943 Risultati per: "AbFrontier"

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Gelsolin superfamily proteins control actin organization by severing filaments, capping filament ends and nucleating actin assembly. Gelsolin, a protein of 82–84 kDa, is the founding member of this family, which now contains at least another six members: villin, adseverin, capG, advillin, supervillin and flightless I. Gelsolin exists as a cytoplasmic as well as a plasma isoform, and can bind, sever and cap actin filaments. Plasma gelsolin level decreases dramatically as a result of major trauma and reinfusion of gelsolin can protect against lung damage associated with major burn injury and other types of insults. Recent study in Fas antibody-induced liver failure suggests that gelsolin exerts an overall anti-apoptotic effect in vivo. Gelsolin, a marker of motility, could be applied as a biomarker in assessing tumor prognosis. Tumor-associated processes such as invasion and metastasis are known to be critically dependent on dynamic alterations in the organization of the actin cytoskeleton. A causal relationship between gelsolin expression and in vitro invasion by way of signaling through Ras has been reported.

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Paraoxonases are a group of enzymes invloved in the hydrolysis of organophosphates. Paraoxon, an organophosphate, is an acetylcholinesterase inhibitor and the active metabolite of the insecticide parathion. Besides a toxicological role, clinical interest has focused on a protective role in vascular disease.
Paraoxonase-1 (PON1) is a calcium-dependent ester hydrolase that is tightly associated with apoA-I in HDL. PON1 prevents the oxidation of LDL, thereby the formation of atherogenic oxidised-LDL.
Polymorphisms of the human PON1 gene are correlated with coronary artery disease, indicating a genetic association between PON1 and coronary artery disease. PON1 activity is lower in subjects prone to development of atherosclerosis such as in type 1 and type 2 diabetes, familial hypercholesterolemia, and renal disease, indicating the involvement of PON1 in atherosclerosis development.
PON2 is a ubiquitously expressed intracellular protein that can protect cells against oxidative damage.
PON3 is similar to PON1 in activity but differs from it in substrate specificity.
PON1 and PON3 are implicated in lowering the risk of developing coronary artery disease and atherosclerosis. Human PON3 protein shares the 3 conserved cysteine residues identified in PON1, suggesting their importance of in vivo activities.
PON1-based catalytic scavengers can be a way to safe and effective organophosphate intoxication.

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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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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 kDa in molecular size. Catalase has been implicated as an important factor in inflammation, mutagenesis, preven-tion 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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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 kDa in molecular size. Catalase has been implicated as an important factor in inflammation, mutagenesis, preven-tion 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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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’s disease.

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Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3) (1). SOD1 is found in all eukaryotic species as a homodimeric 32 kDa enzyme containing one each of Cu and Zn ion per subunit (2). The manganese containing 80 kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain (3). SOD3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways (4). SOD4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor.

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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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Immunoglobulin G (IgG) is a monomeric immunoglobulin, built of two heavy chains γ and two light chains. Each molecule has two antigen binding sites. This is the most abundant immunoglobulin and is approximately equally distributed in blood and in tissue liquids. This is the only isotype that can pass through the placenta, thereby providing protection to the fetus in its first weeks of life before its own immune system has developed. It can bind to many kinds of pathogens, for example viruses, bacteria, and fungi, and protects the body against them by complement activation (classic pathway), opsonization for phagocytosis and neutralisation of their toxins. There are 4 subclasses: IgG1 (66%), IgG2 (23%), IgG3 (7%) and IgG4 (4%). 1) IgG1, IgG3 and IgG4 cross the placenta easily. 2) IgG3 is the most effective complement activator and IgG4 does not activate complement. 3) IgG1 and IgG3 bind with high affinity to Fc receptors on phagocytic cells. IgG4 has intermediate affinity and IgG2 affinity is extremely low.

