Recombinant Human Baculoviral IAP repeat-containing protein 7 (BIRC7)

Code CSB-YP839300HU
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Source Yeast
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Code CSB-EP839300HU
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Source E.coli
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Code CSB-EP839300HU-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-BP839300HU
MSDS
Size Pls inquire
Source Baculovirus
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Code CSB-MP839300HU
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
BIRC7
Uniprot No.
Alternative Names
Baculoviral IAP repeat containing 7; Baculoviral IAP repeat containing protein 7; Baculoviral IAP repeat-containing protein 7; BIRC 7; birc7; BIRC7_HUMAN; KIAP; Kidney inhibitor of apoptosis protein; Livin; Livin inhibitor of apotosis; Melanoma inhibitor of apoptosis protein; ML IAP; ML-IAP; MLIAP; RING finger protein 50; RNF 50; RNF50
Species
Homo sapiens (Human)
Expression Region
1-298
Target Protein Sequence
MGPKDSAKCL HRGPQPSHWA AGDGPTQERC GPRSLGSPVL GLDTCRAWDH VDGQILGQLR PLTEEEEEEG AGATLSRGPA FPGMGSEELR LASFYDWPLT AEVPPELLAA AGFFHTGHQD KVRCFFCYGG LQSWKRGDDP WTEHAKWFPS CQFLLRSKGR DFVHSVQETH SQLLGSWDPW EEPEDAAPVA PSVPASGYPE LPTPRREVQS ESAQEPGGVS PAEAQRAWWV LEPPGARDVE AQLRRLQEER TCKVCLDRAV SIVFVPCGHL VCAECAPGLQ LCPICRAPVR SRVRTFLS
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
Apoptotic regulator capable of exerting proapoptotic and anti-apoptotic activities and plays crucial roles in apoptosis, cell proliferation, and cell cycle control. Its anti-apoptotic activity is mediated through the inhibition of CASP3, CASP7 and CASP9, as well as by its E3 ubiquitin-protein ligase activity. As it is a weak caspase inhibitor, its anti-apoptotic activity is thought to be due to its ability to ubiquitinate DIABLO/SMAC targeting it for degradation thereby promoting cell survival. May contribute to caspase inhibition, by blocking the ability of DIABLO/SMAC to disrupt XIAP/BIRC4-caspase interactions. Protects against apoptosis induced by TNF or by chemical agents such as adriamycin, etoposide or staurosporine. Suppression of apoptosis is mediated by activation of MAPK8/JNK1, and possibly also of MAPK9/JNK2. This activation depends on TAB1 and NR2C2/TAK1. In vitro, inhibits CASP3 and proteolytic activation of pro-CASP9. Isoform 1 blocks staurosporine-induced apoptosis. Isoform 2 blocks etoposide-induced apoptosis. Isoform 2 protects against natural killer (NK) cell killing whereas isoform 1 augments killing.
Gene References into Functions
  1. The overexpression of PTEN concomitant with Livin gene silencing was confirmed as a feasible and effective in vitro and in vivo gene modulation method, which may represent a potential therapeutic strategy for the treatment of Gastric Cancer. PMID: 29436592
  2. Livin overexpression not only significantly inhibited RCC cell apoptosis and increased cell viability, but completely reversed the si-CCAT1-mediated repression of cell viability PMID: 28470345
  3. our results revealed that Livin induced EMT through the activation of the p38/GSK3beta pathway, which in turn promoted the progression and metastasis of breast cancer, especially for triple-negative breast cancer (TNBC) PMID: 29039608
  4. our results suggest that siRNA-mediated Livin knockdown enhanced the chemosensitivity of the three head and neck squamous cell carcinoma cell lines to cisplatin, 5-FU and docetaxel. PMID: 28440463
  5. Livin is specifically over-expressed in adrenocortical carcinoma. PMID: 28030838
  6. Further experiments confirmed the induction of cell apoptosis and suppression of cell proliferation by anti-MM scFv-tP in LiBr cells, along with efficient silence of Livin gene both in vitro and in vivo. Altogether, our findings provide a feasible approach to transport Livin small interfering RNA to malignant melanoma cells which would be a new therapeutic strategy for combating malignant melanoma PMID: 28459204
  7. MicroRNA-214 inhibits the osteogenic differentiation of human osteoblasts through the direct regulation of BIRC7. PMID: 28109866
  8. the results of the present study suggested that Livin may enhance tumorigenesis by modulating the mitogenactivated/Akt signaling pathways in human HSCC. PMID: 27175933
  9. Positive BIRC7 expression and negative KLF4 expression are associated with the progression of PDAC and poor prognosis in patients with PDAC. PMID: 27802195
  10. High expression of BIRC7 is associated with drug resistance in Renal cell carcinoma. PMID: 27677286
  11. Data show that cylindromatosis (CYLD) overexpression and livin knockdown might improve gemcitabine chemosensitivity by decreasing autophagy and increasing apoptosis in bladder cancer (BCa) cells. PMID: 27448305
  12. The apoptosisinducing effects of livin and surivin knockdown were investigated using a Hoechst staining kit. PMID: 26708654
  13. Expression of livin, survivin and caspase-3 are closely related to the occurrence and development of prostatic cancer. PMID: 26823716
  14. Our results suggested the important role of Livin and its partner molecule in the process of VSV treatment PMID: 26412467
  15. Data showed that Livin knock-down suppressed cell proliferation and inhibited cell invasion, accompanied by downregulation of VEGF and MMP-2/-9. Its silencing resulted in the prevention of xenograft tumor formation. PMID: 26094984
  16. These findings suggest that livin may be used as a novel target for tumor gene therapy. PMID: 25695324
  17. Upregulation of Livin expression and downregulation of caspase activity are observed under cycling and chronic hypoxia in glioblastoma cells and xenografts. PMID: 25370472
