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Validated All-in-One™ qPCR Primer for HSPA5(NM_005347.4) Search again
Product ID:
HQP088416
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
BIP, GRP78, HEL-S-89n
Gene Description:
heat shock protein family A (Hsp70) member 5
Target Gene Accession:
NM_005347.4(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
When Chinese hamster K12 cells are starved of glucose, the synthesis of several proteins, called glucose-regulated proteins (GRPs), is markedly increased. Hendershot et al. (1994) [PubMed 8020977] pointed out that one of these, GRP78 (HSPA5), also referred to as 'immunoglobulin heavy chain-binding protein' (BiP), is a member of the heat-shock protein-70 (HSP70) family and is involved in the folding and assembly of proteins in the endoplasmic reticulum (ER). Because so many ER proteins interact transiently with GRP78, it may play a key role in monitoring protein transport through the cell.[supplied by OMIM].
Gene References into function
- Glucose-regulated protein 78 is induced by chronic hypoxia in human gastric tumor cells through a protein kinase C-epsilon/ERK/AP-1 signaling cascade.
- a coreceptor for coxsackievirus A9, interacts with major histocompatibility complex class I molecules which mediate virus internalization
- p38MAPK is activated by phosphorylated ATF6 and induces HSPA5 binding
- stimulated by HCV replicons
- a molecular chaperone, possibly involved in reduced formation of amyloid-beta protein in the endoplasmic reticulum
- small amounts of circulating, free GRP78 and naturally-occurring anti-GRP78 autoantibodies were detected in the peripheral circulation of healthy human individuals.
- interacts with the large surface protein of hepatitis B virus in vitro
- overexpression of GRP78/BiP decreases thrombin generation thereby suppressing prothrombotic potential of cells
- overexpression of GRP78 results in reduced apoptosis and higher colony survival when challenged with topoisomerase inhibitors
- The endoplasmic reticulum stress pathway mediated by ATF6 and by IRE1-XBP1 systems seems essential for the transformation-associated expression of the grp78 gene in hepatocarcinogenesis
- mononuclear leukocytes responded to BiP with secretion of an antiinflammatory profile of cytokines.
- GRP78 can serve as a novel independent favorable prognostic factor for patients with neuroblastoma.
- ERdj3 is a stress-inducible endoplasmic reticulum DnaJ homologue which serves as a cofactor for BiP's interactions with unfolded substrates
- Interaction with core lipoprotein lipids may facilitate apoB transport out of the ER by reducing Grp78-mediated ER retention.
- Stable BiP binding is essential for ATF6 regulation and that ER stress dissociates BiP from ATF6 by actively restarting the BiP ATPase cycle.
- TFII-I is required for optimal induction of Grp78 by ER stress
- data suggest that amplification of c-myb in tumor cells may lead to robust GRP78 gene induction, which may in turn assist cells in survival under conditions of oxygen deprivation and nutrient stress
- GRP78/BiP plays a protective role against UVC-induced cell death possibly via nucleotide excision repair.
- Upon ER stress, Grp78 promoter is occupied by YY1 mediated in part by the nuclear form of ATF6.
- Endoplasmic reticulum stress pathway mediated by Grp78 may be responsible for controlling the growth of lung cancer cells
- Promotor polymorphisms of HSPA5 may affect the interindividual variability of ER stress response and may confer a genetic risk factor for bipolar disorder.
- Findings indicate that overexpression of GRP78 protein may be an important biomarker for malignant transformation, and increased expression might be related with the posttranscriptional regulation of GRP78 in tumor tissues.
- Disturbed SIL1-HSPA5 interaction and protein folding is the primary pathology in Marinesco-Sjogren syndrome.
- Taken together, GRP78/75 and RHAMM complexes may stabilize microtubules in the interphase, associated with a downregulation of RHAMM. These results reveal a new biochemical activity of RHAMM.
- Up-regulation of GRP78 protein is associated with hepatocellular carcinoma
- REVIEW: transcriptional regulation of Grp78, the molecular basis for the cytoprotective function of GRP78 and its role in cancer progression, drug resistance and potential future cancer therapy
- N-methyl-N'-nitro-N-nitrosoguanidine (MNNG) can induce the clustering of epidermal growth factor receptor (EGFR) with GRP78 in human amnion FL cells.
- These results suggest that CYP2E1 mediated oxidative stress downregulates the expression of GRP proteins in HepG2 cells and oxidative stress is an important mechanism in causing ER dysfunction in these cells.
- The activation and regulation of Akt and NF-kappa B in prostatic cancer cell line 1-LN are reported.
- US2 and US11 bridge the MHC class I heavy chain onto BiP promoting interactions with other ER-associated degradation proteins
- A predictor of responsiveness to drug therapy breast camcer.
- BiP/GRP78 is a defined intracellular target of action and presents an unparalleled opportunity to develop improved therapeutic versions of this cancer-specific apoptosis-inducing cytokine.
- Single molecule dynamics of transcriptional activation in the stress inducible GRP78 promoter, is studied.
- Up-regulation of Grp78 is associated with the development of castration resistance, may serve as an important prognostic indicator of recurrence in a subset of prostate cancer patients
- Retention of amyloidogenic mutant TTRs induced the unfolded protein response and upregulated the expression of BIP.
