heat

The biological activity of the toxin is produced by the A chain, which activates intracellular adenyl cyclase. Heat-labile enterotoxin B chain Protein, E. coli, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 19.2 kDa and the accession number is P32890.

The biological activity of the toxin is produced by the A chain, which activates intracellular adenyl cyclase.

The biological activity of the toxin is produced by the A chain, which activates intracellular adenyl cyclase.

Toxin which activates the particulate form of guanylate cyclase and increases cyclic GMP levels within the host intestinal epithelial cells. Heat-stable enterotoxin ST-2 Protein, E. coli, Recombinant is expressed in E. coli expression system. The predicted molecular weight is 2.0 kDa and the accession number is P01560.

Toxin which activates the particulate form of guanylate cyclase and increases cyclic GMP levels within the host intestinal epithelial cells.

Toxin which activates the particulate form of guanylate cyclase and increases cyclic GMP levels within the host intestinal epithelial cells.

HEATR6 Protein, Human, Recombinant (His & Myc) is expressed in E. coli.

GUCY2C Protein, Human, Recombinant (hFc) is expressed in HEK293 mammalian cells with C-Fc tag. The predicted molecular weight is 90-120 KDa and the accession number is P25092.

α Crystallin B Chain (CRYAB) is a cytoplasmic protein that belongs to the small heat shock protein (HSP20) family. Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20) family. Alpha crystallins acts as molecular chaperones and hold them in in large soluble aggregates. CRYAB is expressed widely in many tissues and organs. It may contribute to the transparency and refractive index of the lens. The deficiency of CRYAB is the cause of myopathy myofibrillar type 2 (MFM2) and cataract posterior polar type 2 (CTPP2).

Heat Shock Factor Protein 2 (HSF2) belongs to the HSF family of transcription factors that bind specifically to the heat-shock promoter element and activate transcription. In higher eukaryotes, HSF is unable to bind to the HSE unless the cells are heat shocked. HSF2 is widely expressed in many cells and tissues. HSF2 is located on Cytoplasmic during normal growth. But when it is activited, HSF2 moves to the nucleus.

Serpin H1 is a serine proteinase inhibitors Which belongs to the serpin family. Serpin H1 is induced by heat shock. Serpin H1 localizes to the endoplasmic reticulum lumen and binds specifically to collagen. Thus it is thought to be a molecular chaperone involved in the maturation of collagen molecules. Autoantibodies to this protein have been found in patients with rheumatoid arthritis. Serpin H1 may be a marker for cancer and nucleotide polymorphisms in this gene may be associated with preterm birth caused by preterm premature rupture of membranes.

Heat Shock Protein β-11 (HSPB11) is a stress-responsive protein that is required to deal with proteotoxic stresses. HSPB11 is composed of an IFT complex B composed of IFT88, IFT57, TRAF3IP1, IFT52, IFT27, HSPB11 and IFT20 and is detected in placenta. HSPB11 has beeb shown to form oligomeric complexes and prevent the aggregation of in vitro denaturated aldolase and glyceraldehyde-3-phosphate dehydrogenase in accordance with the chaperone model of HSPB1 and HSPB5. HSPB11 overexpression protected against etoposide-induced cell death that correlated with a decreased release of mitochondrial Cytochrome C into the cytosol. Inhibition of HSP90 function completely abrogated the protective effect of HSPB11. This data suggests that at least in the case of HSPB11, interaction with other chaperone machines besides HSPA1A may contribute to functional specificity and cellular functioning.

Chaperone protein required for seedling and chloroplast development under heat stress, probably by maintaining plastid-encoded RNA polymerase (PEP)-dependent transcription. HSP21, chloroplastic Protein, Arabidopsis thaliana, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 28.4 kDa and the accession number is P31170.

Molecular chaperone. Has ATPase activity. HtpG Protein, Bacteroides fragilis, Recombinant (His & Myc & SUMO) is expressed in E. coli expression system with N-10xHis-SUMO and C-Myc tag. The predicted molecular weight is 57.0 kDa and the accession number is Q5LCH4.

