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Validated All-in-One™ qPCR Primer for HSPB1(NM_001540.4) Search again
Product ID:
HQP009089
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
CMT2F, HEL-S-102, HMN2B, HS.76067, HSP27, HSP28, Hsp25, SRP27
Gene Description:
heat shock protein family B (small) member 1
Target Gene Accession:
NM_001540.4(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
The protein encoded by this gene is induced by environmental stress and developmental changes. The encoded protein is involved in stress resistance and actin organization and translocates from the cytoplasm to the nucleus upon stress induction. Defects in this gene are a cause of Charcot-Marie-Tooth disease type 2F (CMT2F) and distal hereditary motor neuropathy (dHMN). [provided by RefSeq].
Gene References into function
- Phosphatase inhibitors prevent HSP27 dephosphorylation, destruction of stress fibrils, and morphological changes in endothelial cells during ATP depletion
- Characterization of proteins associated with heat shock protein hsp27 in the squamous cell carcinoma cell line A431
- HSP27 expression is cell differentiation and oral squamous cell carcinoma
- in asthmatic subjects the basal epithelium cells express a high level of Hsp27 but no apoptotic morphology.
- Expression of heat-shock protein 25 in dental pulp and enamel organ during odontogenesis in the rat molar. Hsp 25 is related to the formation and maintenance of the ruffled border of ruffle-ended ameloblasts and enamel-free-area cells.
- Has specific actions in renal epithelia subjected to energy depletion, including interacting with actin to preserve architecture in specific intracellular domains.
- Hsp27 has a role in regulating apoptosis through control of Akt activity
- Maps to chromosome 7q11.23. Deletion may be resonsible for cognitive features of Williams syndrome.
- Hsp27 is overexpressed in both dexamethasone resistant multiple myeloma cell lines and primary patient cells.
- HSP27-dependent thermotolerance is suppressed by mumps virus infection through the destruction of STAT-1.
- Taken together, our findings demonstrate that constitutively activated Stat3 up-regulates HSP27 and may facilitate phosphorylation of HSP27 at serine residue 78.
- HSP27 expression was reduced in metaplasia and then significantly increased with neoplastic progresssion in Barrett esophagus. Gender-related differences were obnserved and HSP27 expression was higher in poorly-differentiated adenocarcinoma.
- missense mutation in the gene encoding 27-kDa small heat-shock protein B1 (HSPB1, also called HSP27) that segregates in a family with Charcot-Marie-Tooth disease
- HSP27 is involved in the UVC-resistance of human cells, at least those tested, possibly via functioning in nucleotide excision repair.
- Hsp27 expression and cell survival are regulated by the POU transcription factor Brn3a
- Results showed significant increases in expression and in HSP27 isoform numbers in renal cell carcinoma compared to normal kidney.
- definition of the binding-competent oligomeric state of human Hsp27
- wild-type protein forms smaller oligomers than previously believed, define the roles played by various structural domains in Hsp27 oligomerization
- Hsp27 protects against cytotoxic effects induced by oxidative stress in cultured mammalian cells
- HSP27, an ERbeta-associated protein, shows attenuated expression with coronary atherosclerosis and modulates estrogen signaling.
- Ser(82) in the human heat shock protein Hsp27 is a novel substrate for PKD
- MEK6E activates p38 and results in phosphorylation of its downstream substrate, heat shock protein 27
- HSP25 downregulates PKCdelta, which is a key molecule for radiation-induced ROS generation and mitochondrial-mediated caspase-dependent apoptotic events.
- particularly in conditions of enhanced oxidative stress, lymphomonocytes from liver disease patients present an increased expression of HSP27
- Taken together, our results indicated that expanded ataxin-7 that leads to neurodegeneration significantly impaired the expression of Hsp27 and Hsp70 protein.
- One Hsp27 missense mutation, C379T, was detected in 4 autosomal dominant families with CMT disease type 2, and haplotype analysis indicated that the 4 families probably had a common founder.
- Our results suggest that forms of stress that upregulate HSP27 and its phosphorylation may be useful as novel approaches to prevent adverse ocular effects arising from UV exposure in humans.
- increased level of Hsp27 may reflect a dynamic process of the survived cells to unfold and remove mutant ataxin-3
- The first report of HSP27 gene mutation in Chinese patients with Charcot-Marie-Tooth disease , but it may be not common(0.90%). The C379T mutation in HSP27 gene also causes CMT2 except for distal hereditary motor neuropathy.
