943 Results for: "AbFrontier"

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Polo-like kinases (Plks) are important regulators of the cell cycle. Plk1, the most studied Plk, has been implicated in regulating centrosome maturation, mitotic entry, sister chromatid cohesion, the anaphase-promoting complex/cyclosome (APC/C), and cytokinesis. Sister chromatid separation and the subsequent formation of two genetically identical daughter cells depend on the symmetrical attachment of all chromosomes to the mitotic spindle, a process called chromosome biorientation. Several mitosis-specific protein kinases have been implicated in bipolar spindle assembly and chromosome biorientation. For example, Cdk1 (cyclin-dependent kinase 1) is known to phosphorylate Eg5, a kinesin that is required for the migration of centrosomes and is thus needed for the formation of bipolar spindles.
At the onset of mitosis, Plks contribute to the activation of Cdk1-cyclinB, and they are also required for the inactivation of Cdk1 and exit from mitosis. Plks are important regulators of the APC/C, a key component of the ubiquitin-dependent proteolytic degradation pathway.

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Complement factor C9, 71kDa, is the last of the human complement components creating the membrane attack complex (MAC). Activation of the complement system leads to the formation of the MAC, which in turn causes lysis, and death of target cells. C9 plays an important role in inflammatory reactions since it is essential for lytic action of the MAC. Such lytic action could be the basis for complement autotoxicity. Like most of the complement components, C9 belongs to the acute-phase proteins which are generally of hepatic origin, and their plasma concentrations increase (or decrease) following tissue injury and inflammation. Also, because C9 is required for the MAC of complement to become functional, interfering with signaling pathways that stimulate its production could offer new therapeutic strategies for treating various neurodegenerative disorders.

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Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx VI belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 – 30 kilodalton in molecular size and vary in subcellular localization: Prx I, II, and VI in cytosol, Prx III in mitochondria, Prx IV in ER and secretion, Prx V showing complicated distribution including peroxisome, mitochondria and cytosol.

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Ceruloplasmin, 132kDa, is a serum ferroxidase that contains greater than 95% of the copper found in plasma. This protein is a member of the multicopper oxidase family, an evolutionarily conserved group of proteins that utilize copper to couple substrate oxidation with the four-electron reduction of oxygen to water. Despite the need for copper in ceruloplasmin function, this protein plays no essential role in the transport or metabolism of this metal. Serum ceruloplasmin level is reduced in Wilson's disease, malnutrition nephrotic syndrome and increased in pregnancy, oestrogen containing contraceptives, acute infection, some types of chronic liver disease, malignancy, rheumatoid arthritis.

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Creatine kinase (CK), also known as phosphocreatine kinase or creatine phosphokinase (CPK) is an enzyme expressed by various tissue types. It catalyzes the reversible transfer of the N-phosphoryl group from phosphocreatine (PCr) to ADP to regenerate ATP. Creatine kinase plays a key role in the energy homeostasis of cells with intermittently high, fluctuating energy requirements, such as skeletal and cardiac muscle cells, neurons, photoreceptors, spermatozoa and electrocytes.
Creatine kinase consists of two subunits, which can be either B (brain type) or M (muscle type). Therefore, three different cytosolic isoenzymes exist: CK-MM, CK-BB and CK-MB. Cytosolic CK isoenzymes are always co-expressed in a tissue-specific fashion together with a mitochondrial isoform. Skeletal muscle expresses CK-MM (98%) and low levels of CK-MB (1%). The heart muscle expresses CK-MM at 70% and CK-MB at 25-30%. CK-BB is expressed in all tissues at low levels.
Cytosolic CKs, in close conjunction with Ca2+-pumps, play a crucial role for the energetics of Ca2+-homeostasis. Octameric mitochondrial Mi-CK binds and crosslinks mitochondrial membranes. The CK system is
regulated by AMP-activated protein kinase via PCr/Cr and ATP/AMP ratios.
The cardiac-specific isoenzyme of creatine kinase, CK-MB, is a biomarker for myocardial infarction along with other markers such as cardiac Troponin I and myoglobin. The introduction of immunologic mass determination of CK-MB was a major breakthrough that replaced the traditional enzymatic assay.

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Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis.
Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx VI belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 – 30 kilodalton in molecular size and vary in subcellular localization: Prx I, II, and VI in cytosol, Prx III in mitochondria, Prx IV in ER and secretion, Prx V showing complicated distribution including peroxisome, mitochondria and cytosol (1).