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Cellular retinaldehyde-binding protein (CRALBP) is a cytoplasmic protein, abundantly expressed in the retinal pigment epithelium (RPE) and Müller glia of the retina and in the pineal gland. Structurally, human CRALBP is a ∼36-kDa monomeric protein, proposed to adopt an “open” or “closed” conformation, depending on whether it is carrying an endogenous ligand. CRALBP interacts structurally and functionally with 11-cis-retinol dehydrogenase (RDH5), an enzyme of the visual cycle in RPE. CRALBP is a member of the CRAL_TRIO family of proteins that share a lipid-binding domain derived from the yeast Sec14 protein.
Mutations in the human CRALBP gene cause retinal pathology and delayed dark adaptation. CRALBP knockout mice have a delayed response in rhodopsin regeneration, 11-cis-retinal production and dark adaptation after illumination.

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Cyclin-dependent kinase-5 (CDK5) is a member of the cyclin-dependent kinase family of serine/threonine kinases. Its mRNA and protein are expressed in kidney, testes, and ovary. And Its activity is detected almost exclusively in brain extracts.
Similar to other Cdks, monomeric Cdk5 displays no enzymatic activity, but Cdk5 is not activated by cyclins. Instead, Cdk5 activity requires association with one of two brain-specific regulatory subunits called p35 and p39. The two activators regulate the spatial and temporal expression of active Cdk5 to restrict its activity primarily to post-mitotic neurons.

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C reactive protein(CRP) is a major acute phase reactant synthesized primarily in the liver hepatocytes. It is a pentraxin(cyclic pentameric protein) compound of five identical nonglycosylated subunits of 206 amino acids each(M.W 24kDa) that are bound noncovalently to form the physiologic CRP molecule(M.W. 117.5kDa). CRP binds to several nuclear components, including chromatin and histones. This may indicate that it functions as a scavenger during cell necrosis. CRP also appears to have the strongest association with cardiovascular events; It may, therefore, be associated with ischemic heart disease. Its rapid increase in synthesis within hours after tissue injury or infection suggests that it contributes to host defense and that it is part of the innate immune response.

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Vitamin D-binding protein (DBP, VDBP), also called group-specific component (Gc) and macrophage-activating factor (GcMAF/DBP-MAF), is 52 to 58kDa plasma glycoprotein with many functions, such as transport of vitamin D metabolites, control of bone development, binding of fatty acids, sequestration of actin, and modulating immune and inflammatory responses. DBP is synthesized predominantly by hepatic parenchymal cells and detected in plasma, cerebrospinal fluid, seminal fluid, saliva and breast milk. The exploitation of the unique properties of DBP could enable the development of important therapeutic agents such as vitamin D-associated conditions, actin sequestering in trauma and inflammation, chronic obstructive pulmonary disease, osteopetrosis, cancer therapy and immune modulation by macrophage activation. The DBP molecule is therefore an ideal candidate molecule for further investigation by biotechnology-based companies seeking a platform from which to pursue new therapeutic options.

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Chromogranin A (CGA) was identified as a major soluble protein in adrenal medullary chromaffin granules. CHGA derived peptides are also known as Catestatin, Vasostatin-I,-II, Prochromacin, Pancreastatin and Parastatin.
CGA and its processed products are involved in the biogenesis of densecore secretory granules and have a role in immunity against microbes, and function as potential markers for several types of tumors. They have also been implicated in neurodegenerative disorders and cardiovascular diseases such as a hypertension. CGA accumulates in the senile and preamyloid plaques of Alzheimer’s disease, in Lewy bodies of Parkinson’s disease, and in the swollen neurons of Pick’s disease.