- A tumor marker for hepatocellular hepatoma.
- Hsp27 is an active participant in the (de)phosphorylation cascade controlling the activity of the splicing regulator SRp38.
- findings provide a model system for the study of metastatic potential of tumors and are suggestive of an earlier unrecognized role for Hsp25 in tumor migration
- A mutation in the small heat-shock protein HSPB1 leading to distal hereditary motor neuronopathy disrupts neurofilament assembly and the axonal transport of specific cellular cargoes.
- Up-regulation of Hsp27 protein is associated with hepatocellular carcinoma
- Both MAPKAPK2 and HSP27 are necessary for TGFbeta-mediated increases in MMP-2 and cell invasion in human prostate cancer.
- Hsp27 can exploit a large number of oligomerization states
- Heat-shock protein 27 of endothelial cells is modified by methylglyoxal, which may contribute to changes in endothelial cell function associated to diabetes..
- Can be degraded by enzymes released from atherosclerotic plaques. May reflect proteolytic imbalance. Downregulation decreases vascular smooth muscle cell resistance to proteolytically-induced apoptosis. Might play role in prevention of plaque rupture.
- KNG modulate bone marrow derived stromal/preosteoblast cell proliferation and suppress etoposide-induced apoptosis through ERK and HSP27 activation, respectively.
- HSP25 and HSP70i activate HSF1 and have roles in inhibition of ERK1/2 phosphorylation
- Acidic pH exposure protects HEMEC through induction of Hsps and activation of MAPK and PI3 kinase pathway.
- Data show that the suppression of NF-kappaB activation by Entamoeba histolytica in intestinal epithelial cells is mediated by heat shock protein 27.
- Overexpression of HSP27 in Hep-2 cells confers chemoresistance which is associated with the delay in cell growth.
- Hsp27 expression is increased in the normal-appearing vessel adjacent to carotid atherosclerotic plaque.
- A mutation (S135F) in HSP27 that is also associated with these inherited peripheral motor neuron disorders showed increased interaction with wild-type HSP22 also, suggesting linkage of these two etiologic factors, HSP22 and HSP27, into one common pathway
- Exposure to low-level radiofrequency field up to 800 mW/kg does not induce phosphorylation of hsp27 or expression of hsp gene family.
- HSP27 is required for both IL-1 and TNF-induced signaling pathways for which the most upstream common signaling protein is TAK1.
- Plasminogen bound to hsps 27, 60, and 70 and Angiostatin predominantly bound to hsp 27 and to hsp 70 in a concentration- and kringle-dependent manner.
- The muscle of patients undergoing haemodialysis undergoes some adaptive responses in total glutathione content, heat shock protein content and catalase activity that are potentially related to chronic oxidative stress.
- Hsp27 regulates neutrophil chemotaxis and exocytosis
- The function of CD10 in prostate cancer is largely unknown. In the C4-2 CaP cell line, CD10 was found to interact with both HSP27 and HSP70.
- These data highlight an extranuclear interaction between ERbeta and HSP27 that may be of potential importance in modulating estrogen signaling.
- Hsp27 facilitates actin-based Listeria monocytogenes motility through a phosphorylation cycle that shuttles actin monomers to regions of new actin filament assembly.
- HSPs play a role in skeletal muscle recovery and remodeling/adaptation processes to high-force exercise
- Neurotensin induces a striking increase in Hsp27 phosphorylation on Ser-82 in PANC-1 cells through convergent p38 MAPK, PKD, and PKD2 signaling.
- 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.
- caspase-3 prodomain binding to heat shock protein 27 regulates monocyte apoptosis by inhibiting caspase-3 proteolytic activation
- heat shock protein 27-mediated resistance to DNA damaging agents is inhibited by a novel PKC delta-V5 heptapeptide
- These data suggest a potential dynamic and antagonistic interaction between HIV-1 Vpr and a host cell HSP27, suggesting that HSP27 may contribute to cellular intrinsic immunity against HIV infection.
- This study suggests that the functional HSPB1 variant may represent a genetic modifier in the pathogenesis of motor neuron disease
- Contributes to an increased chaperone capacity of cells by binding unfolded proteins that are hereby kept competent for refolding by Hsp70 or that are sorted to nuclear granules if such refolding fails.