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CAD (caspase-activated DNase), a 40kDa nuclear protein, is primarily responsible for cell-autonomous DNA degradation during apoptosis. CAD is present in healthy cells where it is held in an inactive state through the association with its inhibitor ICAD. The ICAD protein is inactivated in apoptotic cells via caspase-3 cleavage thereby releasing CAD, which subsequently cleaves chromosomal DNA. CAD is a magnesium-dependent endonuclease specific for double stranded DNA that generates double strand breaks with 3'-hydroxyl ends. The nuclease preferentially attacks chromatin in the internucleosomal linker DNA. However, the nuclease hypersensitive sites can be detected and CAD is potentially involved in large-scale DNA fragmentation as well. CAD-mediated DNA fragmentation triggers chromatin condensation that is another hallmark of apoptosis.

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ζ-chain associated protein kinase, ZAP70, is a 70 kDa member of the Syk family kinase predominantly involved in T cell receptor (TCR) signaling. It is structurally homologous to Syk, a PTK that is involved in proximal BCR signaling. ZAP-70 is a key signaling molecule in T cell activation and also plays a role in apoptosis and cell migration.
SYK family tyrosine kinases contain a C-terminal kinase domain and tandem N-terminal SH2 domains that bind phosphorylated ITAMs (immunoreceptor tyrosine-based activation motif). Linker region that contains multiple tyrosines separates the SH2 domains from the kinase domain. Phosphorylated tyrosines act as docking sites for phospholipase Cγ1 (PLCγ1).
ZAP-70 and Syk are functionally homologous in antigen receptor signaling. Expression of ZAP-70 in Syk− B cells reconstitutes SCR function. Reconstitution requires the presence of functional Src homology 2 (SH2) and catalytic domains of ZAP-70.
Expression of ZAP-70 is an important negative prognostic factor in chronic lymphocytic leukemia (CLL) with more rapid disease progression and shorter survival.

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The mitochondrial protein Smac/DIABLO(second mitochondria-derived activator) performs a critical function in apoptosis by eliminating the inhibitory effect of IAPs (inhibitor of apoptosis proteins) on caspases. The newly synthesized Smac protein contains 239 amino acids. Its N-terminal 55 residues encode the mitochondrial-targeting sequence and are proteolytically removed in the mature Smac protein. In the intrinsic cell death pathway, the key event leading to the activation of caspases is the release of several pro-apoptotic proteins such as Smac/DIABLO from the intermembrane space of mitochondria into the cytosol. During apoptosis, Smac is released from mitochondria and re-activates the processed initiator and effector caspases by relieving IAP-mediated inhibition. Furthermore, Smac/DIABLO plays an important regulatory role in the sensitization of cancer cells to both immune-and drug-induced apoptosis.

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A growing body of evidence relates selenium to cancer prevention, immune system function, male fertility, cardiovascular disorder, control of the aging and neurodiseases process. Selenoproteins are thought to be responsible for the majority of these biomedical effects of selenium. Approximately 17 selenoproteins have been identified until now. Although the function of many selenoproteins are unknown, some play important roles in anti-oxidant mechanisms. It has been also implicated in the regulation of  signaling pathways through catalysis of thiol/ disulfide exchange.
Selenoprotein M(SelM) is especially expressed in a mammalian brain and is localized to the perinuclear structures (Golgi/ER). The roles of selM have not been clearly identified until present time.

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Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis.
Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx VI belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 – 30 kilodalton in molecular size and vary in subcellular localization: Prx I, II, and VI in cytosol, Prx III in mitochondria, Prx IV in ER and secretion, Prx V showing complicated distribution including peroxisome, mitochondria and cytosol.

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Parkinson’s disease (PD) is the second most common neurodegenerative disorder after Alzheimer’s disease, with a prevalence of 1–2% in population aged 65 years or older. PD is a complex, multifactorial disorder that typically manifests after the age of 50 years.
The pathology involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain. α-synuclein and parkin are thought to be firmly associated with PD.
The exact biological function of the DJ-1 protein is currently unknown. It may play a role in the oxidative stress response, and this function could be important in preventing the onset of PD. Defects in PARK7 are the cause of autosomal recessive early-onset Parkinson disease 7 (PARK7).
The human DJ-1 protein contains 189 amino acid residues. DJ-1 may possess an active site and could also be a protease/hydrolase similar to the PfpI proteases.
The DJ-1 gene has been highly conserved in evolution. The structures of the mouse and human DJ-1 genes are similar, and human and mouse DJ-1 proteins display 90% amino acid identity.

