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Fibroblast Growth Factors (FGFs) comprise a family of at least eighteen structurally realted proteins that are involved in a multitude of physiological and pathological cellular processes, including cell growth, differentation, angiogenesis, wound healing and tumorgenesis. The biological activities of the FGFs are mediated by a family if type I transmembrane tyrosine kinases which undergo dimerization and autophosphorylation after ligand binding. Four distinct genes encoding closely related FGF receptors, FGFR-1to -4 are known. Multiple forms of FGFR-1 to -3 are generated by alternative splicing of the mRNAs. A frequent splicing event involving FGFR-1 and -2 results in receptors containing all three Ig domains, referred to as the alpha isoform, or only IgII and IgIII, referred to as the ? isoform. Only the alpha isoform has been identified for FGFR-3 and FGFR-4. Additional splicing events for FGFR-1 to -3, involving the C-terminal half of the IgIII domain encoded by two mutually exclusive alternative exons, generate FGF receptors with alternative IgIII domains (IIIb and IIIc). A IIIa isoform which is a secreted FGF binding protein containing only the N-terminal half of the IgIII domain plus some intron sequences has also been reported for FGFR-1. Mutations in FGFR-1 to -3 have been found in patients with birth defects involving craniosynostosis.

Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signalling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occurring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin.

Oxidative Stress Responsive 1, also known as OXSR1 belongs to the neuronal calcium sensor gene family. OXSR1 encodes calcium-binding proteins which expressed mainly in neurons and regulates G protein-coupled receptor phosphorylation in a calcium-dependent way. OXSR1 regulates downstream kinases in response to environmental stress and functions in regulating the actin cytoskeleton.

TPRKB is a member of the CGI121/TPRKB family. TPRKB is localized to nucleus and cytoplasm and is ubiquitously expressed. TPRKB is known to cooperate with TP53RK/PRPK.

Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signaling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation.
Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occuring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin.

Ephrin type-B receptor 4 isoform b (Ephb4) belongs to the Eph receptor tyrosine kinase family which functions in neuronal guidance and mediate venal/arterial separation. EPHB4-mediated forward signaling regulates cellular repulsion and segregation form EFNB2-expressing cells. Furthermore, Ephb4 has a role in postnatal blood vessel remodeling, morphogenesis and permeability and is therefore essential in the context of tumor angiogenesis.

Fibroblast growth factors (FGFs) comprise a family of at least eighteen structurally related proteins that are involved in a multitude of physiological and pathological cellular processes, including cell growth, differentiation, angiogenesis, wound healing and tumorgenesis. The biological activities of the FGFs are mediated by a family of type I transmembrane tyrosine kinases which undergo dimerization and autophosphorylation after ligand binding. Four distinct genes encoding closely related FGF receptors, FGF R1 - 4, are known. All four genes for FGF Rs encode proteins with an N-terminal signal peptide, three immunoglobulin (Ig)-like domains, an acid-box region containing a run of acidic residues between the IgI and IgII domains, a transmembrane domain and the split tyrosine-kinase domain. Multiple forms of FGF R1 - 3 are generated by alternative splicing of the mRNAs. A frequent splicing event involving FGF R1 and 2 results in receptors containing all three Ig domains, referred to as the a isoform, or only IgII and IgIII, referred to as the b isoform. Only the a isoform has been identified for FGF R3 and FGF R4. Additional splicing events for FGF R1 - 3, involving the C-terminal half of the IgIII domain encoded by two mutually exclusive alternative exons, generate FGF receptors with alternative IgIII domains (IIIb and IIIc). A IIIa isoform which is a secreted FGF binding protein containing only the N-terminal half of the IgIII domain plus some intron sequences has also been reported for FGF R1. Mutations in FGF R1 - 3 have been found in patients with birth defects involving craniosynostosis. The complex patterns of expression of these receptors as well as the specificity of their interactions with the various FGF ligand family members are under investigation.