- HSP27 expression is modulated in concordance with migration dependent parameters in trophoblast cells.
- activation of protein kinase C delta regulates the phosphorylation of heat shock protein 27 via p38 mitogen-activated protein kinase
- HSP-27 has the potential to redirect monocyte differentiation, derange dendritic cells (DC) and/or macrophage (Mphi)activation, and distort DC or Mphi interaction potential by altering receptor expression, signal transduction, or cytokine production.
- During mitosis, HSF2 is bound to the HSE promoter elements of other heat shock genes, including hsp90 and hsp27, and the proto-oncogene c-fos. The presence of HSF2 is important for expression of these genes.
- A novel pathway regulating human myometrial contraction at labor with HSP27 and alphaB-crystallin as potential targets for future tocolytic studies.
- P38MAP kinase and HSP27 are phosphorylated in pemphigus skin
- Alterations in HSP27 may give early evidence for intracellular differences in aortic aneurysm of patients with bicuspid aortic valve and tricuspid aortic valve.
- These data identify novel nongenomic mechanisms involving androgen, AR, and Hsp27 activation that cooperatively interact to regulate the genomic activity of AR.
- Hsp27 plays a protective role in regulating inflammatory responses in skin
- In response to UBV irradiation, HSP27 in melanocytes translocated from the cytoplasm to the nucleus. The HSP27 responses may provide some protective role against UVB-induced cell damage in the skin.
- HSP27 identified as a differentiation and prognostic marker in neuroblastoma but not in Ewing's sarcoma
- Hsp27 may play a general role in regulation of cellular senescence by modulating the p53 pathway.
- hsp27 not only causes hormone resistance in New World primates but is also crucial to normal estrogen signaling in human cells.
- Heat shock protein 27 (HSP27) was also verified as a downstream common activated protein of PKC beta-ERK(1/2) and PKC beta-p38 MAPK in hepatocellular carcinoma.
- Hsp27 inhibits oxidative stress-induced H9c2 damage and inhibition of ROS generation and the augmentation of Akt activation may be involved in the protective signaling.
- Here we report a novel mutation, G84R, in an elderly patient presenting with strikingly asymmetrical weakness. Expression of this and other known mutations in cell culture demonstrated enhanced aggregation of mutant HSPB1 protein compared with wild-type.
- expression of phosphomimicking HSP27 was sufficient for retaining microfilament formation even when co-expressed with dominant-negative RhoA (EGFP-RhoN17). Thus, HSP27 activation is necessary for microfilament stability independently of RhoA activation
- Sequential measurement intraoperatively of the levels of the heat shock proteins HSP70 and HSP27 in the cerebrospinal fluid can predict those patients who are at greatest risk for paralysis during thoracic aneurysm surgery.
- HSP27 is a novel downstream effector of SPARC-regulated cell morphology and cell migration.
- Hsp27, which is phosphorylated by MK2 in the MAPK pathway, protects epithelial cells from oxidant stress.
- HSP27 regulates cell adhesion and invasion via modulation of focal adhesion kinase and MMP-2 expression.
- phosphorylated heat shock protein 27 up-regulated the levels of p38 mitogen-activated protein kinase and mitogen-activated protein kinase phosphatase-1, an inhibitory protein of extracellular signal-regulated kinase
- Chaperone Hsp27 is a novel subunit that is itself an AU-rich elements (ARE)-binding protein essential for rapid ARE-mRNA degradation.
- Ser135Phe mutation is associated with distal hereditary motor neuropathy type 2 phenotype in a large Korean family
- Data report the expression patterns of HSP27 in the human testes and show differential expression during normal spermatogenesis, and altered expression abnormal spermatogenesis, suggesting that it may be related to the pathogenesis of male infertility.
- Results reveal a novel post-translational modification of Hsp27 involving truncation of the N-terminal Met and acetylation of the penultimate Thr.
- Mutations in the HSP27 (HSPB1) gene cause dominant, recessive, and sporadic distal HMN/CMT type 2.
- HSP27 is closely connected with 5-FU resistance in colon cancer
- Heat shock protein 27 physically interacts with tumor necrosis factor receptor-associated factor 6 and promotes ubiquitination.
- findings show a significant association between low HSP27 expression and nonresponse to neoadjuvant chemotherapy in esophageal adenocarcinoma patients