Recombinant Human Heat Shock Protein Beta-2 (HSPB2) Protein (GST)

Name: Recombinant Human Heat Shock Protein Beta-2 (HSPB2) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-08885P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Heat Shock Protein Beta-2 (HSPB2) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q16082
Target Symbol	HSPB2
Synonyms	DMPK-binding protein; Heat shock 27kD protein 2; Heat shock 27kDa protein 2; Heat shock protein beta-2; Heat-shock protein beta-2; Hs.78846; HSP27; HspB2; HSPB2_HUMAN; LOH11CR1K; MGC133245; MKBP
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MSGRSVPHAHPATAEYEFANPSRLGEQRFGEGLLPEEILTPTLYHGYYVRPRAAPAGEGSRAGASELRLSEGKFQAFLDVSHFTPDEVTVRTVDNLLEVSARHPQRLDRHGFVSREFCRTYVLPADVDPWRVRAALSHDGILNLEAPRGGRHLDTEVNEVYISLLPAPPDPEEEEEAAIVEP
Expression Range	1-182aa
Protein Length	Full Length
Mol. Weight	47.2kDa
Research Area	Signal Transduction
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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: 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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.