Calmodulin-2 acts as an intracellular calcium sensor protein. When the intracellular Ca2+ concentration increases, calmodulin can bind up to four Ca2+, changing its conformation and regulating cellular functions such as activation or inhibition of a large number of enzymes, ion channels, and receptors. P53 protein stimulates CALM2 gene expression in 041 cells. CALM-2 is involved in the processes of Ca(2+)-induced neuronal cell death and the blockage of calmodulin attenuates brain injury after cerebral ischemia. Calmodulin-2 mediates the control of a large number of enzymes and other proteins by ca(2+). among the enzymes to be stimulated by the calmodulin-ca(2+) complex are a number of protein kinases and phosphatases.

Recombinant Protein A/G fusion protein joins IgG binding domains of both Protein A and Protein G.
Protein A/G includes four Fc binding domains from Protein A and two from Protein G, yielding a final mass of 50.4 kDa. The binding dependency to pH of Protein A/G lower than Protein A, but has the additive properties of Protein A and G together. Protein A/G binds to all subclasses of human IgG, making it helpful for purifying polyclonal or monoclonal IgG antibodies whose subclasses have not been identifieed. Protein A/G binds to IgA, IgE, IgM and IgD. Protein A/G binds to all subclasses of mouse IgG excluding mouse IgA, IgM or serum albumin. This permits Protein A/G to be used in purification and detection of mouse monoclonal IgG antibodies, with no interference from IgA, IgM and serum albumin. Mouse monoclonal antibodies normally have a stronger affinity to the chimeric Protein A/G than to either Protein A or Protein G. Protein A/G also has been used for purification of macaque IgG.

Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVE supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.

MAPKSP1 is a scaffold protein which operates in the extracellular signal-regulated kinase (ERK) cascade. MAPKSP1 protein is restricted to late endosomes by the mitogen-activated protein-binding protein-interacting protein, and binds specifically to MAP kinase kinase MAP2K1/MEK1, MAP kinase MAPK3/ERK1, and MAP kinase MAPK1/ERK2.

Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signaling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation.
Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occuring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin.

Hexokinases phosphorylate glucose to produce glucose-6-phosphate, thus committing glucose to the glycolytic pathway. Hexokinase 2 is the predominant form found in skeletal muscle. It localizes to the outer membrane of mitochondria. Expression of this gene is insulin-responsive, and studies in rat suggest that it is involved in the increased rate of glycolysis seen in rapidly growing cancer cells.

Kallikrein-3 (KLK3) is a part of the kallikrein-related peptidase family. Kallikreins are a subgroup of serine proteases having various physiological functions. Numerous kallikreins take part in carcinogenesis and some may be prospective cancer and other disease biomarkers. Kallikrein-3 is 1 of the 15 kallikrein subfamily members located in a cluster on chromosome 19 and is a protease present in seminal plasma. KLK3 hydrolyzes semenogelin-1 consequently leading to the liquefaction of the seminal coagulum. KLK3 acts normally in the liquefaction of seminal coagulum, probably by hydrolysis of the high molecular mass seminal vesicle protein. Serum level of the KLK3 protein, called PSA in the clinical setting, is beneficial in the diagnosis and monitoring of prostatic carcinoma.

FGFR1 oncogene partner (FGFR1OP) is a member of the FGFR1OP family. The FGFR1OP protein is an essentially hydrophilic protein proposed to be a leucine-rich protein family member. A t(6;8)(q27;p11) chromosomal translocation, fusing the FGFR1OP gene and the FGFR1 gene, is seen in cases of myeloproliferative disorder. The ensuing chimeric protein contains the N-terminal leucine-rich region of the FGFR1OP protein fused to the catalytic domain of FGFR1. The FGFR1OP gene is believed to play a significant role in normal proliferation and differentiation of the erythroid lineage.

