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Human HSPB1 ELISA Kit for Sandwich ELISA - ABIN2964829
Miyazaki, Nakamura, Hineno, Kobayashi, Kinoshita, Yoshida, Ikeda: Elevation of serum heat-shock protein levels in amyotrophic lateral sclerosis. in Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology 2016
Cow (Bovine) HSPB1 ELISA Kit for Sandwich ELISA - ABIN416577
Hu, Zhang, Zheng, Cheng, Wang: The effect of heat stress on gene expression and synthesis of heat-shock and milk proteins in bovine mammary epithelial cells. in Animal science journal = Nihon chikusan Gakkaihō 2016
this results show the central role of Hsp27 in RACK1 (show GNB2L1 ELISA Kits) pseudosubstrate or LPS (show IRF6 ELISA Kits)-induced cell activation of primary leukocytes
High p-Hsp27 expression is associated with cisplatin resistance in lung cancer.
Low p-Hsp27 expression is associated with pancreatic cancer.
The up-regulation of Hsp27 by E2 is mediated by ERalpha (show ESR1 ELISA Kits)/Sp1 (show PSG1 ELISA Kits).
Study report a novel interaction between mutant HSPB1-P182L and the RNA binding protein (show PTBP1 ELISA Kits) PCBP1 (show PCBP1 ELISA Kits), leading to a reduction in its translational repression activity. Identifying PCBP1 (show PCBP1 ELISA Kits) mRNA targets revealed a marked prevalence for an RNA recognition motif, preferably seen in their 5' and 3'UTRs. Findings further support a role for mutant HSPB1 in neurodegenerative diseases.
Hsp 70 (show HSP70 ELISA Kits) and Hsp 27 were expressed in middle ear effusions
Data suggest that hnRNPK plays role in heat shock response of cells by regulating HSF1; hnRNPK inhibits HSF1 activity, resulting in reduced expression of HSP27 and HSP70 mRNAs; hnRNPK also down-regulates binding of HSF1 to heat shock response element. (hnRNPK = heterogeneous-nuclear ribonucleoprotein K; HSF1 = heat shock transcription factor 1; HSP = heat-shock protein)
High Hsp27 expression is associated with Thyroid Tumors.
There is overwhelming evidence that molecular chaperones such as Hsp27, Hsp70 (show HSP70 ELISA Kits) and Hsp90 (show HSP90 ELISA Kits) are expressed at elevated levels in a wide range of cancers by stabilizing the mutated neoplasm proteins. (Review)
Bradykinin stimulates myofibroblast migration through protein kinase D (show PRKD1 ELISA Kits)-mediated activation of COX-2 (show COX2 ELISA Kits) and Hsp27.
HspB1 is recruited to sites of increased traction force in cells geometrically constrained on micropatterned substrates. Findings elucidate a molecular pathway by which a mechanical signal is transduced via activation of p38 MAPK (show MAPK14 ELISA Kits) to influence actin remodeling and cell migration via a zyxin (show ZYX ELISA Kits)-independent process.
Study report a novel interaction between mutant HSPB1-P182L and the RNA binding protein PCBP1 (show PCBP1 ELISA Kits), leading to a reduction in its translational repression activity. Identifying PCBP1 (show PCBP1 ELISA Kits) mRNA targets revealed a marked prevalence for an RNA recognition motif, preferably seen in their 5' and 3'UTRs. Findings further support a role for mutant HSPB1 in neurodegenerative diseases.
Expression of a phosphomimetic HSPB1 mutant in astrocytes reduced toxicity to motor neurons.
AMPK (show PRKAA1 ELISA Kits)-mediated HSPB1 expression enhanced insulin (show INS ELISA Kits) sensitivity in the skeletal muscle.
e confirmed the modulatory effect of Hspb1 on Purkinje cell degeneration (show AGTPBP1 ELISA Kits) in vivo, as knockdown by Hspb1 shRNA significantly enhanced neuron loss. These results suggest that strategies to promote HSPB1 activity may slow the rate of cerebellar degeneration in NPC (show NPC1 ELISA Kits) disease and highlight the use of bioinformatics tools to uncover pathways leading to neuronal protection in neurodegenerative disorders
Dp71Delta78-79 dystrophin (show DMD ELISA Kits) mutant stimulates neurite outgrowth in cultured neuronal cells via upregulation and phosphorylation of HspB1.