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p53 is a transcription factor that regulates the cell cycle and hence functions as a tumor suppressor. p53 has been described as "the guardian of the genome", referring to its role in conserving stability by preventing genome mutation. p53 has many anti-cancer mechanisms: activating DNA repair proteins when DNA has sustained damage, holding the cell cycle at the G1/S regulation point on DNA damage recognition, initiating apoptosis if the DNA damage proves to be irrepairable. Human p53 is 393 amino acids long and has three domains: N-terminal transcription-activation domain (TAD), which activates transcription factors. 2) central DNA-binding core domain (DBD) 3) C-terminal homo-oligomerisation domain (OD); tetramerization greatly increases the activity of p53 in vivo. Mutations that deactivate p53 in cancer usually occur in the DBD and most of these mutations destroy the ability of the protein to bind to its target DNA sequences.

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Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis.
Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx VI belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 – 30 kilodalton in molecular size and vary in subcellular localization: Prx I, II, and VI in cytosol, Prx III in mitochondria, Prx IV in ER and secretion, Prx V showing complicated distribution including peroxisome, mitochondria and cytosol (1).

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Ezrin, radixin and moesin (ERM) proteins are widely distributed proteins located in the cellular cortex, in microvilli and adherens junctions. They are mediate linkage of actin cytoskeleton to plasma membrane in many cells. ERM proteins contain an N-terminal FERM (4.1/ezrin/radixin/moesin)
domain that binds to phosphatidylinositol-(4,5)phosphate and cellular membrane proteins. The ERM, particularly ezrin, is important for reconstructing cell-surface architecture during T cell activation. Despite the high degree of homology, the three proteins exhibit a distinct receptor-specific pattern of phosphorylation. ERM activity is regulated in part by phosphorylation at a C-terminal threonine(ezrin-Thr567, radixin-Thr564, moesin-Thr558).

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The His tag antibody was generated by immunization with highly purified His-tagged proteins produced in E.coli. This antibody reacts with polypeptides which include a 6-His tag.

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The Ras superfamily of small GTPases includes the Ras, Rho, Arf, Rab, and Ran families. Ras-regulated signal pathways control such as actin cytoskeletal integrity, proliferation, differentiation, cell adhesion, apoptosis, and cell migration. These GTPases function as molecular switches that control eukaryotic cell function by cycling between two interconvertible forms, a GDP-bound inactive form and a GTP-bound active form. The binding of GTP leads to a conformational change in the downstream effector-binding domain of the G-protein.
The small GTPases are monomeric G-proteins with molecular masses over the range 20–30 kDa. Ras is attached to the cell membrane by prenylation.
Mutations in the Ras family of proto-oncogenes (comprising H-Ras, N-Ras and K-Ras) are very common, being found in 20% to 30% of all human tumours. The frequency of RAS mutations is among the highest for any gene in human cancer. K-ras mutations occur frequently in non-small-cell lung, colorectal, and pancreatic carcinomas; H-ras mutations are common in bladder, kidney, and thyroid carcinomas; N-ras mutations are found in melanoma, hepatocellular carcinoma, and hematologic malignancies.

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Receptor protein tyrosine phosphatase rho (RPTPρ/PTPRT) is a transmembrane protein that is highly expressed in the developing and adult central nervous system. It is a member of the RPTP R2B subfamily, which includes PTPκ, PTPμ and PCP-2. The R2B phosphatases are known to interact with members of the cadherin/catenin complex.
These four RPTPs share the same domain structure: an extracelluar domain, a juxtamembrane region, and two phosphatase domains. The extracellular domain of PTPR mediates cell-cell aggregation and that mutational inactivation of this phosphatase could promote tumor migration and metastasis. PTPRT is the most frequently mutated PTP in human cancers. STAT3 is a substrate of PTPRT. Phosphorylation of a tyrosine at 705 is essential for the function of STAT3, and PTPRT specifically dephosphorylated STAT3 at this position.

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Caspase-activated DNase (CAD) cleaves chromosomal DNA during apoptosis. Apoptosis which is a cell death process removing toxic and/or useless cells during mammalian development can be induced by a variety of stimuli, including the death factors of the tumor necrosis factor family,  or UV irradiation, anticancer drugs, and survival factor deprivation. The apoptotic process is accompanied by shrinkage and fragmentation of the cells and nuclei and degradation of the chromosomal DNA into nucleosomal units.
CAD, which can be activated by caspases, exists as a complex with its inhibitor, inhibitor of CAD (ICAD). ICAD helps correct folding of CAD and remains complexed with CAD to inhibit the DNase activity of CAD. Caspase, which is activated during the apoptotic process, cleaves ICAD, and the CAD released from ICAD enters the nuclei to cleave the chromosomal DNA. Internal as well as external signals can activate caspases and this is under the control of the balance between pro-and anti-apoptotic proteins of the Bcl-2 family, heat shock proteins, and inhibitors of apoptosis proteins (IAPs). Currently, fourteen members of the caspase family have been identified, of which seven mediate apoptosis.

