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Artikel-Nr: (ABFRLF-MA0311)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-MA0311

Beschreibung: 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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Artikel-Nr: (ABFRLF-MA0191)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-MA0191

Beschreibung: Btk (Bruton's tyrosine kinase) is a member of the Tec family of protein tyrosine kinases (PTKs) and plays a modulatory role in many cellular processes, such as proliferation, development, differentiation, survival, and apoptosis. The Tec kinases are the second largest family of non-receptor tyrosine kinases and include Tec, Btk, Bmx, Itk, and TXK/Rlk. Mutations of Btk gene cause a primary immunodeficiency disease in humans, X-linked aγglobulinemia (XLA) which is characterized by a lack of circulating B lymphocytes and an absence of immunoglobulins as a result of defects in B cell maturation and function. Btk is found in all hematopoietic cells, with the exception of T lymphocytes and plasma cells. Btk contains amino-terminal PH (pleckstrin homology) domain which binds phosphatidylinositol (3,4,5)-trisphosphate (PIP3) helping membrane translocation upon PI3 kinase activation. The Tec kinases have similar structure of N-terminal PH domains followed by Tec homology (TH), Src homology 3 (SH3), Src homology 2 (SH2), and kinase domains. Autophosphorylation of Tyr223 in SH3 domain is necessary for full activation of Btk. Various binding proteins have been reported to interact with different domains of Btk.

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Artikel-Nr: (ABFRLF-MA0195)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-MA0195

Beschreibung: PRAK is a 471 amino acid protein with 20-30% sequence identity to the known MAP kinase-regulated protein kinases RSK1/2/3, MNK1/2 and MAPKAPK2/3.
The p38 mitogen-activated protein kinase (MAPK) pathway plays an important role in cellular responses to inflammatory stimuli and environmental stress. There are at least six protein kinases that can be regulated by p38α and/or p38β. These downstream kinases of p38s include MAPK-activated protein kinase 2 (MAPKAPK2 or MK2), MAPKAPK3, MAPK-interacting kinase 1 (MNK1), MNK2, p38-activated/regulated protein kinase (PRAK or MAPKAPK5), and mitogen- and stress-activated protein kinase (MSK). PRAK can be activated in response to cellular stress and proinflammatory cytokines. T182 within the activation loop of PRAK has been determined to be the regulatory phosphorylation site. PRAK has been reoprted to be essential for ras-induced senescence and tumor suppression. PRAK mediates senescence upon activation by p38 in response to oncogenic ras.

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Artikel-Nr: (ABFRLF-MA0202)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-MA0202

Beschreibung: The members of the Src-family kinases are Src, Lyn, Fyn, Yes, Hck, Lck, Fgr, Blk, and Yrk. Each of these have a common structure consisting of an unique domain at the N-terminal, followed by SH3, SH2 and tyrosine kinase domains.
In immume cells, the Src-family kinases play roles as critical regulators of a large number of intracellular signaling pathways, including integrin signaling pathway. Integrins are major cellular receptor that mediate cell to cell and cell to substratum interactions.
Src is expressed ubiquitously, however the expression level is higher in brain, osteoclasts, and platelets. Src plays a role in cell adhesion, cell morphology and motility, and bone resorption.
Src contains a 14-carbon myristoyl group attached to an SH4 domain, a unique domain, an SH3 domain, an SH2 domain, an SH2-kinase linker, a protein–tyrosine kinase domain (the SH1 domain), and a C-terminal regulatory segment.
One of the two most important regulatory phosphorylation sites in Src is Tyr527. Under basal conditions in vivo, 90–95% of Src is phosphorylated at Tyr527, and phosphotyrosine 527 binds intramolecularly with the Src SH2 domain. Tyrosine 416 is present in the activation loop and its phosphorylation promotes kinase activity.

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Artikel-Nr: (ABFRLF-MA0197)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-MA0197

Beschreibung: 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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Artikel-Nr: (ABFRLF-MA0299)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-MA0299

