Human Programmed cell death 6-interacting protein(PDCD6IP) ELISA kit

Code CSB-EL017673HU
Size 96T,5×96T,10×96T
Trial Size 24T ELISA kits trial application
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Product Details

Target Name programmed cell death 6 interacting protein
Alternative Names AIP1 ELISA Kit; ALG 2 interacting protein 1 ELISA Kit; ALG-2-interacting protein 1 ELISA Kit; ALG2 interacting protein X ELISA Kit; Alix ELISA Kit; Apoptosis linked gene 2 interacting protein X ELISA Kit; Dopamine receptor interacting protein 4 ELISA Kit; DRIP4 ELISA Kit; Hp95 ELISA Kit; KIAA1375 ELISA Kit; MGC17003 ELISA Kit; PDC6I_HUMAN ELISA Kit; PDCD6 interacting protein ELISA Kit; PDCD6-interacting protein ELISA Kit; PDCD6IP ELISA Kit; Programmed cell death 6 interacting protein ELISA Kit; Programmed cell death 6-interacting protein ELISA Kit
Abbreviation PDCD6IP
Uniprot No. Q8WUM4
Species Homo sapiens (Human)
Sample Types serum, plasma, tissue homogenates, cell lysates
Detection Range 47 pg/mL-3000 pg/mL
Sensitivity 11.7 pg/mL
Assay Time 1-5h
Sample Volume 50-100ul
Detection Wavelength 450 nm
Research Area Cell Biology
Assay Principle quantitative
Measurement Sandwich
Intra-assay Precision (Precision within an assay): CV%<8%
Three samples of known concentration were tested twenty times on one plate to assess.
Inter-assay Precision (Precision between assays): CV%<10%
Three samples of known concentration were tested in twenty assays to assess.
To assess the linearity of the assay, samples were spiked with high concentrations of human PDCD6IP in various matrices and diluted with the Sample Diluent to produce samples with values within the dynamic range of the assay.
  Sample Serum(n=4)
1:1 Average % 91
Range % 83-99
1:2 Average % 90
Range % 84-94
1:4 Average % 97
Range % 93-103
1:8 Average % 103
Range % 95-107
The recovery of human PDCD6IP spiked to levels throughout the range of the assay in various matrices was evaluated. Samples were diluted prior to assay as directed in the Sample Preparation section.
Sample Type Average % Recovery Range
Serum (n=5) 101 96-107
EDTA plasma (n=4) 89 84-94
Typical Data
These standard curves are provided for demonstration only. A standard curve should be generated for each set of samples assayed.
pg/ml OD1 OD2 Average Corrected
3000 2.522 2.554 2.538 2.370
1500 1.984 2.069 2.027 1.859
750 1.472 1.464 1.468 1.300
375 0.849 0.828 0.839 0.671
187.5 0.514 0.499 0.507 0.339
94 0.356 0.381 0.369 0.201
47 0.239 0.252 0.246 0.078
0 0.168 0.167 0.168  
and FAQs
Storage Store at 2-8°C. Please refer to protocol.
Lead Time 5-7 working days