  18. Livin expression was higher in condyloma acuminatum than in normal cells and was correlated with survivin and Ki-67. PMID: 26122233
  19. Livin gene has a high expression in osteosarcoma and inhibits apoptosis in tumor tissue. PMID: 25374170
  20. livin is associated with invasive and oncogenic phenotypes such as tumor cell invasion, tumor cell migration, tumor cell proliferation, and resistance to apoptosis in human oral squamous cell carcinoma cells. PMID: 25242075
  21. These data suggest that livin overexpression plays an important role in tumor invasiveness by mediating resistance to apoptosis. PMID: 25339450
  22. effectively silence Livin gene expression in LoVo colon cancer cells, inhibit cell proliferation and colony formation, induce apoptosis, and enhance sensitivity to cisplatin PMID: 24938471
  23. In diagnostically difficult cases of diffuse large B-cell lymphoma and Hodgkin lymphoma, focus on livin as marker may provide useful corroborative information. PMID: 24767895
  24. Low livin expression is associated with childhood acute lymphoblastic leukemia. PMID: 24696218
  25. Co-silencing of Livin and Survivin can effectively inhibit the cell proliferation and apoptosis of lung cancer cells. PMID: 25261663
  26. Livin expression was not associated with survival in pancreas ductal adenocarcinoma. PMID: 25090821
  27. our findings indicate that the expression of Livin is increased in human GC and correlates with tumor differentiation and lymph node metastases PMID: 24220265
  28. The expression of Livin was was independently related to survival in rectal cancer patients PMID: 24295240
  29. Livin expression was positively correlated with the proliferation marker Ki-67, but was negatively correlated with caspase-3 expression in human ampullary carcinoma patients. PMID: 23343959
  30. Data suggest that Livin has a role in thrombopoiesis by regulating the apoptotic and antiapoptotic balance in MK endoreplication and platelet production. PMID: 24287698
  31. High livin expression is associated with lymph node micrometastasis in non-small cell lung cancer. PMID: 23404657
  32. no significant correlation was found between Livin expression and various clinicopathological parameters including survival. PMID: 24008725
  33. Livin is associated with tumor progression by increasing tumor cell motility and inhibiting apoptosis in colorectal cancer PMID: 24023847
  34. our data suggest that Livin is involved in tumorigenesis of human osteosarcoma and may serve as a promising therapeutic target for osteosarcoma. PMID: 23632777
  35. Livin interaction with caspase-3 and Livin role in the regulation of cell death PMID: 23563149
  36. BRG1 regulates ML-IAP expression by cooperating with MITF to promote transcriptionally permissive chromatin structure on the ML-IAP promoter. PMID: 23480510
  37. High BIRC7 expression is associated with lymph node metastasis in squamous cell/adenosquamous carcinomas and adenocarcinoma of gallbladder. PMID: 23906305
  38. Livin expression promotes breast cancer metastasis through the activation of AKT signaling and induction of EMT in breast cancer cells both in vitro and in vivo. PMID: 23524337
  39. Livin may inhibit apoptosis in cervical squamous cell carcinoma by downregulating caspase-3, thereby promoting disease progression. PMID: 23781587
  40. Genistein can suppress Livin gene expression, induce melanoma cell apoptosis, hinder the cell cycle, and restrain cell proliferation. PMID: 22931613
  41. Survivin and livin mRNA levels in patients with lung cancer were significantly higher than in those with benign lung disease. PMID: 22930255
  42. The increased expression of CD44v6 and Livin in gastric cancer tissue may be closely related with development and progression of gastric cancer. PMID: 22932199
  43. Overexpression of Livin led to cisplatin resistance in colon cancer. PMID: 23188704
  44. study demonstrated the expression of inhibitor of apoptosis proteins, survivin and Livin and the pro-apoptotic protein TSP-1 in endemic Burkitt lymphoma (BL); no significant difference was found between BL and reactive lymphoid hyperplasia PMID: 23030305
  45. Livin expression may be regulated by miR-198 in human prostate cancer cell lines. PMID: 23069480
  46. our data reveal a new, Livin-dependent, apoptotic role for TEAD1 in mammals and provide mechanistic insight downstream of TEAD1 deregulation in cancers. PMID: 23029054
  47. study concludes PTEN and Livin are important in renal clear cell carcinoma development PMID: 22938441
  48. data suggested that livin plays an important role in inhibiting the apoptosis of ovarian cancer cells PMID: 22766624
  49. Bortezomib and arsenic trioxide can induce apoptosis by inhibiting the expression of livin mRNA in Jurkat cells. PMID: 21867610
  50. Livin and survivin may be involved in the pathogenesis and progression of adult acute lymphoblastic leukemia. PMID: 21867615

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Subcellular Location
Nucleus. Cytoplasm. Golgi apparatus. Note=Nuclear, and in a filamentous pattern throughout the cytoplasm. Full-length livin is detected exclusively in the cytoplasm, whereas the truncated form (tLivin) is found in the peri-nuclear region with marked localization to the Golgi apparatus; the accumulation of tLivin in the nucleus shows positive correlation with the increase in apoptosis.
Protein Families
IAP family
Tissue Specificity
Isoform 1 and isoform 2 are expressed at very low levels or not detectable in most adult tissues. Detected in adult heart, placenta, lung, lymph node, spleen and ovary, and in several carcinoma cell lines. Isoform 2 is detected in fetal kidney, heart and
Database Links

HGNC: 13702

OMIM: 605737

KEGG: hsa:79444

STRING: 9606.ENSP00000217169

UniGene: Hs.256126

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