binding family B member 1; Amyloid beta precursor protein binding family B member 1; APBB 1; APBB1; APBB1_HUMAN; FE 65; Fe65 protein; Protein Fe65; RIR; stat like protein
Species
Homo sapiens (Human)
Expression Region
1-710
Target Protein Sequence
MSVPSSLSQS AINANSHGGP ALSLPLPLHA AHNQLLNAKL QATAVGPKDL RSAMGEGGGP EPGPANAKWL KEGQNQLRRA ATAHRDQNRN VTLTLAEEAS QEPEMAPLGP KGLIHLYSEL ELSAHNAANR GLRGPGLIIS TQEQGPDEGE EKAAGEAEEE EEDDDDEEEE EDLSSPPGLP EPLESVEAPP RPQALTDGPR EHSKSASLLF GMRNSAASDE DSSWATLSQG SPSYGSPEDT DSFWNPNAFE TDSDLPAGWM RVQDTSGTYY WHIPTGTTQW EPPGRASPSQ GSSPQEESQL TWTGFAHGEG FEDGEFWKDE PSDEAPMELG LKEPEEGTLT FPAQSLSPEP LPQEEEKLPP RNTNPGIKCF AVRSLGWVEM TEEELAPGRS SVAVNNCIRQ LSYHKNNLHD PMSGGWGEGK DLLLQLEDET LKLVEPQSQA LLHAQPIISI RVWGVGRDSG RERDFAYVAR DKLTQMLKCH VFRCEAPAKN IATSLHEICS KIMAERRNAR CLVNGLSLDH SKLVDVPFQV EFPAPKNELV QKFQVYYLGN VPVAKPVGVD VINGALESVL SSSSREQWTP SHVSVAPATL TILHQQTEAV LGECRVRFLS FLAVGRDVHT FAFIMAAGPA SFCCHMFWCE PNAASLSEAV QAACMLRYQK CLDARSQAST SCLPAPPAES VARRVGWTVR RGVQSLWGSL KPKRLGAHTP
Protein Length
Full length 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.

