Artikel-Nr: (ABFRLF-MA0262)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-MA0262

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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Artikel-Nr: (ABFRLF-MA0247)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-MA0247

Beschreibung: Cyclin-dependent kinase 7 (CDK7) has essential roles in the cell-division cycle as a CDK-activating kinase (CAK) and in the transcription as a component of the general transcription factor TFIIH.
This protein forms a trimeric complex with cyclin H and MAT1, which functions as a Cdk-activating kinase (CAK), phosphorylating cell-cycle CDKs. It is also an essential component of the transcription factor TFIIH, which phosphorylates the C-terminal domain (CTD) of the largest subunit of Pol II. This protein is thought to serve as a direct link between the regulation of transcription and the cell cycle.
Embryonic stem cells (ESCs) shows a very unusual cell cycle structure, characterized by a short G1 phase and a high proportion of cells in S-phase. This is associated with a unique mechanism of cell cycle regulation by the activity of cyclin dependent protein kinase (Cdk). The unique cell cycle structure and mechanism of cell cycle control indicates that the cell cycle machinery plays a role in establishment or maintenance of the stem cell state.

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Artikel-Nr: (ABFRLF-MA0265)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-MA0265

Beschreibung: Vimentin is a member of the intermediate filament family of proteins found in various non-epithelial cells, especially mesenchymal cells. Vimentin is responsible for maintaining cell shape, integrity of the cytoplasm, and stabilizing cytoskeletal interactions. Vimentin plays a significant role in supporting and anchoring the position of the organelles in the cytosol. Although most intermediate filaments are stable structures, vimentin also has a dynamic nature which is important when offering flexibility to the cell.
Two monomers which have central α-helical domains, capped on each end by non-helical domains twist around each other to form a coiled-coil dimer. Two dimers then form a tetramer, which, in turn, form a sheet by interacting with other tetramers.
There are some reports related to the biochemical function of intermediate filament network. The intracellular movement of LDL-derived cholesterol from the lysosome to the site of esterification is a vimentin-dependent process. A role for vimentin in mechanotransduction of shear stress has also been suggested. The mechanical stress of fluid shear on endothelial cells seems to trigger MAPK signaling pathways and stimulates proliferation.

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Artikel-Nr: (ABFRLF-MA0270)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-MA0270

Beschreibung: Focal adhesion kinase subfamily consists of the non-receptor proline-rich protein tyrosine kinases (PTKs). Two members of the family are focal adhesion kinase (FAK) and proline-rich tyrosine kinase 2 (PYK2). These two kinases have molecular mass between 110-125 kDa and are closely related in their structure. The presence of two proline-rich motifs within the C-terminal domains is conserved.
FAK is a nonreceptor and nonmembrane associated PTK which does not contain Src homology 2 (SH2) or SH3 protein interaction domains. The centrally located kinase domain of FAK is flanked by large N- and C-terminal noncatalytic domains.
FAK links integrin receptors to intracellular signaling pathways that are important for cell growth, survival, and migration. Integrin receptor engagement with ligands such as fibronectin can stimulate FAK autophosphorylation which enables FAK to function within a network of integrin-stimulated signaling pathways leading to the activation of targets such as the ERK and JNK/mitogen-activated protein kinase pathways. Recent study reveals that FAK is essential for angiogenesis in the embryo, functions in heart development and modulates the response of cardiomyocytes to pressure overload in adult mice.

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Artikel-Nr: (ABFRLF-MA0188)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-MA0188

Beschreibung: The complement system is a part of the larger immune system and three biochemical pathways are present: the classical complement pathway, the alternative pathway, and the mannose-binding lectin pathway.
Complement component C4 is an essential component of humoral immune response. In its activated form, C4b becomes a subunit of the C3 convertase, which is an enzymatic complex that activates C3 of the classical and lectin complement activation pathways. The classical pathway is initiated by the activation of the C1-complex (C1q, C1r and C1s) by C1q's binding to antibody-antigen. The C1-complex now binds to and splits C2 and C4 producing C2a and C4b. C4b and C2a bind to form C3-convertase. Production of C3-convertase leads to cleavage of C3 into C3a and C3b and C3b joins with the C3 convertase to make C5 convertase.
Human C4 is the most polymorphic protein of the complement system. Complement C4 exists as two isotypes, C4A (acidic) and C4B (basic). Although the sequence identity is very high, they have different hemolytic activities, covalent affinities to antigens and immune complexes, and serological reactivities. Each C4 contains β chain, α chain, C4a anaphyltoxin, C4b, and γ chain.
C4-deficient mice shows incomplete clearance of microbial attack and C4-deficiency in human shows increased autoimmune diseases.