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Target Data

Function Multifunctional protein involved in endocytosis, multivesicular body biogenesis, membrane repair, cytokinesis, apoptosis and maintenance of tight junction integrity. Class E VPS protein involved in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome. Binds to the phospholipid lysobisphosphatidic acid (LBPA) which is abundant in MVBs internal membranes. The MVB pathway requires the sequential function of ESCRT-O, -I,-II and -III complexes
Gene References into Functions
  1. our results identify the CD63-syntenin-1-ALIX complex as a key regulatory component in post-endocytic HPV trafficking. PMID: 27578500
  2. Alix acts in concert with endophilin A to promote clathrin-independent endocytosis of cholera toxin and to regulate cell migration. PMID: 27244115
  3. Revealed the transition of diffuse ALIX protein signals into a multivesicular body-like pattern during adenoma-carcinoma sequence in colorectal neoplasms. PMID: 27150162
  4. Alix plays an important role in the proliferation of glioma cells and overexpression in gliomas predicts poor survival. PMID: 26980041
  5. ALIX regulates P2Y1 degradation. PMID: 27301021
  6. farnesylation of K-Ras was required for its packaging within extracellular nanovesicles, yet expressing a K-Ras farnesylation mutant did not decrease the number of nanovesicles or the amount of Alix protein released per cell. PMID: 27909058
  7. These findings indicate that Alix binds to Ago2 and miRNAs, suggesting that it plays a key role in miRNA enrichment during extracellular vesicles biogenesis. PMID: 26935291
  8. The authors find that HIV-1 nucleocapsid mimics the PDZ domains of syntenin, a membrane-binding adaptor involved in cell-to-cell contact/communication, to capture the Bro1 domain of ALIX, which is an ESCRTs recruiting cellular adaptor. PMID: 26962944
  9. We found that ARRDC3 is required for ALIX ubiquitination induced by activation of PAR1 PMID: 26490116
  10. phosphorylation of the intramolecular interaction site in the PRD is one of the major mechanisms that activates the ESCRT function of ALIX PMID: 26859355
  11. homologous domain of human Bro1 domain-containing proteins, Alix and Brox, binds CHMP4B but not STAM2, despite their high structural similarity PMID: 26866605
  12. Accordingly, ALIX depletion leads to furrow regression in cells with chromosome bridges, a phenotype associated with abscission checkpoint signaling failure. PMID: 26929449
  13. Findings indicate that the PDCD6IP 15bp insertion/deletion polymorphism decreases the risk of breast neoplasm in an Iranian population. PMID: 26063962
  14. The serum lever of Alzheimer's disease were decrease and the expression of ALIX strongly correlated with the Mini-Mental State Examination scores of the AD patients PMID: 25502766
  15. our findings identify heparanase as a modulator of the syndecan-syntenin-ALIX pathway, fostering endosomal membrane budding and the biogenesis of exosomes by trimming the heparan sulfate chains on syndecans PMID: 25732677
  16. Our data reveal that AIP1, by inhibiting VEGFR2-dependent signaling in tumor niche, suppresses tumor EMT switch, tumor angiogenesis, and tumor premetastatic niche formation to limit tumor growth and metastasis. PMID: 26139244
  17. Lack of ALG-2, ALIX or Vps4B each prevents shedding, and repair of the injured cell membrane PMID: 25534348
  18. Alix is critically involved in multivesicular body sorting of membrane receptors in mammalian cells. PMID: 25510652
  19. Aip1 has a role in actin filament severing by cofilin and regulates constriction of the cytokinetic contractile ring PMID: 25451933
  20. ALIX is recruited to the neck of the assembling HIV-1 virion and is mostly recycled after virion release. PMID: 24834918
  21. Results suggest that programmed cell death 6 interacting protein (PDCD6IP) insertion/deletion polymorphism was potentially related to non-small cell lung cancer (NSCLC) susceptibility in Chinese Han population. PMID: 24870593
  22. HIV-1 Nef interacts with Alix in late endosomes, and this is required for efficient lysosomal targeting of CD4. PMID: 25118280
  23. Syntenin-ALIX exosome biogenesis and budding into multivesicular bodies are controlled by ARF6 and PLD2. PMID: 24637612
  24. Alix protein plays a critical role in the maintenance of the barrier function of T84 monolayers PMID: 24712823
  25. ALIX regulates these mammalian cell-specific cytokinesis, exosome release, and virus budding. [Review] PMID: 24287454