Acts as a chaperone.

Chaperone that expresses an ATPase activity. Involved in maintaining mitochondrial function and polarization, downstream of PINK1 and mitochondrial complex I. Is a negative regulator of mitochondrial respiration able to modulate the balance between oxidative phosphorylation and aerobic glycolysis. The impact of TRAP1 on mitochondrial respiration is probably mediated by modulation of mitochondrial SRC and inhibition of SDHA. TRAP1 Protein, Human, Recombinant (GST) is expressed in E. coli expression system with N-GST tag. The predicted molecular weight is 54.5 kDa and the accession number is Q12931.

N/A. HSP18.1 Protein, Pisum sativum, Recombinant (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 34.1 kDa and the accession number is P19243.

HSP90AA1 Protein, Pig, Recombinant (His) is expressed in Baculovirus insect cells with N-6xHis tag. The predicted molecular weight is 19.7 kDa and the accession number is O02705.

Toxin which activates the particulate form of guanylate cyclase and increases cyclic GMP levels within the host intestinal epithelial cells. Could play an important role in pathogenesis.

N/A. HSP100 Protein, Trypanosoma cruzi, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 22.9 kDa and the accession number is O15885.

GUCY2C Protein, Human, Recombinant (His & Avi), Biotinylated is expressed in HEK293 mammalian cells with C-6xHis-Avi tag. The predicted molecular weight is 65-110 KDa and the accession number is P25092.

Human PAP, also known as 28 kDa heat- and acid-stable phosphoprotein, PDGF-associated protein, PDGFA-associated protein 1, PDAP1, HASPP28, is a protein which belongs to the PDAP1 family. The encoded protein in rodents has been shown to bind PDGFA with a low affinity. PDGF-Associated Protein (PAP) is a phosphoprotein that may enhance PDGFA-stimulated cell growth in fibroblasts, but inhibits the mitogenic effect of PDGFB. PDAP1 expression is induced by TNF-alpha, and cells overexpressing PDAP1 show significantly less apoptosis on exposure to TNF-alpha.

Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is involved in regulation of expression of heat shock genes. Intracellular concentration of free RpoH protein increases in response to heat shock, which causes association with RNA polymerase (RNAP) and initiation of transcription of heat shock genes, including numerous global transcriptional regulators and genes involved in maintaining membrane functionality and homeostasis. RpoH is then quickly degraded, leading to a decrease in the rate of synthesis of heat shock proteins and shut-off of the heat shock response.

HSPA8 Protein, Human, Recombinant (His) is expressed in Yeast.

Molecular chaperone. Has ATPase activity.

A DNA-binding protein implicated in transcriptional repression (silencing). Also involved in bacterial chromosome organization and compaction. H-NS binds tightly to AT-rich dsDNA and inhibits transcription. Binds upstream and downstream of initiating RNA polymerase, trapping it in a loop and preventing transcription. Binds to hundreds of sites, approximately half its binding sites are in non-coding DNA, which only accounts for about 10% of the genome. Many of these loci were horizontally transferred (HTG); this offers the selective advantage of silencing foreign DNA while keeping it in the genome in case of need. Suppresses transcription at many intragenic sites as well as transcription of spurious, non-coding RNAs genome-wide. Repression of HTG by H-NS is thought to allow their DNA to evolve faster than non-H-NS-bound regions, and facilitates integration of HTG into transcriptional regulatory networks. A subset of H-NS/StpA-regulated genes also require Hha (and/or Cnu, ydgT) for repression; Hha and Cnu increase the number of genes DNA bound by H-NS/StpA and may also modulate the oligomerization of the H-NS/StpA-complex. The protein forms 2 clusters in the nucleoid which gather hns-bound loci together, bridging non-contiguous DNA, and causes DNA substantial condensation. Binds DNA better at low temperatures than at 37 degrees Celsius; AT-rich sites nucleate H-NS binding, further DNA-binding is cooperative and this cooperativity decreases with rising temperature. Transcriptional repression can be inhibited by dominant-negative mutants of StpA or itself. May effect transcriptional elongation. Can increase translational efficiency of mRNA with suboptimal Shine-Dalgarno sequences. Plays a role in the thermal control of pili and adhesive curli fimbriae production, by inducing transcription of csgD. Plays a role in flagellar function. Represses the CRISPR-cas promoters, permits only weak transcription of the crRNA precursor; its repression is antagonized by LeuO. Binds preferentially to the upstream region of its own gene recognizing two segments of DNA on both sides of a bend centered around -150. Overexpression suppresses secY24, a temperature-sensitive mutation. Has also been reported to activate transcription of some genes.

