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Artikel-Nr: (ABFRLF-MA0068)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-MA0068

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 (1).

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Artikel-Nr: (ABFRLF-MA0253)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-MA0253

Beschreibung: Protein tyrosine phosphatases (PTPs) are a group of enzymes that remove phosphate groups from phosphorylated tyrosine residues on proteins. Together with tyrosine kinases, PTPs regulate the phosphorylation state of many important signaling molecules, such as the MAP kinase family. Recently, increasing attention has been focused on the growing family of PTPs. Like PTKs, PTPs have been implicated in cell signaling, cell growth and proliferation, and oncogenic transformation. Moreover, some PTPs can be involved in cell cycle regulation and embryogenesis.
Dual specificity phosphatases (DSPs) are an emerging subclass of the protein tyrosine phosphatase (PTP) gene superfamily, which appears to be selective for dephosphorylating the critical phosphothreonine and phosphotyrosine residues. The prototypical DSP is the VH1 gene in vaccinia virus expressed in late-stage viral infection.
A shallow active site pocket in VHR allows for the hydrolysis of phosphorylated serine, threonine, or tyrosine protein residues, whereas the deeper active site of protein tyrosine phosphatases (PTPs) restricts substrate specificity to only phosphotyrosine.

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Artikel-Nr: (ABFRLF-MA0335)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-MA0335

Beschreibung: Lactate dehydrogenase (LDH) is the enzyme in the glycolytic pathway that converts pyruvate to lactate with concomitant interconversion of NADH and NAD+. In mammals, the enzyme is encoded by three genes: LDHA (M or muscle form), LDHB (H or heart form), and LDHC (X or testis form). The three human LDHs have 84–89% sequence similarities and 69–75% amino acid identities. There are five different LDH isoenzymes based on the proportion of M and H chains existing in the LDH tetrameric structure.
The LDHA is hypoxia inducible and its expression is directly controlled by the transcriptional activity of the hypoxia inducible factor 1a (HIF1a). LDHB is also known to be upregulated in many cancers.

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Artikel-Nr: (ABFRLF-MA0201)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-MA0201

Beschreibung: Shc is a prototype adapter protein that is expressed from the earliest stages of T-cell development. Shc becomes rapidly tyrosine phosphorylated after T-cell receptor (TCR) engagement.
Three shc genes have been identified in mammals and their gene products have been referred to as ShcA, ShcB and ShcC. ShcA is ubiquitously expressed, while shcB and ShcC expression appear limited to neuronal cells. ShcA is expressed as three isoforms of about 46, 52 and 66 kDa.
Shc is composed of an N-terminal PTB, a central collagen-homology (CH) domain and a C-terminal SH2 domain. The 66 kDa isoform of ShcA is expressed in most cells except in the hematopoietic lineage and contains an additional amino-terminal CH-like region.
The tyrosine phosphorylation of Shc has been noticed upon engagement of numerous cell surface receptors such as growth factor receptors, antigen receptors, cytokine receptors, G-protein coupled receptors and hormone receptors. The involvement of ShcA in the Ras signaling pathway is initiated by the tyrosine-phosphorylation of the receptor protein tyrosine kinases (RPTKs) and subsequent interaction with Grb2 and Ras guanine nucleotide exchange factor, Sos. The Shc : Grb2 : Sos complex gets localized to the membrane through the interaction of Shc with the phosphorylated receptor. Membrane-bound Sos then activates Ras by catalysing GDP/GTD exchange. GTP-bound Ras then triggers downstream events, which include Raf, the mitogen-activated protein kinases (MAPKs) and MAPK kinase (MEK).

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Artikel-Nr: (ABFRLF-MA0203)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-MA0203

