Recombinant Human HspB2 Protein (C-6His)

Name: Recombinant Human HspB2 Protein (C-6His)
Brand: Beta LifeScience
SKU: BL-0889NP
Availability: InStock

BL-0889NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Human Heat Shock Protein Beta-2 is produced by our E.coli expression system and the target gene encoding Met1-Pro182 is expressed with a 6His tag at the C-terminus.
Accession	Q16082
Synonym	Heat shock protein beta-2;HspB2;DMPK-binding protein;MKBP;
Gene Background	Heat shock protein beta-2(HSPB2) is a protein that in humans is encoded by the HSPB2 gene. HSPB2 belongs to the superfamily of small heat-shock proteins containing a conservative alpha-crystallin domain at the C-terminal part of the molecule. It is expressed preferentially in the heart and skeletal muscle. HSPB2 has been shown to interact with TRAF6, HSPB8, Myotonic dystrophy protein kinase and CRYAB. HSPB2 regulates Myotonic Dystrophy Protein Kinase, which plays an important role in maintenance of muscle structure and function.
Molecular Mass	21.3 KDa
Apmol Mass	22-25 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of 10mM Tris-HCl, 150mM NaCl, 1mM EDTA, pH 8.0.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution	Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	May regulate the kinase DMPK.
Subcellular Location	Cytoplasm. Nucleus. Note=Localizes to nuclear foci.
Protein Families	Small heat shock protein (HSP20) family
Database References	HGNC: 5247 OMIM: 602179 KEGG: hsa:3316 STRING: 9606.ENSP00000457706 UniGene: Hs.709660
Tissue Specificity	Expressed preferentially in skeletal muscle and heart but not in the lens.