Acts as a co-chaperone of HSP90AA1. Activates the ATPase activity of HSP90AA1 leading to increase in its chaperone activity. Competes with the inhibitory co-chaperone FNIP1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins. Competes with the inhibitory co-chaperone TSC1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins. AHSA1 Protein, Human, Recombinant (GST) is expressed in E. coli expression system with N-GST tag. The predicted molecular weight is 65.3 kDa and the accession number is O95433.

N/A. HSP70 Protein, Toxoplasma gondii, Recombinant (His) is expressed in E. coli expression system with N-10xHis tag. The predicted molecular weight is 78.9 kDa and the accession number is A0A125YXI9.

HSP60 Protein, Mouse, Recombinant (His) is expressed in E. coli expression system with His tag. The predicted molecular weight is 62.3 kDa and the accession number is P63038-1.

HSP70 Protein, Human, Recombinant (His) is expressed in Baculovirus insect cells with His tag. The predicted molecular weight is 72.2 kDa and the accession number is A8K5I0.

Cpn10/HSPE1 Protein, Human, Recombinant (His) is expressed in E. coli expression system with His tag. The predicted molecular weight is 13.2 kDa and the accession number is A0A384N6A4.

HSP70 Protein, Rat, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 71.6 kDa and the accession number is A6KTP2.

DnaJ Homolog Subfamily B Member 1 (DNAJB1) is a member of the heat shock protein family. Heat shock proteins (HSPs) are a highly conserved family of stress response proteins. HSPs function primarily as molecular chaperones, facilitating the folding of other cellular proteins, preventing protein aggregation, or targeting improperly folded proteins to specific degradative pathways. DNAJB1 regulates cellular processes by aiding in the folding, transport and assembly. DNAJB1 contains a J-domain which controls interaction with the ATPase domain of DnaK. DNAJB1 interacts with HSP70 and can stimulate its ATPase activity. In addition, DNAJB1 stimulates the association between HSC70 and HIP.

HSP70 Protein, Chicken, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 48.6 kDa and the accession number is P08106.

DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. Degrades transiently denatured and unfolded or misfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. Its proteolytic activity is essential for the survival of cells at elevated temperatures. It can degrade IciA, Ada, casein, globin and PapA. DegP shares specificity with DegQ. DegP is also involved in the biogenesis of partially folded outer-membrane proteins (OMP).

HSP70 Protein, Gallus gallus, Recombinant (His & Myc) is expressed in Baculovirus insect cells with N-10xHis and C-Myc tag. The predicted molecular weight is 46.5 kDa and the accession number is P08106.

HSP90AA1 Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 36.0 kDa and the accession number is P07900.

HSP90AB1 Protein, Human, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 88.1 kDa and the accession number is P08238.

Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate. Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to disrupt the dimerization of ERN1/IRE1, thereby inactivating ERN1/IRE1. Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP from ERN1/IRE1, allowing homodimerization and subsequent activation of ERN1/IRE1. Plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). May function as an allosteric modulator for SEC61 channel-forming translocon complex, likely cooperating with SEC62 to enable the productive insertion of these precursors into SEC61 channel. Appears to specifically regulate translocation of precursors having inhibitory residues in their mature region that weaken channel gating. May also play a role in apoptosis and cell proliferation.

HSP90 alpha Protein, Human, Recombinant (His) is expressed in Baculovirus insect cells with His tag. The predicted molecular weight is 87.06 kDa and the accession number is NP_005339.3.