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Target Background

Function
Transcription coregulator that can have both coactivator and corepressor functions. Adapter protein that forms a transcriptionally active complex with the gamma-secretase-derived amyloid precursor protein (APP) intracellular domain. Plays a central role in the response to DNA damage by translocating to the nucleus and inducing apoptosis. May act by specifically recognizing and binding histone H2AX phosphorylated on 'Tyr-142' (H2AXY142ph) at double-strand breaks (DSBs), recruiting other pro-apoptosis factors such as MAPK8/JNK1. Required for histone H4 acetylation at double-strand breaks (DSBs). Its ability to specifically bind modified histones and chromatin modifying enzymes such as KAT5/TIP60, probably explains its transcription activation activity. Functions in association with TSHZ3, SET and HDAC factors as a transcriptional repressor, that inhibits the expression of CASP4. Associates with chromatin in a region surrounding the CASP4 transcriptional start site(s). Involved in hippocampal neurite branching and neuromuscular junction formation, as a result plays a role in spatial memory functioning. Plays a role in the maintenance of lens transparency. May play a role in muscle cell strength.
Gene References into Functions
  1. Fe65 is an adaptor protein involved in both processing and signaling of the Alzheimer-associated amyloid-beta precursor protein, APP. Here, the subcellular localization was further investigated using TAP-tagged Fe65 constructs expressed in human neuroblastoma cells. Our results indicate that PTB2 rather than the WW domain is important for the nuclear localization of Fe65. PMID: 28323844
  2. Fe65 Ser289 phosphorylation did not affect the transcriptional activity of the Fe65-APP complex, in contrast to the previously described Ser228 site. PMID: 27176072
  3. Our findings imply that APBB1 plays an important role in the maintenance of EMT-associated CSC-like properties and gamma-radiation resistance via activation of IGF1Rbeta/AKT/GSK3beta pathway in lung cancer cells, highlighting APBB1 as a potential target for therapeutic cancer treatment. PMID: 27836546
  4. Targeted enhancement of the signaling through the Fe65-cortactin pathway, by either HDAC6 inhibition or Tip60 activation, may lead to the development of new therapeutic drugs that are effective for patients with metastatic breast cancers. PMID: 26166158
  5. FE65 influences APP degradation via the proteasome, and phosphorylation of FE65 Ser(610) by SGK1 regulates binding of FE65 to APP, APP turnover and processing. PMID: 26188042
  6. A novel phosphorylation site was identified within Fe65 which mediates gene transcription. PMID: 25397632
  7. The SV2A/FE65 interaction might play a role in synaptic signal transduction. PMID: 24284412
  8. Data indicate that Fe65 is a positive estrogen receptor alpha (ERalpha) transcriptional regulator. PMID: 24619425
  9. FE65 interactions with BLM and MCM proteins may contribute to the neuronal cell cycle re-entry observed in brains affected by Alzheimer's disease. PMID: 23572515
  10. A ternary complex consisting of AICD, FE65, and TIP60 down-regulates Stathmin1. PMID: 22902274
  11. Both amyloid-beta precursor protein and Fe65 are co-localized in model Hirano bodies associated with Alzheimer's disease. PMID: 20133016
  12. Fe65 carries out different functions depending on its location in the regulation of Notch1 signaling. PMID: 22199353
  13. A novel FE65 isoform and the regulation of the splicing events leading to its production may contribute to elucidating neuronal specific roles of FE65 and its contribution to Alzheimer's disease pathology. PMID: 21824145
  14. Phosphorylation of LRP1 regulates the interaction with Fe65. PMID: 21968187
  15. Fe65 binds preferentially to low-density lipoprotein receptor-related protein (LRP) carboxyl terminus when phosphorylated at tyrosine-4507 and in complex with amyloid precursor protein (APP). PMID: 21650223
  16. Fe65 and Dab1 compete for binding to APP. Dab1 significantly decreased the amount of APP bound to LRP and the level of secreted APP and APP-CTF in LRP expressing cells PMID: 20568118
  17. reduced levels of Sp1 resulted in downregulation of endogenous FE65 mRNA and protein PMID: 20091743
  18. The data of this demonstrated that the induction of AICD/Fe65 or transgelin significantly alters actin dynamics and mitochondrial function in neuronal cells PMID: 20405578
  19. The transcriptional activity of the APP intracellular domain-Fe65 complex is inhibited by activation of the NF-kappaB pathway. PMID: 12653567
  20. Adjusting for age and sex, we found a slight risk associated with the deletion in intron 13 of the APBB1 gene for subjects less than 65 years. PMID: 12727304
  21. gamma-Secretase cleavage and binding to FE65 regulate the nuclear translocation of the intracellular C-terminal domain (ICD) of the APP family of proteins. PMID: 12779321
  22. APP and Fe65 mediate transactivation with low density lipoprotein receptor-related protein PMID: 12888553
  23. Abnormal accumulations of the amyloid-beta precursor protein associated with the aging cellular muscle fibers and appear to be the key pathogenic event in iclusion-body myositis. PMID: 14569203
  24. Alcadein and amyloid beta-protein precursor regulates FE65-dependent gene transactivation PMID: 15037614
  25. Fe65 is activated by the APP intracellular domain during transcriptional transactivation PMID: 15044485
  26. p65FE65 may be an intracellular mediator in a signaling cascade regulating alpha-secretion of APP PMID: 15647266
  27. The present work provides evidence that FE65 plays a role in the regulation of amyloid precursor protein processing in an in vivo transgenic mouse model. PMID: 15816856
  28. multiple interactions of AICD with FE65 and 14-3-3gamma modulate FE65-dependent gene transactivation PMID: 16223726
  29. FE65 is the key agent of Gal4DB-mediated transcriptional transactivation, whereas Tip60 is an FE65-associated repressor. PMID: 16332686
  30. Notch1 intracellular domain plays the role of a negative regulator in AICD signaling via the disruption of the AICD-Fe65-Tip60 trimeric complex. PMID: 17368826
  31. Nek6 binds to Fe65 through its (267)PPLP(270) motif; the protein-protein interaction between Nek6 and Fe65 regulates their subcellular localization and cell apoptosis PMID: 17512906
  32. We demonstrated that treatment with EGCG reduced the A beta levels by enhancing endogenous APP nonamyloidogenic proteolytic processing. PMID: 17590240
  33. Results describe the crystal structures of the human FE65 WW domain (residues 253-289) in the apo form and bound to the peptides PPPPPPLPP and PPPPPPPPPL, which correspond to human Mena residues 313-321 and 347-356, respectively. PMID: 17686488
  34. Fe65 regulation of APP proteolysis may be integrally associated with its nuclear signaling function, as all antecedent proteolytic steps prior to release of Fe65 from the membrane are fostered by the APP-Fe65 interaction PMID: 17855370
  35. APP-regulated FE65 plays an important role in the early stress response of cells and that FE65 deregulated from APP induces apoptosis. PMID: 18468999
  36. Thyroid cancers are characterized by APP upregulation, increased membrane targeting of the APP ectodomain and significantly increased mRNA levels of the APP scaffold proteins JIP1, ShcA and Fe65. PMID: 18480379
  37. crystallographic analysis of the human Fe65-phosphotyrosine domain PMID: 18550529
  38. Single nucleotide polymorphisms in APBB1 gene is associated with nicotine dependence. PMID: 18777128
  39. the beta-sheet edge in some natively folded amyloid oligomers is designed positively to prevent beta aggregation PMID: 18800165
  40. Study determined the crystal structure of the carboxy-terminal APP intracellular domain in complex with the C-terminal phosphotyrosine-binding (PTB) domain of Fe65; The unique interface involves the NPxY PTB-binding motif and two alpha helices. PMID: 18833287
  41. Dexras1 functions as a suppressor of FE65-APP-mediated transcription, and FE65 tyrosine 547 phosphorylation enhances FE65-APP-mediated transcription, at least in part, by modulating the interaction between FE65 and Dexras1 PMID: 18922798
  42. The protein-protein interaction between the WW domain of Fe65 and the putative binding motif of Nedd4-2 down-regulates Fe65 protein stability and subcellular localization through its ubiquitylation, to contribute to cell apoptosis. PMID: 19381069

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Subcellular Location
Cell membrane. Cytoplasm. Nucleus. Cell projection, growth cone. Nucleus speckle.
Tissue Specificity
Highly expressed in brain; strongly reduced in post-mortem elderly subjects with Alzheimer disease.
Database Links

HGNC: 581

OMIM: 602709

KEGG: hsa:322

STRING: 9606.ENSP00000299402

UniGene: Hs.372840

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