Beschreibung: Human carboxypeptidase N (CPN) [(EC) 3.4.17.3], a member of the CPN/E subfamily of “regulatory” metallo-carboxypeptidases, is a zinc metalloprotease, which cleaves basic amino acids, lysine and arginine, from the carboxy-terminus of biologically active peptides and proteins.
CPN is an extracellular glycoprotein synthesized in the liver and secreted into the blood, where it controls the activity of vasoactive peptide hormones, growth factors and cytokines by specifically removing C-terminal basic residues. Human CPN was discovered as an enzyme that inactivates bradykinin by cleaving its carboxy-terminal arginine and was also referred to as kininase I.
CPN is a major inactivator of anaphylatoxins C3a, C4a and C5a and also cleaves off C-terminal Lys residues from larger protein substrates, such as the M and B subunits of creatine kinase, released from the heart after myocardial infarction.
CPN is a tetramer (280 kDa) comprised of two heterodimers each
consisting of a catalytic CPN1(48 – 55 kDa) and non-catalytic CPN2 (83kDa) subunit.The CPN2 subunit keeps the smaller catalytic subunit in the circulation and protects it against inactivation at 37 °C. The CPN2 subunit may also promote the cleavage of higher molecular mass plasma protein substrates by the catalytic CPN1 subunit.
The most conserved region of the carboxypeptidase proteins is the active site. All mammalian carboxypeptidases contain a zinc binding site, a substrate binding site, an amino acid involved in peptide specificity, and an amino acid involved in catalytic activity of the protein.
Patients with reduced CPN level present chronic recurrent angioedema, which is unrelated to diet or environment.

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Artikel-Nr: (ABFRLF-MA0200)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-MA0200

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). 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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Artikel-Nr: (ABFRLF-MA0198)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-MA0198

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-MA0350)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-MA0350

Beschreibung: Anti-NF2 Mouse Monoclonal Antibody [clone: AF1G4]

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Artikel-Nr: (ABFRLF-MA0211)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-MA0211

Beschreibung: Hematopoietic progenitor kinase 1 (HPK1) is a 97 kDa serine/threonine protein kinase expressed only in hematopoietic cells and tissues. HPK1 is comprosed of a STE20-like kinase domain in its N-terminus, four proline-rich motifs (-P-x-x-P-), a caspase cleavage site, and a distal C-terminal Citron homology domain. The proline-rich motifs are capable of binding proteins that contain SH3 domains.
HPK1 is involved in many cellular signaling cascades that include MAPK signaling, antigen receptor signaling, apoptosis, growth factor signaling, and cytokine signaling. HPK1 binds many adaptor proteins including members of the Grb2 family, Nck family, Crk family, SLP-76 family, and actin-binding adaptors. HPK1 contains 13 potential tyrosine phosphorylation residues, some of which may be phosphorylated by ZAP-70, which provide potential docking sites for SH2 domains containing proteins.
HPK1 is activated by both EGF and PDGF stimulation where adaptor proteins are involved in mediating the localization of effector molecules to cell surface receptors.
Activation-induced cell death (AICD)-resistant T cells contain full-length HPK1, while AICD-sensitive T cells have HPK1-C (cleaved form). HPK1 might be a possible molecular switch used to discriminate between the extrinsic pathway involving death receptors and the intrinsic pathway determined by the ratio between anti- and pro-apoptotic Bcl-2 family members.

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Artikel-Nr: (ABFRLF-MA0020)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-MA0020

Beschreibung: The mammalian thioredoxin reductases (TrxRs) are a family of selenocysteine-containing pyridine nucleotide-disulfide oxido-reductases. 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-MA0367)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-MA0367

Beschreibung: Moesin (for membrane-organizing extension spike protein) is a member of the EMR protein family which includes ezrin and radixin. ERM proteins appear to function as cross-linkers between plasma membranes and actin-based cytoskeletons.

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Artikel-Nr: (ABFRLF-PA0183)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-PA0183

Beschreibung: Sequential activation of protein kinases within the MAPK (mitogen-activated protein kinases) cascades is a common mechanism of signal transduction in many cellular processes. The ERK signaling cascade is a central MAPK pathway that plays a role in the regulation of various cellular processes such as proliferation, differentiation, development, learning, and survival. Mitogen-activated protein kinase kinases (MAPKK) phosphorylate MAPK. MEK (MAP kinase or ERK kinase) is the immediate upstream activator kinase of ERK.
MEK6 encodes a 334-amino acid protein with 82% identity to MKK3. MEK6 is highly expressed in skeletal muscle like many other members of this family, but in contrast to MKK3 its expression in leukocytes is very low. The human MEKs (MEK1, MEK2, MEK3) show remarkably different activity toward ERKl and ERK2. MEK2 is the most active ERK activator. MEK3 is inactive toward ERKl or ERK2. MEK3, MEK4, and MEK6 phosphorylate and activate p38 MAP kinase. The p38 mitogen-activated protein (MAP) kinase signal transduction pathway is activated by proinflammatory cytokines and environmental stress. Transcription factors such as ATF2 and Elk-1 are targets of the p38 MAP kinase signal transduction pathway.