HSP90 alpha Protein, Mouse, Recombinant (His) is expressed in Baculovirus insect cells with His tag. The predicted molecular weight is 87.19 kDa and the accession number is NP_032328.2.

Heat-Responsive Protein 12 (HRSP12) is an endoribonuclease that belongs to the Rut family. HRSP12 is found mainly in the human adult kidney and liver and is responsible for inhibiting protein translation by cleaving mRNA. HRSP12 only cleaves phosphodiester bonds in single-stranded RNA and inhibits cell-free protein synthesis. The levels of both mRNA and protein are markedly reduced in heptatocellular tumors and in human hepatoma cell lines compared with normal liver tissues. Moreover the levels of HRSP12 are different depending on the grade of the tumor. This had led to the suggestion that HRSP12 may be an important biomarker for heptatic carcinoma.

Heat shock protein beta-8 (HSPB8) belongs to the small heat shock protein (HSP20) family. This protein can be inducted by 17-beta-estradiol, and is predominantly expressed in skeletal muscle and heat, mainly located in the cytoplasm and nucleus. HSPB8 usually exists in monomer, it can interact with HSPB1 and DNAJB6. HSPB8 displays temperature-dependent chaperone activity，appears to be involved in regulation of cell proliferation, apoptosis, and carcinogenesis, and mutations in this gene have been associated with different neuromuscular diseases, including Charcot-Marie-Tooth disease.

Cornulin is a member of the fused gene family of molecular chaperones. Human Cornulin contains N-terminus EF-hand domains and Ca2+ binding domains, and two glutamine- and threonine-rich 60 amino acid repeats in its C-terminus. Cornulin involves in the mucosal/epithelial immune response and epidermal differentiation. Cornulin is a survival factor that participates in the clonogenicity of squamous esophageal epithelium cell lines, attenuates deoxycholic acid (DCA)-induced apoptotic cell death and release of calcium. When Cornulin is overexpressed in oral squamous carcinoma cell lines, it regulates negatively cell proliferation by the induction of G1 arrest.

AtHsp23.6 Protein, Arabidopsis thaliana, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 24.4 kDa and the accession number is Q96331.

HSP 90-alpha 1 Protein, Danio rerio, Recombinant (His & Myc) is expressed in Baculovirus insect cells with N-10xHis and C-Myc tag. The predicted molecular weight is 27.9 kDa and the accession number is Q90474.

HSPA5 Protein, Mouse, Recombinant (His) is expressed in yeast with N-6xHis tag. The predicted molecular weight is 72.5 kDa and the accession number is P20029.

Associates with aggregated proteins, together with IbpB, to stabilize and protect them from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-dependent chaperone systems ClpB and DnaK/DnaJ/GrpE. Its activity is ATP-independent.

HSP90 alpha Protein, Human, Recombinant is expressed in E. coli expression system. The predicted molecular weight is 22.6 kDa and the accession number is K9JA46.

Heat shock factor protein 1, also known as heat shock transcription factor 1, HSF1, and HSTF1, is a cytoplasm and nucleus protein that belongs to the HSF family. HSF1 is the major transcription factor of HSPs (heat shock proteins) in response to various stresses. Wild type HSF1 (heat shock transcriptional factor 1) is normally inactive. HSF1 / HSTF1 is a DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. In higher eukaryotes, HSF is unable to bind to the HSE unless the cells are heat shocked. HSF1 / HSTF1 protects cells and organisms against various types of stress, either by triggering a complex response that promotes cell survival or by triggering cell death when stress-induced alterations cannot be rescued. HSF1 / HSTF1 is the key protein in regulating the stress response. It can be activated under heat, oxidative, or other stress conditions. Dominant-positive and dominant-negative HSF1 are two types of HSF1 mutants. Both of them gain DNA binding activity in the absence of stress. Also, dominant-positive HSF1 acquires transcriptional activity, which dominant-negative HSF1 does not acquire. HSF1 / HSTF1 was also reported to contribute to cell resistance against genotoxic stress, such as that caused by doxorubicin, an anticancer drug in common clinical use.