Gene Functions References

in differentiating myoblasts, nuclear HSPB2 compartments sequester lamin A. PMID: 28854361
HSPB2 competes with HSPB8 for binding to BAG3. In contrast, HSPB3 negatively regulates HSPB2 association with BAG3. PMID: 28181153
HspB2 has roles in maintaining ATP levels and as well as chaperone-dependent functions for metabolic homeostasis PMID: 26465331
Results suggest a limited function of alphaB-crystallin and HSP27 in preventing abnormal tau protein deposition in glial cells and neurons; in addition, the expression of alphaB-crystallin phosphorylated at Ser59 may act as a protective factor in glial cells. PMID: 24985029
These findings provide novel insights into the role of p53 as a regulator of bidirectional gene pair HspB2/alpha B-crystallin-mediated ROS and the Warburg effect PMID: 24859470
Study shows that HspB2 oligomers exchange subunits. PMID: 22272249
promoter methylation of heat shock protein B2 is a novel molecular biomarker in human esophageal squamous cell carcinoma PMID: 21258768
Reveal a novel function of HspB2 as an anti-apoptotic protein that negatively regulates apical caspase 3/8 activation in the extrinsic apoptotic pathway. PMID: 20087649
Hsp27, but not the classic Hsp60 and Hsp70, may be associated with the development bronchiolitis obliterans syndrome. PMID: 20456980
Sodium salicylate can induce the expression of HSP27 in human lens epithelial cells. PMID: 19513626
analysis of CEA-, Her2/neu-, BCRP- and Hsp27-positive microparticles in breast cancer patients PMID: 20592365
HSP27 is linked to multi-drug resistance in cell line HepG2/VCR. PMID: 17524270
The abnormal expression of 14-3-3 sigma and HSP27 is significantly associated with lymph node metastasis in colorectal cancer. PMID: 20336542
5-fluorouracil & carboplatin specifically induce expression of Hsp27 in hepatoma cells. siRNA knockdown of Hsp27 diminishes survival of drug-exposed cells. PMID: 19901540
HSP27 confers reresistance to androgen ablation and chemotherapy in prostate cancer cells through eIF4E PMID: 20101233
PM induces ROS generation in human lung endothelium, resulting in oxidative stress-mediated EC barrier disruption via p38 MAPK- and HSP27-dependent pathways. PMID: 19520919
study indicate that monocytes do not trigger apoptosis of vascular endothelial cells; proapoptotic activation mediated by PUMA seemed to be counterbalanced by significant increase of antiapoptotic HSP70, HSP27 and especially phospho-HSP27 proteins level PMID: 20065497
HSP27 and p53 protein levels play a key role(s) in heat shock-mediated switch of glucose depreivation-induced necrosis to apoptosis. PMID: 20043073
Small interfering RNA-mediated silencing of heat shock protein 27 (HSP27) Increases chemosensitivity to paclitaxel by increasing production of reactive oxygen species in ovarian cancer. PMID: 19930842
HSP27 and alphaB-crystallin are increased, phosphorylated and localized in aggresomes when proteasome activity is inhibited PMID: 11926998
HSP27 nuclear staining can serve as a sensitive marker for skin irritation or cellular stress in excised skin PMID: 12473058
HSP72 biosynthesis was analyzed by an image processing, computer-assisted imaging method in an endothelial vascular cell line and compared to a hand-calculated method. No differences were seen. PMID: 12503731
Hsp27 regulates apoptosis through an ability to interact with key components of the apoptotic signalling pathway [review] PMID: 12510153
hsp72 reduces caspase-3-mediated proteolysis of FAK, an anti-apoptotic protein PMID: 12611892
Hsp27 plays a significant role in the IFN-gamma-induced sensitization of oral SCC cells to anticancer drugs PMID: 12700631
Data show that heat shock protein 72 suppressed extracellular signal-regulated kinase activation by protecting dual-specificity phosphatases and suppressing MEK1/2. PMID: 12748284
Associates with the I kappa B kinase complex regulates tumor necrosis factor alpha-induced NF-kappa B activation. PMID: 12829720
down regulation in neuronal and non-neuronal cells expressing mutant ataxin-3 PMID: 12832059
HSP27 is a ubiquitin-binding protein involved in I-kappaBalpha proteasomal degradation PMID: 12897149
Phosphorylated HSP27 favors reduced bead motions that are probably due to stabilization of the actin cytoskeleton. PMID: 14729728
HSP27 may provide a neuroprotective effect in AD and other tauopathies PMID: 14963027
positive effect of Id-1 on TGF-beta1-induced cell motility was mediated through activation of MEK-ERK signaling pathway and subsequent phosphorylation of HSP27 PMID: 17916352
a cellular defense against dysregulated proteins, in the form of Hsp27 and alphaB-crystallin, might contribute to the cell cycle reentry seen in AD cells. PMID: 18061943
These data show that Hsp27 antagonizes Bax-mediated mitochondrial injury and apoptosis by promoting Akt activation via a PI3-kinase-dependent mechanism. PMID: 18299320
Upon heating at 43 degrees C, Hsp27 effectively suppresses myosin subfragment 1 aggregation, and this effect is enhanced by mutations mimicking Hsp27 phosphorylation. PMID: 18387368
In a large cohort of type 1 diabetic subjects, we found an independent association between serum HSP27 and distal symmetrical polyneuropathy. PMID: 18390793
These findings identify a novel pathway for vascular endothelial growth factor-induced HSP27 serine 82 phosphorylation via PKC-mediated PKD activation and direct phosphorylation of HSP27 by PKD. PMID: 18440775
HSP27 phosphorylation is correlated with ADP-induced platelet granule secretion. PMID: 18471985
annexin II is a novel HSP27-interacted protein which is involved in UVC resistance in human cells PMID: 18494762
Mechanistic in vitro studies showed upregulated HSP27 expression and secretion in human macrophages treated with estrogen or acLDL. PMID: 18566345
In conclusion, despite the protective action against acute motor neuron injury, Hsp27 alone is not sufficient to protect against the chronic motor neuron injury due to the presence of mutant SOD1. PMID: 18624915
Pint mutations in patients with type 2 diabetes and their families were studied. mitochondrial genes including np3316, np3394 and np3426 in the ND1 region and np3243 in the tRNA(Leu(UUR))were screened. PMID: 18701018
Overexpression of HSP27 in squamous cell carcinoma of the uterine cervix: a proteomic analysis using archival formalin-fixed, paraffin-embedded issues is reported. PMID: 18755499
HSP27 and HSP60 are predictors of biochemical recurrence of prostate cancer after radical prostatectomy. PMID: 19132982
show that Hsp27 and actin are in the same complex in cells and that Hsp27 is important for cell motility. PMID: 19224398
the differential expression patterns of alphaB-crystallin and Hsp27 indicate functional differences between these highly related proteins in placental tissues. PMID: 19238749
data show islet protection in mice by human HSP27 by mitigation of apoptosis, possibly through nuclear factor kappaB regulation. PMID: 19325007
Findings revealed a possible effect of HSP27 on apoptosis in metastatic HCC cells, in which HSP27 may regulate NF-kB pathway activation. PMID: 19331697
findings provide the first evidence that expanded ataxin-3 interferes with Hsp27 synthesis, which may contribute to the impairment of the cells' ability to respond to stresses and trigger the progression of Machado-Joseph disease PMID: 19429074
Overexpression of huHSP27 protects against hepatic injury and acute kidney injury associated with liver ischemia-reperfusion injury in mice. PMID: 19656912

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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