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Artikel-Nr: (ABFRLF-PA0093)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-PA0093

Beschreibung: Bone morphogenetic protein 4, also known as BMP4, is a member of the bone morphogenetic protein family which is part of the transforming growth factor-β superfamily. The superfamily includes large families of growth and differentiation factors. Bone morphogenetic proteins were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo. BMPs also regulate cell proliferation, differentiation, lineage determination, motility, and death.
BMP4 is a potent bone-inducing morphogen, and a reduction in expression has been associated with a variety of bone diseases, including the heritable disorder Fibrodysplasia Ossificans Progressiva.
BMP4 is a critical signaling molecule required for the early differentiation of the embryo and establishing of a dorsal-ventral axis. It also plays a role in the epithelial-mesenchymal interactions leading to tooth formation.
Both BMP2 and BMP4 have been found in calcified atherosclerotic plaques and aortic valve diseases, which suggests their importance in cardiovascular diseases.

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Artikel-Nr: (ABFRLF-MA0318)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-MA0318

Beschreibung: Son of sevenless (SOS) is a guanine nucleotide exchange factor that
activates Ras in response to growth factor stimulation. Sos1, and its
closely related Sos2 paralog, are comprised of an N-terminal
histone-binding domain, a RacGEF catalytic (DH) domain juxtaposed with
a PH domain, a Ras exchanger motif (REM) domain, a RasGEF catalytic
domain, and a C-terminal proline-rich region. Sos1 catalyzes the
GDP-GTP exchange within the membrane-bound GTPase Ras and
thereby switches on a key signaling circuit that involves the activation of
MAPK cascade central to cellular proliferation, survival and differentiation.
Growth factor stimulation rapidly induces the phosphorylation of Sos on
multiple serine and threonine sites. Phosphorylation of residues within the
Sos C-terminus by the MAP/ERK kinase disrupts the Grb2-Sos complex.

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Artikel-Nr: (ABFRLF-MA0283)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-MA0283

Beschreibung: Acetylcholinesterase hydrolyzes the neurotransmitter acetylcholine at neuromuscular junctions and brain cholinergic synapses, and thus terminates signal transmission. In addition, acetylcholinesterase contributes to various physiological processes through its involvement in the regulation of cell proliferation, differentiation and survival.
Because of alternative splicing at the C-terminus of acetylcholinesterase mRNA, it has three different isoforms: synaptic (S), erythrocytic (E) and read-through (R). These acetylcholinesterase variants selectively participate in the processes involved in promoting or attenuating cell death that accompany changes in expression, distribution and balance among the enzyme variants.
Impairment of cholinergic neurotransmission is a well-established fact in Alzheimer’s disease (AD). AD is characterized by a loss of cholinergic neurons and their cortical projections from the nucleus basalis and associated areas in the basal forebrain.
The cholinesterase inhibitors (ChE-Is) attenuate the cholinergic deficit underlying the cognitive and neuropsychiatric dysfunctions in patients with AD. Inhibition of brain acetylcholinesterase (AChE) has been the major therapeutic target of cholinesterase inhibitor treatment strategies for Alzheimer's disease (AD).

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Artikel-Nr: (ABFRLF-MA0051)

Lieferant: AbFrontier

Hersteller Artikel Nummer : LF-MA0051

Beschreibung: In vivo, tyrosine phosphorylation is reversible and dynamic; the phosphorylation states are governed by the opposing activites of protein tyrosine kinases (PTKs) and protein tyrosine phosphatases (PTPs). PTPs are involved in controlling of diverse array of cellular process. They are large(~100) and structurally diverse family of enzymes. PTPs contain one or two catalytic domains which is approximately 280 residues and are characterized by the existence of the signature motif HC(X)5R. The Cys and Arg residues in this motif have essential functions for catalytic activity. PTPs regulate cell growth and metabolism, with special emphasis on its ability to regulate integrin, growth factor, and cytokine signaling.

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