HSPB1 depletion in a mouse model of lung tumorigenesis induced the endothelial-to-mesenchymal transition
Overexpression of HSP27-S135F protein causes peripheral neuropathy. The mouse model can be applied to future development of therapeutic strategies forhereditary motor neuropathy (dHMN) and Charcot-Marie-Tooth disease type 2 F.
cardiac HMGB1 (show HMGB1 ELISA Kits) increases HSPB1 expression and attenuates cardiomyocyte apoptosis associated with doxorubicin-induced cardiomyopathy.
These results suggest that Sox2 (show SOX2 ELISA Kits)-Hspb1 signaling is a possible pathway responsible to tumor progression of QRsP-11
Loss of HspB1 specifically reduces myofibril size in embryonic craniofacial muscles.
Results show the sequence, expression, regulation, and function of a zebrafish protein (zfHsp27) and define zebrafish as a new model for the study of Hsp27 function.
initial upregulation of hsp27 expression occurs during early gastrulation
hspb1 is expressed during development
Hsp27 is dispensable for zebrafish morphogenesis but could play a role in long-term maintenance of heart and muscle tissues.
The data support a mechanism of Hsp27 function where interactions with the titin (show TTN ELISA Kits) filament system protect myofibrils from stress-induced degradation.
Xenopus HSP27, like HSP30, is a developmentally-regulated heat-inducible molecular chaperone (show HSP90AA1 ELISA Kits).
It indicated that Hsp27 was required for porcine circovirus type 2 replication in PK-15 cells culture.
HSP27 expression is gut (show GUSB ELISA Kits) region- and cell type-specific in response to dietary components, microbes, and microbial metabolites to which the mucosa surface is exposed.
These results indicate that Hsp27 expression in the porcine gut (show GUSB ELISA Kits) could be associated with specific dietary fiber components but not the overall microbiota diversity.
Data suggest that targeting HSP27 might offer a useful strategy in cancer treatment.
Data show that the expression of HSP27 and CLIC1 (show CLIC1 ELISA Kits) was strongly positive in 61 (59.2%) and 49 cases (47.6%), respectively.
Data suggest that HSP27 enhanced the metastatic property of NPC (show NPC1 ELISA Kits) cells probably via the NF-kappaB (show NFKB1 ELISA Kits)-mediated activation of MMPs.
Hsp27 expression and its direct chaperoning interaction increase Akt (show AKT1 ELISA Kits) stability and p21 (show CDKN1A ELISA Kits) phosphorylation and nuclear-to-cytoplasm translocation, both essential effects for the survival of ultraviolet-induced DNA-damaged cells.
HSP27 could be a good candidate involved in migration and/or function of neutrophils within the porcine endmetrium.
HSP27 and HSP70 (show HSP70 ELISA Kits) may be used as differential markers to distinguish conventional and low grade central osteosarcoma.
HSP-27 and HSP-70 (show HSP70 ELISA Kits) contribute to modulation of K(+) channel (show KCNC4 ELISA Kits)-induced pial artery dilation
These findings suggest that HSPB1 mediates androgen signaling by binding directly to androgen receptor (show AR ELISA Kits) and then enhancing androgen-mediated myogenesis in myogenic cells.
HSPB1 could have an important role during testosterone-related myogenesis.
CaMKII (show CAMK2G ELISA Kits) is required for redox-sensitive activation of p38 MAPK (show MAPK14 ELISA Kits)/heat shock protein 27 (show HSP27 ELISA Kits) pathway and ERK1/2 (show MAPK1/3 ELISA Kits)
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).
28 kDa heat shock protein
, HSP 27
, estrogen-regulated 24 kDa protein
, heat shock 27 kDa protein
, heat shock 27kD protein 1
, heat shock protein beta-1
, stress-responsive protein 27
, HSP 25
, growth-related 25 kDa protein
, heat shock 25 kDa protein
, heat shock 27kDa protein 1
, heat shock protein, 25 kDa
, truncated hsp25
, heat shock 27 kDa protein 1
, 25 kDa heat shock protein
, 25 kDa IAP
, actin polymerization inhibitor
, inhibitor of actin polymerization
, heat-shock protein
, heat shock protein 27