- GRP78 protein expression is significantly higher in prostate cancer than in benign prostatic tissue. The intensity of expression is significantly associated with survival and clinical recurrence
- Grp78 was present in the uterus and oviduct epithelial cells and was shown to bind to human spermatozoa. Incubation with either exogenous Hsp60 or Grp78 did not affect sperm viability, motility or acrosomal integrity.
- Endoplasmic reticulum chaperones stabilize nicotinic receptor subunits and regulate receptor assembly.
- ERGIC-53 provides a platform that receives micro(2)L(2) subunits from the BiP-dependent checkpoint, assisting polymerization. In this process, ERp44 couples thiol-dependent assembly and quality control.
- proteins co-localize, and changes in the expression of the glucoseregulated protein 78 affect the expression of voltage-dependent anion channel
- When islets were cultured for 24 h at 11.1 mmol/l glucose, there was induction of BiP and XBP-1 in type 2 diabetes islets but not in non-diabetic islets.
- study showed that BiP is significantly increased in mid-frontal cortical grey matter of HIV-infected and neurocognitively impaired patients
- HSPA5 polymorphisms examined in this study are not involved in susceptibility to suicide.
- By contrast, five other human cell lines with lower basal expression of GRP78 protein did not undergo apoptosis when treated with GRP78 siRNA.
- These data suggest that one effect of the controlled expression of BiP/GRP78 in cells infected with cytomegalovirus is to aid in cytoplasmic virion assembly and egress.
- cells coexpressing GRP78 and Cripto grow much more rapidly in soft agar than do cells expressing either protein individually
- The aim was to study the activation of ATF6 and Grp78 in transfected human epithelial cells expressing the DeltaF508-CFTR protein.
- GRP78 may stabilize Raf-1 to maintain mitochondrial permeability and thus protect cells from endoplasmic reticulum stress-induced apoptosis.
- HSP105 appears to chaperone the responses to endoplasmic reticulum (ER) stress through its interactions with GRP78 and GSK3, and without HSP105 cell death following ER stress proceeds by a non-caspase-3-dependent process.
- Culture of human RS cells with pancreatic cancer KP-4 cell-conditioned medium resulted in increased UV mutagenicity, possibly via the down-regulation of glucose-regulated protein 78kDa(GRP78)
- The fully human monoclonal IgM antibody, SAM-6, was isolated from a gastric cancer patient and it binds to a new variant of GRP78 with a molecular weight of 82 kDa. The epitope is an O-linked carbohydrate moiety and is specific for malignant cells.
- tert-butyl hydroperoxide (tBH) increases oxidative stress, increases accumulation of ROS in the ER, and upregulates expression of GRP-78 and GADD153.
- We could demonstrate an association of GRP78 and GRP94 mRNA and protein expression with tumor stage and behaviour in esophageal adenocarcinomas.
- The data of this study suggest that the HSPA5 -415 G/A, -370 C/T, and -180 del/G polymorphisms are unlikely to play a major role in risk of developing PD in Taiwan.
- GRP78 contributes to the increased apoptosis resistance and growth of glioma cells
- Grp78/BiP has a role in T-cadherin-dependent cell survival
- Up-regulated expression of GRP78 and GRP94 was possibly involved in pathogenesis, growth, invasion, and metastasis of gastric carcinomas.
- GRP78 (glucose-regulated protein 78kD) was found to be significantly upregulated in a sustained manner under atheroprone, but not atheroprotective flow up to 24 hours
- These results hint to a new role of BiP in guiding posttranslational hepatitis B virus large envelope protein import into the mammalian ER.
- The endoplasmic reticulum chaperone GRP78/BiP is generally highly elevated in the vasculature derived from human glioma specimens, compared with minimal GRP78 expression in normal brain tissues and blood vessels.
- Expression of GRP78 in macrophages was increased significantly in the affected peripheral joints of ankylosing spondylitis compared with osteoarthritis patients.
- binding of DMP1 with GRP-78 receptor might be an important mechanism by which DMP1 is internalized and transported to the nucleus during bone and tooth development
- overexpression of wild-type BRCA1 suppressed the expression of GRP78, whereas expression of mutant BRCA1 gene or targeted inhibition of endogenous BRCA1 using small-interfering RNA (siRNA) enhanced GRP78 expression.
- our preliminary results may suggest a protective role of the HSPA5 -415 A/-180 G allele in Taiwanese Alzheimer's disease susceptibility
- Grp78 actively regulates multiple malignant phenotypes, including cell growth, migration, and invasion.
- analysis of transcriptional repression of the prosurvival endoplasmic reticulum chaperone GRP78/BIP by E2F1
- These results provide new insights into resistance mechanisms of melanoma cells to CDDP and adriamycin and identify GRP78 as a potential target for enhancing chemosensitivity in melanoma.
- altered expression of proteins that underlie pathogenesis of SCA17
- alpha(2)-macroglobulin-induced increase in GRP78 synthesis is caused by transcriptional upregulation of TFII-I
- Using shotgun mass spectrometry, we found this protein differentially expressed in the dorsolateral prefrontal cortex from patients with schizophrenia.