MAPKSP1 is a scaffold protein which operates in the extracellular signal-regulated kinase (ERK) cascade. MAPKSP1 protein is restricted to late endosomes by the mitogen-activated protein-binding protein-interacting protein, and binds specifically to MAP kinase kinase MAP2K1/MEK1, MAP kinase MAPK3/ERK1, and MAP kinase MAPK1/ERK2.

Forty-two antigenic domains were identified across the hepatitis A virus (HAV) polyprotein by using a set of 237 overlapping 20-mer synthetic peptides spanning the entire HAV polyprotein. Nineteen antigenic domains were found within the structural proteins, and 22 were found within the nonstructural proteins, with 1 domain spanning the junction of VP1 and P2A proteins. Five of these domains were considered immunodominant, as judged by both the breadth and the strength of their immunoreactivity. One domain is located within the VP2 protein at position 57-90 aa. A second domain, located at position 767-842 aa, contains the C-terminal part of the VP1 protein and the entire P2A protein. A third domain, located at position 1403-1456 a.a, comprises the C-terminal part of the P2C protein and the N-terminal half of the P3A protein. The fourth domain, located at position 1500-1519 a.a, includes almost the entire P3B, and the last domain, located at position 1719-1764 aa, contains the C-terminal region of the P3C protein and the N-terminal region of the P3D protein. Four of the five most immunoreactive domains are derived from small HAV proteins and/or encompass protein cleavage sites separating different HAV proteins.

Neurotrophic Receptor Tyrosine Kinase 2, also referred to NTRK2, is a tyrosine-protein kinase receptor which takes part in the development & the maturation of the central and the peripheral nervous systems through regulation of neuron survival, migration, proliferation, differentiation and synapse formation & plasticity. NTRK2 acts in learning and memory by regulating both short term synaptic function and long-term potentiation. The substrates that are known for the TRK family receptors are: SHC1, PI-3 kinase and PLC-gamma-1.

PGK1 is an X-linked enzyme that has a major role in the glycolytic pathway. PGK1 is a glycolytic enzyme which catalyzes the conversion of 1,3-diphosphoglycerate to 3-phosphoglycerate, generating an ATP molecule. PGK1 may also act as a cofactor for polymerase alpha. Defects in the PGK1 gene are usually associated with chronic hemolytic anemia, though it can be accompanied by either mental retardation or muscular disease (rhabdomyolysis). Overexpression of PGK1 and its signalling targets are possibly an expression-pathway in diffuse primary gastric carcinomas promoting peritoneal dissemination. It was shown that PGK1 is differentially expressed in the dorsolateral prefrontal cortex from patients with schizophrenia.

HSPB8 displays temperature-dependent chaperone activity. HSPB8 acts as a mn(2+)-dependent serine-threonine- specific protein kinase. we are not convinced that this is its true role. Defects in HSPB8 are a cause of distal hereditary motor neuropathy type ii (DHMN2) also known as distal spinal muscular atrophy (DSMA) and spinal muscular atrophy of the charcot-marie-tooth type. it is an autosomal dominant disorder of lower motor neurons characterized by distal muscle weakness.

AK1 is a small ubiquitous enzyme which is essential for maintenance and cell growth. It is involved in the regulation of adenine nucleotide composition within a cell by catalyzing the reversible transfer of the terminal phosphate group between ATP and AMP. The AK1 protein is found in the cytosol of skeletal muscle, brain and erythrocytes. Defects in the AK1 gene are the cause of a form of hemolytic anemia.

Protein A is a cell wall component produced by several strains of Staphylococcus aureus. The recombinant Protein A is genetically engineered protein and holds 5 IgG-binding regions of protein A. Recombinant Protein A functions basically the same as native Protein A and is perfect for purification of polyclonal or monoclonal IgG antibodies. Protein A binds to human IgG1, IgG2 and IgG4, mouse IgG2a, IgG2b and IgG3 and rat IgG2c. Protein A also binds to total IgG from rabbit, pig, dog, cat, and guinea pig.