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Diazepam Binding Inhibitor(DBI) is a highly conserved 10 kDa polypeptide which is expressed in various species range from yeast to mammals. As an inverse agonist for benzodiazepine receptors, DBI downregulates inhibitory effects of GABA. It also has potential to induce anxiety. Found in central and peripheral tissues, DBI also participates in metabolism of steroids, which has been known to partially modify GABAA receptor function in the CNS. In peripheral tissues, DBI plays regulatory roles in steroidogenesis. DBI levels have been reported to be decreased in the cerebrospinal fluid obtained from patients with Alzheimer disease.

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Ubiquitin(Ub) is a small protein that is composed of 76 amino acids. Ub is found only in eukaryotic organisms and is highly conserved. Ub can exist either in free form or as part of a complex with other proteins. In the latter case, Ub is attached(conjugated) to proteins through a covalent bond between the glycine at the C-terminal end of Ub and the side chains of lysine on the proteins; Ubiquitination.  Ub functions to regulate protein turnover in a cell by closely regulating the degradation of specific proteins. Ubiquitin has been immunohistochemically localized to a number of pathological inclusions, including ; Lewy bodies of Parkinson’s disease,neurofibrillary of Alzheimer’s disease, Pick bodies of Pick’s disease.

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The mammalian thioredoxin reductases (TrxRs) are a family of selenocysteine-containing pyridine nucleotide-disulfide oxidoreductases. All the mammalian TrxRs are homologous to glutathione reductase with respect to primary structure including the conserved redox catalytic site (-Cys-Val-Asn-Val-Gly-Cys-) but distinctively with a C-terminal extension containing a catalytically active penultimate selenocysteine (SeCys) residue in the conserved sequence(-Gly-Cys-SeCys-Gly). TrxR is homodimeric protein in which each monomer includes an FAD prosthetic group, a NADPH binding site and a redox catalytic site. Electrons are transferred from NADPH via FAD and the active-site disulfide to C-terminal SeCys-containing redox center, which then reduces the substrate like thioredoxin. The members of TrxR family are 55 - 58 kilodalton in molecular size and composed of three isoforms including cytosolic TrxR1, mitochondrial TrxR2, and TrxR3, known as Trx and GSSG reductase (TGR). TrxR plays a key role in protection of cells against oxidative stress and redox-regulatory mechanism of transcription factors and various biological phenomena (1).

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Glutamine Synthetase(GS) catalyzes the conversion of ammonia and glutamate to glutamine. This reaction consumes a molecule of ATP:
Glutamate + NH4+ + ATP
 Glutamine + ADP + Pi
GS is found in astrocytes as an octamer of identical 45kDa subunits. Most well known function of GS is the detoxification of brain ammonia. It also has an important role in controlling metabolic regulations of neurotransmitter glutamate. Because of the multiple functions and importance of GS in cellular metabolism, both catalytic activities and synthesis are highly regulated. The activity of GS is controlled by adenylylation. Its activity is decreased in the cerebral cortex of brains affected by Alzheimer’s disease, particularly in the vicinity of senile plaques. It is also decreased under conditions of glucose deprivation. On the other hands, the level of expression of GS is increased during ischemia in vivo or hypoxia in culture.

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Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis. Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx VI belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 – 30 kilodalton in molecular size and vary in subcellular localization: Prx I, II, and VI in cytosol, Prx III in mitochondria, Prx IV in ER and secretion, Prx V showing complicated distribution including peroxisome, mitochondria and cytosol.

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Check point kinase 1 (Chk1) is a serine / threonine protein kinase and a key mediator in the DNA damage-induced checkpoint network. Chk1 is an evolutionarily conserved protein kinase that functions to ensure genomic integrity upon genotoxic stress. When the G2 or S checkpoint is abrogated
by the inhibition of Chk1, p53-deficient cancer cells undergo mitotic catastrophe and eventually apoptosis, whereas normal cells are still arrested in the G1 phase. Thus, Chk1 inhibitors can preferentially
potentiate the efficacy of DNA damaging agents in cancer cells, and Chk1 is an attractive therapeutic target for cancer treatment, especially since approximately 50% of all human cancers are p53-deficient.

