HSPB8 (Human) Recombinant Protein (Q01)
- Known as:
- HSPB8 (Human) Recombinant Protein (Q01)
- Catalog number:
- H00026353-Q01-25
- Product Quantity:
- 25 ug
- Category:
- -
- Supplier:
- Abno
- Gene target:
- HSPB8 (Human) Recombinant Protein (Q01)
Related genes to: HSPB8 (Human) Recombinant Protein (Q01)
- Gene:
- HSPB8 NIH gene
- Name:
- heat shock protein family B (small) member 8
- Previous symbol:
- -
- Synonyms:
- H11, E2IG1, HSP22, HspB8, CMT2L
- Chromosome:
- 12q24.23
- Locus Type:
- gene with protein product
- Date approved:
- 2004-01-29
- Date modifiied:
- 2019-04-23
Related products to: HSPB8 (Human) Recombinant Protein (Q01)
Related articles to: HSPB8 (Human) Recombinant Protein (Q01)
- This study aims to investigate the role of the lncRNA LUCAT1 in cerebral infarction-induced neurological damage. In vitro experiments employed N2a cells to establish an OGD/R model, while in vivo experiments utilized male C57BL/6 mice to construct a MCAO model. Cell viability and apoptosis were assessed via the CCK-8 assay and flow cytometry, respectively. RT-qPCR measured mRNA expression of LUCAT1, miR-337-3p, and HSPB8. The molecular targeting relationship was validated using dual luciferase reporter assays and RNA pull-down experiments. ELISA was used to measure the levels of IL-6, IL-1β, and TNF-α. DCFH-DA fluorescent probes and commercial kits were employed to measure ROS levels, MDA and SOD activity. Neurological function assessment included Longa score, Bederson score, adhesive removal test, and modified neurological severity score. In both OGD/R and MCAO models, LUCAT1 expression was downregulated while miR-337-3p expression was upregulated. LUCAT1 was found to directly bind to miR-337-3p. Under OGD/R conditions, LUCAT1 overexpression enhanced cell viability, inhibited apoptosis, and alleviated inflammation and oxidative stress, with these protective effects being reversed by miR-337-3p overexpression. Animal experiments further confirmed that LUCAT1 overexpression improved neuroinflammation, oxidative stress, and neurological deficits in MCAO mice, an effect that was attenuated by co-expression of miR-337-3p. HSPB8 was identified as a direct target gene of miR-337-3p; inhibition of miR-337-3p exerted protective effects by upregulating HSPB8, whereas HSPB8 knockdown counteracted this protective effect. The long noncoding RNA LUCAT1 exerts neuroprotective effects in cerebral infarction by sponging miR-337-3p and relieving its inhibitory action on HSPB8. - Source: PubMed
Publication date: 2026/05/20
Lei LeiGuo MengnanZou Qixin - HSPB8 belongs to the small heat shock protein family, which comprises ten chaperones with molecular weights below 29 kDa. HSPB8 is broadly expressed across human tissues, with the highest levels in skeletal muscles, the cardiac muscle, and the nervous system. In muscles, HSPB8 plays a crucial role in chaperone-assisted selective autophagy (CASA), contributing to protein quality control and maintaining proteostasis. The most extensively studied mutations affecting the HSPB8 K141 codon are associated with autosomal dominant neuromuscular disorders such as Charcot-Marie-Tooth disease type 2L and distal hereditary motor neuropathy type 2 (dHMN2). Of note, recent findings have identified Myofibrillar Myopathy type 13 (MFM13) with Rimmed Vacuoles as a distinct disorder caused by frameshift (fs) mutations in the carboxy-terminus of HSPB8. This review focuses on the known HSPB8-fs mutations leading to MFM13, their associated clinical phenotypes and histological findings, and highlights the need to further understand the underlying etiologies and mechanisms. - Source: PubMed
Publication date: 2026/04/06