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Hematopoietic tyrosine phosphatase (HePTP, PTPN7) belongs to a subgroup of PTPases with two other members, STEP and PCPTP1.
HePTP is a 38 kDa class I non-receptor protein tyrosine phosphatase (PTP) that is strongly expressed in T cells. The protein consists of a short, amino-terminal extension that contains a conserved 16-amino acid kinase interaction motif (KIM) and a carboxy-terminal protein tyrosine phosphatase domain. HePTP binds the MAPK family kinases, Erk1/2 and p38 via KIM. Erk phosphorylates HePTP (at Thr45 and Ser72) and HePTP dephosphorylates Erk(at Tyr185).
HePTP is phosphorylated at Ser23 within the KIM by PKA in T cells. This
phosphorylation results in dissociation of the HePTP/ERK2 complex and reduced ability of HePTP to dephosphorylate ERK.

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Calcium binding proteins (CBPs) regulate intracellular levels of calcium Ca2+) ions. CBPs are involved in numerous functions, such as cell signaling, calcium uptake and transport, and cell motility. Calretinin (CR), calbindin D-28k (CB) and parvalbumin (PV) belong to the large family of Efhand calcium-binding proteins. The EF-hand is an amino acid sequence with a haracteristic threedimensional helix-loop-helix structure with high affinity for Ca2+. Calbindin D28k (calbindin) is a hexa EF-hand protein of 261 residues with 59% sequence identity to calretinin. It is a single-domain protein and the six EF hands interact extensively with one another so that they form one large globular domain. Calbindin is found in the brain and central nervous system with a distinct distribution over certain neuronal subtypes. Neuroprotective effects of calbindin has been reported in ischemic and glutamate toxicity models, primarily due to its ability to chelate calcium. Mice lacking calbindin have been shown to suffer from impaired motor coordination due to altered neuronal Ca2+-homeostasis. Notably, calbindin is found in high concentration in the kidney and in pancreatic b-cells, where it has been shown to protect against apoptosis. In osteoblasts, anti-apoptic activity of calbindin through the binding to caspase-3 has also been reported. Calbindin protects against apoptotic and necrotic cell death, suggesting its ability to buffer calcium.
Calbindin has been reported to binds Zn2+, revealing negative allosteric effect between the Zn2+- and Ca2+-binding events.

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Paraoxonases are a group of enzymes invloved in the hydrolysis of organophosphates. Paraoxon, an organophosphate, is an acetylcholinesterase inhibitor and the active metabolite of the insecticide parathion. Besides a toxicological role, clinical interest has focused on a protective role in vascular disease.
Paraoxonase-1 (PON1) is a calcium-dependent ester hydrolase that is tightly associated with apoA-I in HDL. PON1 prevents the oxidation of LDL, thereby the formation of atherogenic oxidised-LDL.
Polymorphisms of the human PON1 gene are correlated with coronary artery disease, indicating a genetic association between PON1 and coronary artery disease. PON1 activity is lower in subjects prone to development of atherosclerosis such as in type 1 and type 2 diabetes, familial hypercholesterolemia, and renal disease, indicating the involvement of PON1 in atherosclerosis development.
PON2 is a ubiquitously expressed intracellular protein that can protect cells against oxidative damage.
PON3 is similar to PON1 in activity but differs from it in substrate specificity.
PON1 and PON3 are implicated in lowering the risk of developing coronary artery disease and atherosclerosis. Human PON3 protein shares the 3 conserved cysteine residues identified in PON1, suggesting their importance of in vivo activities.
PON1-based catalytic scavengers can be a way to safe and effective organophosphate intoxication.

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TAK1 (transforming growth factor-β-activated kinase 1) is a MAPKKK activated by TGF-β, or the pro-inflammatory cytokines TNF (tumour necrosis factor) and IL-1 (interleukin-1), or bacterial LPS (lipopolysacchar-ide). It plays a key role in switching on several pro-inflammatory signaling pathways, including those that activate the MAPKs (mitogen-activated protein kinases), termed p38α MAPK, JNK1/2 (c-Jun N-terminal kinase 1/2) and ERK1/2 (extracellular-signal-regulated kinase 1/2), as well as the transcription factor NFκB (nuclear factor κB).
TAB1 (TAK1-binding protein 1) is one of the regulatory subunits of TAK1 and plays a role as an activator of TAK1 in response to stimulation of ΤGF-β. TAB-1 can also mediate MKK-independent p38 kinase. Recently, induction of p38 autophosphorylation and consequent kinase activation by TAB1 expression in cultured neonatal cardiomyocytes have been reported.