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Plasminogen, a 92kDa glycoprotein, is produced by the liver and is present in plasma and extracellular fluids. Plasminogen is the inactive precursor of plasmin, a potent serine protease involved in the dissolution of fibrin blood clots. Plasminogen can be converted into the active plasmin by plasminogen activators urokinase (uPA), tissue plasminogen activator (tPA), factor XII-dependent components. The plasmin system has been implicated in a variety of physiological and pathological processes such as fibrinolysis, tissue remodeling, cell migration, inflammation, and tumor invasion and metastasis. Hereditary defects of plasminogen is a predisposing risk factor for thromboembolic disease.

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ubiquitously expressed proteins which catalyze the reduction of hydrogen peroxides and organic hydroperoxides by glutathione. There are several isoforms which differ in their primary structure and localization. The classical cytosolic/mitochondrial GPx1 (cGPx) is a selenium-dependent enzyme, first of the GPx family to be discovered. GPx2, also known as gastrointestinal GPx (GI-GPx), is an intracellular enzyme expressed only at the epithelium of the gastrointestinal tract (1). Extracellular plasma GPx (pGPx or GPx3) is mainly expressed by the kidney from where it is released into the blood circulation (2). Phospholipid hydroperoxide GPx4 (PH-GPx) expressed in most tissues, can reduce many hydroperoxides including hydroperoxides integrated in membranes, hydroperoxy lipids in low density lipoprotein or thymine (3). All mammalian GPx family members, except for the recently described Cys containing GPx3 and epididymis-specific secretory GPx (eGPx or GPx5) isoforms, possess selenocysteine at the active site (4-5).

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Enolase (2-phosphogly-cerate hydrolyase or phosphopyruvate hydrates) is a glycolytic enzyme that catalyzes the dehydration and conversion of 2-phosphoglycerate to phosphoenolpyruvate. It comprises three distinct subunits, alpha, beta and gamma. Non Neuronal Enolase(ENO1) is an isoform of mammalian enolase and is composed of 2 alpha subunits. The gene for ENO1 also encodes a shorter monomeric structural lens protein, tau-crystallin.
Multifunctional enzyme that, as well as its role in glycolysis, plays a part in various processes such as growth control, hypoxia tolerance and allergic responses. May also function in the intravascular and pericellular fibrinolytic system due to its ability to serve as a receptor and activator of plasminogen on the cell surface of several cell-types such as leukocytes and neurons. Stimulates immunoglobulin production.
Used as a diagnostic marker for many tumors and, in the heterodimeric form, alpha/gamma, as a marker for hypoxic brain injury after cardiac arrest. Also marker for endometriosis. Antibodies against alpha-enolase are present in sera from patients with cancer-associated retinopathy syndrome (CAR), a progressive blinding disease which occurs in the presence of systemic tumor growth, primarily small-cell carcinoma of the lung and other malignancies. Is identified as an autoantigen in Hashimoto encephalopathy (HE) a rare autoimmune disease associated with Hashimoto thyroiditis (HT). HT is a disorder in which destructive processes overcome the potential capacity of thyroid replacement leading to hypothyroidism

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p38 MAPK cascade regulates a variety of cellular responses to stress, inflammation and other signals. p38 MAPK is relatively inactive in the non-phosphorylated form and becomes rapidly activated by dual phosphorylation of a Thr-Gly-Tyr motifs. There are four isoforms of p38 MAPK, , ,  and , which differ in their tissue expression and affinity for upstream activators and downstream effectors.
When cells are exposed to tumor necrosis factor-, interleukin-1, heat shock, or other activating stimuli, activation of MAPK kinase-3 and –6 occurs by phosphorylation. Activated MAPK kinase-3/6 phosphorylate each residue of Thr180 and Tyr182 in p38 MAPK. Phospho-p38 MAPK activates ATF-2, CHOP-1, MEF-2 and other transcription factors through phosphorylation.

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IκBα is the major IκB protein member of IκB family that function to inhibit the NF-κB transcription factor. IκBs have an N-terminal regulatory domain, followed by six or more ankyrin repeats and a PEST domain near their C terminus. IκBα inhibits NF-κB by masking the nuclear localization signals (NLS) of NF-κB proteins and keeping them in an inactive state in the cytoplasm. In addition, IκBα blocks the ability of NF-κB transcription factors to bind to DNA, which is required for NF-κB's proper functioning.
Upon stimulation by the proinflammatory cytokine tumor necrosis factor (TNF), signaling pathways lead to activation of the subunit of the IκB kinase (IKK) complex, which then phosphorylates IκB proteins on two N-terminal serine residues. The IKK is an unusual kinase in that it contains two related kinases, IKKα and IKKβ, and a regulatory subunit, NEMO (NF-κB essential modifier). The primary role of NF-κB is to maintain normal cellular functions that range from cell-to-cell communication to cell motility, cell cycle progression, and cell lineage development.