Zhou WenliMarchesi VeronicaMcLeod MatthewKordala Anna JolantaSzwec SylwiaMielcarz Julia AnnaPoletti AngeloTedesco Barbara - Filamin C is an adapter protein involved in the regulation of cytoskeleton; it interacts with more than 90 protein partners, including small heat shock proteins (sHsps). However, the details of filamin C interaction with sHsps remain poorly characterized. Here, we used immunochemistry methods, size-exclusion chromatography, native gel electrophoresis, and chemical crosslinking to investigate the interactions of a long C-terminal fragment of filamin C containing immunoglobulin (Ig)-like domains 19-24 (FLNC19-24) with sHsps. Out of five analyzed sHsps (HspB1, phosphorylation-mimicking 3D mutant of HspB1, HspB5, HspB6, HspB7, and HspB8), only HspB7 formed complexes with FLNC19-24. Taking into account that HspB7 interacted with the isolated Ig-like domain 24 and filamin fragments containing Ig-like domains 22-24 and 19-24, we concluded that HspB7 is a bona fide partner of filamin C. Selective binding of the α-crystallin domain of HspB7 with the Ig-like domain 24 induced dissociation of filamin dimers, which might promote filamin C translocation in the cell and facilitate the repairs of damaged contractile apparatus. - Source: PubMed
Zamotina Maria AMuranova Lidia KTyurin-Kuzmin Pyotr ASluchanko Nikolai NGusev Nikolai B - The loss of cellular proteostasis through aberrant stress granule formation is implicated in neurodegenerative diseases. Stress granules are formed by biomolecular condensation involving protein-protein and protein-RNA interactions. These assemblies are protective, but can rigidify, leading to amyloid-like fibril formation, a hallmark of the disease pathology. Key proteins dictating stress granule formation and disassembly, such as TDP43, contain low-complexity (LC) domains that drive fibril formation. HSPB8, a small heat shock protein, localizes to stress granules, has known aggregation delaying activity, and helps direct aggregated proteins to protein degradation pathways. It is not known how HSPB8 interacts with aggregation prone LC domains in stress granules. Here, we examine the interaction between isolated HSPB8 and the TDP43 LC using thioflavin T (ThT) and fluorescence polarization (FP) aggregation assays, fluorescence microscopy and photobleaching experiments, and crosslinking mass spectrometry (XL-MS). Our results indicate that HSPB8 delays TDP43 LC aggregation through domain-specific interactions with fibril nucleating species, without affecting fibril elongation rates. These findings provide mechanistic insight into how HSPB8 mediates LC domain aggregation and provides bases for investigating how the TDP43 LC subverts chaperone activity in neurodegenerative disease and comparing differing mechanisms between members of the HSPB protein family. - Source: PubMed
Publication date: 2026/02/04
Jami Khaled MCorbett Katherine EFarb Daniel COsumi Kayla MShafer Catelynn CCriscione SophieMurray Dylan T - Breast cancer (BC) is a widespread and heterogeneous disease in which autophagy plays an essential role in tumor development and progression. It has been suggested that autophagy activation may prevent tumor development in the initial stages of the disease, while in more advanced stages, autophagy might activate survival mechanisms for cancer cells. Moreover, autophagy may be involved in developing therapies resistance and in forming metastases. Some Heat Shock Proteins (HSPs) play an important role in autophagy. The small HSPB8 draws attention because it is generally highly expressed in Estrogen Receptor positive (ER+) BC and its over-expression increases autophagic flux, proliferation, migration and survival of BC cells under stress conditions. HSPB8 mediates the autophagic degradation of client proteins via the chaperone-assisted selective autophagy (CASA) complex in which it binds the BAG cochaperone 3 (BAG3), the HSP70 and the E3-ubiquitin ligase STUB1. Similarly to HSPB8, BAG3 is also highly expressed in BC cells, and its unregulated expression is linked to a poor prognosis. In our previous studies, we showed that HSPB8 and BAG3 silencing reduces proliferation and migratory capacities of hormone-sensitive MCF-7 BC cells. - Source: PubMed
Publication date: 2026/02/10
Piccolella MargheritaTedesco BarbaraFerrari VeronicaFilippone Maria GraziaTucci Francesco AntonioPandolfi AlessandroCasarotto ElenaCozzi MartaChierichetti MartaPramaggiore PaolaCornaggia LauraMilioto CarmeloMagdalena RocioMohamed AliBrodnanova MariaKoshal PrashantRusmini PaolaGalbiati MariaritaTosoni DanielaPece SalvatoreCristofani RiccardoCrippa ValeriaPoletti Angelo