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Cofilin belongs to a family of related proteins with similar biochemical activities called the actin depolymerizing factor (ADF)/cofilin family.
ADF/cofilins play an important role in cytokinesis , endocytosis, and in the development of all embryonic tissues.
Cofilin is a small ubiquitous protein (~19 kDa) that is able to bind both G-actin (monomeric) and F-actin(filamentous actin). Cofilin promotes the regeneration of actin filaments by severing pre-existing filaments.
LIMK or TESK play a central role in the regulation of the actin cytoskeleton by phosphorylating cofilin on Ser3. Phosphorylation of cofilin at Ser3 inhibits its ability to bind to actin.

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Heat shock proteins are ubiquitous proteins and have been characterized as cytoprotective molecular chaperones. The typical function of a chaperone is to assist a protein to attain its functional conformation to prevent non-functional aggregation of misfolded proteins. The principal HSP families are HSP90, HSP70, HSP60 and the small HSPs including HSP27, ubiquitin, α-crystallin, Hsp20 and others. The common functions of small Hsps are chaperone activity, thermotolerance, inhibition of apoptosis, regulation of cell development, and cell differentiation.
Hsp27 has a molecular weight of approximately 27 kDa, although it has been shown to form large aggregates of up to 800 kDa in the cytosol. Hsp27 is found in several types of human cells, including tumour cells. Hsp27 interferes with apoptosis through its ability to interact with and inhibit key components of the apoptotic signaling pathway, including the caspase activation complex. Overexpression of heat shock proteins can increase the tumorigenic potential of tumour cells. HSP27 also has been reported to be involved in development and progression of hormone-refractory prostate cancer.

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The inhibitor of caspase-3-activated DNase (ICAD) is a caspase 3 substrate that controls nuclear apoptosis. ICAD has two isoforms: a functional isoform of 45kDa, ICAD-L/DNA fragmentation factor (DFF) 45; and a 35kDa isoform, ICAD-S/DFF35. Although both ICAD-L and ICAD-S can bind and inhibit CAD, only ICAD-L was reported to be functional. ICAD is cleaved to be inactivated and allow caspase-activated DNase (CAD) to execute nuclear internucleosomal apoptotic DNA fragmentation. In non-apoptotic cells, CAD is complexed with its inhibitor, ICAD. The activation of the CAD/ICAD complex occurs through the caspase 3-mediated
cleavage of ICAD at residues 117 and 224, which results in three ICAD fragments that are then released from CAD. In addition to its DNase
inhibitory activity, ICAD acts as a CAD specific folding chaperone. There are recent reports that ICAD is a potential target for restoring a normal apoptotic signal transduction pathway in colon and brain cancer cells.

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Anti-DUSP12 Mouse Monoclonal Antibody [clone: PK15-AF28F3]

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Dual specificity protein phosphatase 1(Also known as HVH1; MKP1; CL100; MKP-1; PTPN10)is an enzyme that in humans is encoded by the DUSP1 gene.[1][2]
The expression of DUSP1 gene is induced in human skin fibroblasts by oxidative/heat stress and growth factors. It specifies a protein with structural features similar to members of the non-receptor-type protein-tyrosine phosphatase family, and which has significant amino-acid sequence similarity to a Tyr/Ser-protein phosphatase encoded by the late gene H1 of vaccinia virus. The bacterially expressed and purified DUSP1 protein has intrinsic phosphatase activity, and specifically inactivates mitogen-activated protein (MAP) kinase in vitro by the concomitant dephosphorylation of both its phosphothreonine and phosphotyrosine residues. Furthermore, it suppresses the activation of MAP kinase by oncogenic ras in extracts of Xenopus oocytes. Thus, DUSP1 may play an important role in the human cellular response to environmental stress as well as in the negative regulation of cellular proliferation.[3]
DUSP1 has been shown to interact with MAPK14,[4][5] MAPK1[5][6] and MAPK8.[5]