  26. The results of in vitro binding assays using purified recombinant proteins indicated that ALG-2 functions as a Ca(2)-dependent adaptor protein that bridges ALIX and ESCRT-I to form a ternary complex PMID: 23924735
  27. Common genetic variations in PDCD6IP may influence hepatocellular carcinoma risk, possibly through promoter activity-mediated regulation. PMID: 23777424
  28. Alix serves as an adaptor that allows human parainfluenza virus type 1 to interact with the host cell ESCRT system. PMID: 23527201
  29. Lysobisphosphatidic acid recruits ALIX onto late endosomes via the calcium-bound Bro1 domain, triggering a conformational change in ALIX to mediate the delivery of viral nucleocapsids to the cytosol during infection. PMID: 23664863
  30. Data indicate that AP-3 facilitates PAR1 interaction with ALIX. PMID: 22833563
  31. study reports that the V domain of ALIX binds directly and selectively to K63-linked polyubiquitin chains, exhibiting a strong preference for chains composed of more than three ubiquitins PMID: 23201121
  32. BFRF1 recruits the ESCRT components to modulate nuclear envelope for the nuclear egress of Epstein Barr virus. PMID: 22969426
  33. At the midbody, BRCA2 influences the recruitment of endosomal sorting complex required for transport (ESCRT)-associated proteins, Alix and Tsg101, and formation of CEP55-Alix and CEP55-Tsg101 complexes during abscission. PMID: 22771033
  34. Structural recognition mechanisms between human Src homology domain 3 (SH3) and ALG-2-interacting protein X (Alix PMID: 22641034
  35. Identify key role for syndecan-syntenin-ALIX in membrane transport and signalling processes. PMID: 22660413
  36. structural analysis of the Bro1 domain protein BROX and functional analyses of the ALIX Bro1 domain in HIV-1 budding PMID: 22162750
  37. Mutation of residues within the Phe105 loop of the Bro1 domain compromise Alix function in HIV-1 release. PMID: 21889351
  38. Mutations designed to destabilize the closed conformation of the V domain opened the V domain, increased ALIX membrane association, and enhanced HIV-1 budding. PMID: 21715492
  39. Data suggest that the boomerang-shaped Bro1 domain of Alix appears to escort hepatitis B virus naked capsids without ESCRT. PMID: 21129143
  40. HIV-1 infection affects the expression of host factors TSG101 and Alix PMID: 21528537
  41. The authors demonstrate that ALIX/AIP1, an ESCRT-associated host protein, is required for the incorporation of the nucleoprotein of Mopeia virus, a close relative of Lassa virus, into Z-induced virus-like particles (VLPs). PMID: 21248028
  42. Crystal structures revealed that anchoring tyrosines and nearby hydrophobic residues contact the ALIX V domain, revealing how SIV gag proteins employ a diverse family of late-domain sequences to bind ALIX and promote virus budding. PMID: 20962096
  43. studies on intramolecular interactions:the relieving of specific, autoinhibitory interactions within ALIX regulates binding with ESCRT proteins or viral proteins and is critical for ALIX to participate in retroviral budding PMID: 20929444
  44. Examined changes in subcellular proteomes of different cellular compartments of human endothelial cells upon DENV2 infection. Double immunofluorescence staining revealed colocalization of Alix with late endosomal lysobisphosphatidic acid (LBPA). PMID: 20669987
  45. Identification and biophysical assessment of the molecular recognition mechanisms between the human haemopoietic cell kinase Src homology domain 3 and ALG-2-interacting protein X PMID: 20670214
  46. inability of the two-residue shorter ALG-2 isoform to bind Alix PMID: 20691033
  47. The results indicate YLDL motif in M protein is essential for efficient budding in the context of virus infection and suggest involvement of Alix/AIP1 in Sendai virus budding. PMID: 20605035
  48. Together these data support a model in which Alix recruits Nedd4-1 to facilitate HIV-1 release mediated through the LYPX(n)L/Alix budding pathway via a mechanism that involves Alix ubiquitination. PMID: 20519395
  49. p95 has roles in regulating cell adhesion and morphology. PMID: 12360406
  50. AIP1/Alix interacts with the apoptosis-linked protein ALG-2 and recognizes recognize the protein-protein binding motif YPXL/I, where Tyr, Pro, and Leu/Ile are crucial for its interactive properties PMID: 12588984

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Subcellular Location Cytoplasm, cytosol, Melanosome, Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, Secreted, exosome, Cell junction, tight junction, Midbody, Midbody ring
Database Links

HGNC: 8766

OMIM: 608074

KEGG: hsa:10015

STRING: 9606.ENSP00000411825

UniGene: Hs.475896


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