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Artikel-Nr: (ABFRLF-MA0185)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-MA0185

Beschreibung: α-1-B glycoprotein (A1BG) which is a plasma protein with no known function belongs to the immunoglobulin superfamily. Although the human A1BG has been known for four decades, and the information about the amino acid sequence, chromosomal assignment, and even genetic polymorphism in different populations have been known, no biological function has been suggested. A1BG (Mr approximately equal to 63,000) consists of one polypeptide chain of 474 amino acids with four glucosamine oligosaccharides. The polypeptide has five intrachain disulfide bonds and consists of five repeating structural domains, each containing about 95 amino acids and one disulfide bond.
Recently human cyctein-rich secretory protein 3 (CRISP-3) has been found to be a binding partner of A1B, suggesting the A1BG-CRISP-3 complex displays a protecting function from a potentially harmful effect of free CRISP-3 in circulation.

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Artikel-Nr: (ABFRLF-MA0108)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-MA0108

Beschreibung: Fibrinogen is a soluble glycoprotein found in the plasma, with a molecular weight of 340kDa. It comprises of three pairs of non-identical polypeptide chains (α, 63.5kDa β, 56kDa, and γ, 47kDa chains) linked to each other by disulphide bonds. Low plasma fibrinogen concentrations are therefore associated with an increased risk of bleeding due to impaired primary and secondary hemostasis. Therefore Fibrinogen is an essential component of the blood coagulation system. Also it may play key roles in the process of atherosclerotic lesion formation, with subsequent effects on cardiovascular diseases. And increasing evidence from epidemiological studies suggests that elevated plasma fibrinogen levels are associated with an increased risk of ischaemic heart disease(IHD), stroke and other thromboembolism.

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Artikel-Nr: (ABFRLF-PA0024)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-PA0024

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-PA0033)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-PA0033

Beschreibung: Platelet-derived growth factors (PDGFs) have been implicated in the control of cell proliferation, survival and migration. The PDGF family of growth factors consists of five different disulphide-linked dimers built up of four different polypeptide chains encoded by four different genes. Theses isoforms, PDGF-AA, PDGF-AB, PDGF-BB, PDGF-CC and PDGF-DD, act via two receptor tyrosine kinases, PDGF receptors α and β. Thus far, gene-targeting experiments have been attempted to create knockout mice deficient for PDGFR-α or PDGFR-β. Those mice, however, died either at the embryonic stage or several days after birth. Platelet-derived growth factor receptors, PDGFR-α and PDGFR-β, have five extracellular immunoglobulin-like domains and an intracellular tyrosine kinase domain. Upon binding a PDGF, the receptors form homo- and heterodimers. Dimerization of the receptors juxtaposes the intracellular part of the receptors, which allow phosphorylation in trans between the two receptors in the complex. These autophosphorylation provide docking sites for downstream signal transduction molecules. More than 10 different SH2–domain-containing molecules have been shown to bind to different autophosphorylation sites in the PDGF α- and β-receptors. There are signal transduction molecules with enzymatic activity, such as PI3-kinase, PLC-γ, Src, SHP-2, GAP, as well as adaptor molecules such as Grb2, Shc, Nck, Grb7 and Crk, and Stats. Each of the different partners recruited by the activated receptor initiates different signaling pathways, making possible a great variety of cellular response.

UOM: 1 * 0,1 mL

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Artikel-Nr: (ABFRLF-PA0031)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-PA0031

Beschreibung: Methionine sulfoxide reductase (MsrA) reduces methionine sulfoxide (MetO) residues in proteins and free MetO to Methionine (Met). The catalytic activity of MsrA is dependent of bound metal and cofactors but it requires reducing equivalents from either DTT or a thioredoxin-regenerating system. MsrA plays an essential role in protecting cells against oxidative damage. The substrates of MsrA include calmodulin, HIV protease and 1-proteinase-inhibitor (1-3). Recent studies indicate that there is a connection between MsrA and Alzheimer’s disease in mammals (4).

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Artikel-Nr: (ABFRLF-PA0077)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-PA0077

Beschreibung: 14-3-3, a family of acidic and soluble proteins, highly conserved in amino acid sequences from yeast to mammals, is expressed in all eukaryotic cells. Seven isoforms(β, γ, ε, η, ζ, σ and τ/θ) encoded by seven distinct genes are identified in mammals and forms homo- and hetero- dimeric cup-shaped structures. As 14-3-3 is interacted with more than 100 binding partners, it regulates key proteins involved in various biological processes such as signal trans-duction, cell cycle, transcriptional control, cell proliferation, apoptosis, and ion channel physiology. Most 14-3-3 requires phosphorylation of serine or threonine residues in the target sequence. This protein is abundantly expressed in the brain and has been detected in the cerebrospinal fluid of patients with different neurological disorders.