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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.
Human complement factor C8 is one of five components (C5b, C6, C7, C8, and C9) that interact to form the cytolytic membrane attack complex (MAC) which is the cytolytic end product of the complement cascade. MAC is typically formed on the surface of intruding pathogenic bacterial as a result of the activation of the complement system, and it is one of the ultimate weapons of the immune system.
C8 is composed of an α (64 kDa), β (64 kDa), and γ (22 kDa) subunit. Within C8, the subunits are arranged as a disulfide-linked C8 α-γ heterodimer that is noncovalently associated with C8 β. During MAC formation, C8 α mediates binding and self-polymerization of C9 to form a pore-like structure on the membrane of target cells.

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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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ERK1 and ERK2 are widely expressed and are involved in the regulation of meiosis, mitosis, and postmitotic functions in differentiated cells. Many different stimuli, including growth factors, cytokines, virus infection, ligands for heterotrimeric guanine nucleotide binding protein (G protein)-coupled receptors and transforming agents, activate the ERK1 and ERK2 pathways. When growth factors bind to the receptor tyrosine kinase, Ras interacts with Raf, the serine/threonine protein kinase, and activates it as well. Once actived, Raf phosphorylates the other two kinases, MEK1/2, which in turn phosphorylates tyrosine/threonine in ERK 1/2. Upon activation, the ERKs either phosphorylate a number of cytoplasmic targets or migrate to the nucleus, where they phosphorylate and activate a number of transcription factors such as c-Fos and Elk-1.

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The inter-α-trypsin inhibitor (ITI, IαI) family, a typical and classical example for protein-glycosaminoglycanprotein (PGP) complexes, occurs constitutively in plasma at relatively high concentrations and is a result of alternate combinations of three kinds of heavy chains with a common light chain, the bikunin proteoglycan. Bikunin has two proteinase inhibitor domains and belongs to the Kunitz-type protease inhibitor family; it displays an inhibitory activity against trypsin, leukocyte elastase and plasmin. The heavy chains do not have any protease inhibitory properties but have the capacity to interact in vitro and in vivo with hyaluronic acid and this binding promotes the stability of the extra-cellular matrix. The ITI protein family is suspected of playing a key role in the extra-cellular matrix biology.

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The p90 ribosomal S6 kinases (RSKs) comprise a family of serine/threon-ine kinases that lie at the terminus of the ERK pathway. In humans, the RSK family consists of four isoforms (RSK1 to -4). RSK family members are unusual among serine/threonine kinases in that they contain two distinct kinase domains, both of which are catalytically functional. Theses kinase dimains are activated in a sequential manner by a series of phosphorylations. RSK regulates gene expression via association and phosphor-ylation of transcriptional regulators includ-ing c-Fos, estrogen receptor, NFkappaB/Ika-ppaB α, cAMP-response element-binding protein (CREB).

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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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Syk, Spleen tyrosine kinase, is expressed in a wide range of hematopoietic and non-hematopoietic cells and plays a key role in adaptive immune system, which is the immunoreceptor (B cell receptor and Fc-receptors) signaling pathways including Fcγ receptor-mediated phagocytosis. In hematopoietic cells such as B and T lymphocytes, natural killer cells, mast cells, macrophages and platelets, Syk is involved in the proximal signaling downstream of activated immunoreceptors (e.g. BCR, TCR, Fc receptors) containing immunoreceptor tyrosine-based activation motifs (ITAMs) to which it binds using its tandem SH2 domains. Activated and autophosphorylated Syk then phosphorylates its specific substrates including other enzymes and adaptor proteins, orchestrating a complex series of cellular responses such as cell proliferation, differentiation, survival and phagocytosis.