Beschreibung: The Smad family of proteins are functioning in the transmission of extracellular signals in the TGF-β signaling pathway. Binding of a TGF-β superfamily ligands to extracellular receptors triggers phosphorylation of Smad2 at a Serine-Serine-Methionine-Serine (SSMS) motif at its C-terminus. Phosphorylated Smad2 is then able to form a complex with Smad4. These complexes accumulate in the cell nucleus, where they are directly participating in the regulation of gene expression.
In mammals, eight Smad proteins have been identified to date. The Smad family of proteins can be divided into three functional groups: the receptor-activated Smads (R-Smads), common mediator Smads (Co-Smads), and the inhibitory Smads (I-Smads). The R-Smads are directly phosphorylated by the activated type I receptors on their C-terminal Ser-Ser-X-Ser (SSXS) motif and include Smad1, Smad2, Smad3, Smad5, and Smad8. Smad2 and Smad3 are phosphorylated in response to TGF-β and activin, whereas Smad1, Smad5, and Smad8 are phosphorylated in response to BMP (Bone Morphogenetic Protein). This C-terminal phosphorylation allows R-Smad binding to Co-Smad, Smad4, and translocation to the nucleus where they regulate TGF-β target genes. Smad6 and Smad7 belong to the I-Smad which bind to the type I receptor or Smad4 and block their interaction with R-Smads.

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Artikel-Nr: (ABFRLF-MA0189)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-MA0189

Beschreibung: 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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Artikel-Nr: (ABFRLF-PA0023)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-PA0023

Beschreibung: 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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Artikel-Nr: (ABFRLF-MA0361)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-MA0361

Beschreibung: 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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Artikel-Nr: (ABFRLF-MA0013)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-MA0013

Beschreibung: 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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Artikel-Nr: (ABFRLF-MA0304)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-MA0304

Beschreibung: 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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Artikel-Nr: (ABFRLF-PA0182)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-PA0182

Beschreibung: Bcl-2 (B-cell lymphoma 2) family govern mitochondrial outer membrane permeabilization (MOMP) and can be either pro-apoptotic (Bax, BAD, Bak, Bid and Bok) or anti-apoptotic (Bcl-2, Bcl-xL, and Bcl-w). Mitochondrial membrane permeabilization and subsequent release of apoptotic factors are key mechanisms during this process.
The members of the Bcl-2 family share one or more of the four characteristic domains of homology entitled the Bcl-2 homology (BH) domains (named BH1, BH2, BH3 and BH4).
Bid consists of only one Bcl-2 homology domain, BH3. Bid cleavage to tBid (truncated Bid) activates apoptotic pathway at the mitochondrial level. Cleavage of cytosolic Bid and subsequent mitochondrial translocation have been detected in neuronal cell death related to acute or chronic neurodegeneration. Pharmacological inhibition of Bid can be a promising therapeutic strategy in neurological diseases where programmed cell death is prominent.
After Bid activation and mitochondrial translocation, the most prominent downstream mechanisms of Bid-dependent neuronal apoptosis involve disruption of mitochondrial membrane integrity and intracellular calcium homoeostasis and the release of pro-apoptotic mitochondrial factors such as cytochrome c.

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Artikel-Nr: (ABFRLF-PA0089)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-PA0089

Beschreibung: 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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Artikel-Nr: (ABFRLF-PA0079)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-PA0079

Beschreibung: 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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Artikel-Nr: (ABFRLF-PA0078)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-PA0078

Beschreibung: 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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Artikel-Nr: (ABFRLF-MA0271)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-MA0271

Beschreibung: The Smad family of proteins are functioning in the transmission of extracellular signals in the TGF-β signaling pathway. Binding of a TGF-β superfamily ligands to extracellular receptors triggers phosphorylation of Smad2 at a Serine-Serine-Methionine-Serine (SSMS) motif at its C-terminus. Phosphorylated Smad2 is then able to form a complex with Smad4. These complexes accumulate in the cell nucleus, where they are directly participating in the regulation of gene expression.
In mammals, eight Smad proteins have been identified to date. The Smad family of proteins can be divided into three functional groups: the receptor-activated Smads (R-Smads), common mediator Smads (Co-Smads), and the inhibitory Smads (I-Smads). The R-Smads are directly phosphorylated by the activated type I receptors on their C-terminal Ser-Ser-X-Ser (SSXS) motif and include Smad1, Smad2, Smad3, Smad5, and Smad8. Smad2 and Smad3 are phosphorylated in response to TGF-β and activin, whereas Smad1, Smad5, and Smad8 are phosphorylated in response to BMP (Bone Morphogenetic Protein). This C-terminal phosphorylation allows R-Smad binding to Co-Smad, Smad4, and translocation to the nucleus where they regulate TGF-β target genes. Smad6 and Smad7 belong to the I-Smad which bind to the type I receptor or Smad4 and block their interaction with R-Smads.
The Smads share sequence similarities, most notably in the N-terminal and carboxy-terminal regions, referred to as the MH1 (Mad Homology 1) and MH2 domains respectively. Smad2 and Smad3 have 66% amino acid sequence identity between their MH1 domains and 96% amino acid sequence identity between their MH2 domains.

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