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Artikel-Nr: (ABFRLF-PA0205)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-PA0205

Beschreibung: Connexin 43(Cx43) is a widely expressed gap junction protein that
mediates communication between many cell types. Gap junctions are
implicated in tissue homeostasis and control of cell proliferation and
differentiation. Connexin 43 is predominantly localized at the sarcolemma,
where six connexins assemble into a so-called connexon or hemichannel.
Clusters of these channels assemble to make gap junctions. Cx43 is a
target protein of several kinases, among them PKA, PKC, PKG, MAPK,
and casein kinase, but also for protein phosphatases. The
phosphorylation of Cx43 at Ser368 by PKC induces a closure of
Hemichannels. Src can phosphorylate Cx43 to alter gap junction
communication.

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Artikel-Nr: (ABFRLF-PA0178)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-PA0178

Beschreibung: Bcl-2 (B-cell lymphoma 2) family govern mitochondrial outer membrane permeabilization (MOMP) and can be either pro-apoptotic (Bax, BAD, Bak and Bok) or anti-apoptotic (Bcl-2, Bcl-xL, and Bcl-w). The mitochondrial release of cytochrome c through anion channel is regulated by Bcl-2 and Bcl-xL. The Bcl-2 family of proteins are key regulators of many signals leading to caspase, which when activated cause cellular destruction by cleaving a range of vital cellular substrates.
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).
The Bcl-2 gene has been implicated in a number of cancers, including melanoma, breast, prostate, and lung carcinomas, as well as schizophrenia and autoimmunity. It is also thought to be involved in resistance to conventional cancer treatment.
Apoptosis is an important component of the sequence of events during which anticancer drugs induce an antitumor response. The molecular mechanism for drug-induced apoptosis is associated with a mitochondrial dysfunction that is characterized by an increase in MOMP and a release of cytochrome c from mitochondria, indicating that Bcl-2 plays a critical role in anticancer drug-induced apoptosis.

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Lieferant: AbFrontier

Beschreibung: Actin is an abundant cytoskeletal protein found in all mammalian cells. Six distinct actin isotypes have been identified in mammalian cells. Each is encoded by a separated gene and is expressed in a developmentally regulated and tissue-specific manner. α and β-cytoplasmic actins are expressed in a wide variety of cells. Whereas, expression of α-skeletal, α-cardiac, α-vascular and γ-enteric actins
are more restricted to specialized muscle cell type. Actin's filaments form part of the cytoskeleton and play essential roles in regulating cell shape and movement.

Artikel-Nr: (ABFRLF-PA0218)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-PA0218

Beschreibung: Catalase is a homotetrameric heme-containing enzyme present within the matrix of all peroxisomes. It carries out a dismutation reaction in which hydrogen peroxide is converted to water and oxygen. Human catalase has the last four amino acids (-KANL) at the extreme C-terminus for peroxisome targeting. The monomer of human catalase is 61.3 kD in molecular size. Catalase has been implicated as an important factor in inflammation, mutagenesis, prevention of apoptosis, and stimulation of a wide spectrum of tumors. Loss of catalase leads to the human genetic disease, acatalasemia, or Takahara’s disease (1).

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Artikel-Nr: (ABFRLF-PA0175)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-PA0175

Beschreibung: Protein kinase C (PKC) is a family of serine-threonine kinases that regulate a broad spectrum of cellular functions. The family is composed of nine genes that express structurally related phospholipid-dependent kinases with distinct means of regulation and tissue distribution. Based on their structures and sensitivities to Ca2+ and diacylglycerol (DAG), they have been classified into conventional PKCs (α, β, and γ), novel PKCs (δ, ε, η, and θ), and atypical PKCs (ζ and λ/ι).
Mammalian PKC α consists of 672 amino acids and is distributed in all tissues, in contrast to other PKC isotypes whose expression is restricted in the particular tissues. PKC α is activated by a variety of stimuli originating from receptor activation, cell contact and physical stresses. Kinase activity of PKC α is regulated by phosphorylation of three conserved residues in its kinase domain: the activation-loop site Thr-497, the autophosphorylation site Thr-638, and the hydrophobic C-terminal site Ser-657. In some types of cells, PKC α is implicated in cell growth, in contrast, it may play a role in cell cycle arrest and differentiation in other types of cells. The responses are modulated by dynamic interactions with cell-type specific factors.

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