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Validated All-in-One™ qPCR Primer for BNIP3(NM_004052.3) Search again
Product ID:
HQP017619
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
HABON, NIP3
Gene Description:
BCL2 interacting protein 3
Target Gene Accession:
NM_004052.3(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
This gene is a member of the BCL2/adenovirus E1B 19 kd-interacting protein (BNIP) family. It interacts with the E1B 19 kDa protein which is responsible for the protection of virally-induced cell death, as well as E1B 19 kDa-like sequences of BCL2, also an apoptotic protector. This gene contains a BH3 domain and a transmembrane domain, which have been associated with pro-apoptotic function. The dimeric mitochondrial protein encoded by this gene is known to induce apoptosis, even in the presence of BCL2. [provided by RefSeq].
Gene References into function
- The gene expression of BINP3 was up-regulated during early apoptosis of human hepatoma cells exposed to Paeiniae Radix extract in vitro.
- BNIP3 plays a role in hypoxia-induced cell death in epithelial cells that could be circumvented by growth factor signaling
- Silencing of the hypoxia-inducible cell death protein BNIP3 is associated with pancreatic cancer
- High expression of a hypoxia regulated proapoptotic pathway was associated with a selection of an aggressive phenotype of non-small cell lung cancer.
- Inactivation of BNIP3 likely plays a key role in the progression of some gastrointestinal cancers and that it may be a useful molecular target for therapy.
- loss of BNIP3 expression occurs late in pancreatic cancer, contributes to resistance to chemotherapy, and correlates with a worsened prognosis
- Upregulation of the cell death-related protein BNIP3 is one possible mechanism associated with enterocyte cell death observed in the intestine with NEC.
- In glioblastoma multiforme, BNIP3 expression is increased but it remains sequestered in the nucleus in hypoxic regions, thereby blocking BNIP3's ability to associate with the mitochondria, providing tumor cells with a possible survival advantage
- pro-apoptotic proteins BNip3 and Nix are expressed in the human placenta
- Loss of Bnip-3 expression is critical for malignant and metastatic evasion of hypoxia-induced cell death
- BNIP3 mediated rapid apoptosis that was triggered by p53 in lung cancer cells.
- data suggest that BNIP3 plays an important role in hypoxic cell death and epigenetic mechanisms selectively silence its expression in colorectal cancer
- we observed no correlation between BNIP3 expression and intratumoral hypoxia.
- Up-regulation of BNIP3 expression in DCIS and invasive carcinoma suggests a significant role in breast tumor progression
- SidF contributes to apoptosis resistance in L. pneumophila-infected cells by specifically interacting with and neutralizing the effects of BNIP3 and Bcl-rambo, two proapoptotic members of Bcl2 protein family.
- In humans, BNIP3 is strongly expressed in most follicular lymphomas, especially those that are Bcl-2 negative.
- Photodynamic therapy resistant HT29 cell variants are differentially sensitized to UVA compared with UVC due, in part at least, through the altered expression levels of BNip3, Hsp27 and mutant p53.
- Results identify BNIP3 as a key regulator of hypoxia-induced autophagy and suggest a novel role for the RB tumor suppressor in preventing nonapoptotic cell death by limiting the extent of BNIP3 induction in cells.
- Elevated levels of the phosphoprotein correlated with initiation of Bnip3-dependent death, whereas the dephosphorylated species correlated with extreme acidosis.
- S100A4 has a role in suppression of BNIP3 expression, chemoresistance, and inhibition of apoptosis in pancreatic cancer
- High levels of BNIP3 expression cannot be used as one of the predicting factors for gemcitabine chemosensitivity of pancreatic neoplasms.
- The study suggests that BNIP3 may actually allow cell survival either by preventing ATP depletion or by eliminating damaged mitochondria.
- Bnip3, a hypoxia-inducible Bcl-2 homology 3 domain-containing protein, directly binds Rheb and inhibits the mTOR pathway.
- Prolonged hypoxia induces autophagic cell death in apoptosis-competent cells, through a mechanism involving BNIP3.
- Increased expression of BNIP3 in the malignant gastric epithelial cells compared to normal mucosal epithelial cells suggests that BNIP3 expression may be involved in gastric carcinoma development.
- BNIP3 is directly regulated by hypoxia but that there may be a hormonal independent mechanism coordinating the expression of BNIP3 in prostate tumors.
- These findings suggest that the suppression of BNIP3 expression by TP prevents, at least in part, hypoxia-induced apoptosis.
- ACAA2 is a functional BNIP3 binding partner and provide a possible linkage between fatty acid metabolism and apoptosis of cells.
- Results report that oxygen deprivation can activate the autophagic pathway in human cancer cell lines via AMPK activity, independent of HIF-1, BNIP3, and BNIP3L.
- Preserved BNIP3 function in CRC cells lowers apoptosis, and may thus be involved in alternative cell death pathways, such as autophagic cell death. However, BNIP3 silencing in tumour cells does not impact on hypoxia-driven poorer prognosis
- Expression profiling of apoptosis-related genes in megakaryocytes: BNIP3 is downregulated in primary myelofibrosis.
- under basal nonapoptotic conditions that NF-kappaB constitutively occupies and transcriptionally silences Bnip3 gene transcription by competing with E2F-1