act 2

Expression system: E. coli
Length: 24-92, Full Length of Mature Protein
Activity: Cell Activity

Expression system: E. coli
Length: 24-92, Full Length of Mature Protein
Activity: Cell Activity

Expression system: E. coli
Length: 24-92, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 29-151, Full Length of Mature Protein
Activity: Not Tested

HDAC4 (histone deacetylase 4), belongs to class II of the histone deacetylase AcuC APhA family. Histone Deacetylases (HDACs) are a group of enzymes closely related to sirtuins. They catalyze the removal of acetyl groups from lysine residues in histones and non-histone proteins, resulting in transcriptional repression. In general, they do not act autonomously but as components of large multiprotein complexes, such as pRb-E2F and mSin3A, that mediate important transcription regulatory pathways. There are three classes of HDACs; classes 1, 2, and 4, which are closely related to Zn2+-dependent enzymes. HDACs are ubiquitously expressed and they can exist in the nucleus or cytosol. Their subcellular localization is affected by protein-protein interactions and by the class to which they belong. HDACs have a role in cell growth arrest, differentiation, and death and this has led to substantial interest in HDAC inhibitors as possible antineoplastic agents. HDAC4 possesses histone deacetylase activity and represses transcription when tethered to a promoter. It does not bind DNA directly but through transcription factors MEF2C and MEF2D. HDAC4 seems to interact in a multiprotein complex with RbAp48 and HDAC3.

Mitogen-activated protein kinase 8 (MAPK8), also known as JNK1, is a member of the MAP kinase family. MAP kinases act as an integration point for multiple biochemical signals and are involved in a wide variety of cellular processes such as proliferation, differentiation, transcription regulation, and development. The protein kinases JNK1 has been found to serve as critical molecular links between obesity, metabolic inflammation, and disorders of glucose homeostasis. It is critically involved in the promotion of diet-induced obesity, metabolic inflammation, and beta-cell dysfunction. The selective deficiency of JNK1 in the murine nervous system is sufficient to suppress diet-induced obesity. Genetic analysis indicates that the effects of JNK1 can be separated from the effects of JNK1 on obesity. JNK1 is a potential pharmacological target for the development of drugs that might be useful for the treatment of metabolic syndrome, and type 2 diabetes. Furthermore, JNK1 plays a major role in hypoxic cellular damage. JNK1 protein might be an attractive target for anti-hypoxic therapy in increasing resistance to many pathological conditions and diseases, leading to the oxygen deficit.

Acyl-Protein Thioesterase 1 (APT-1) is lysophospholipase that belongs to the AB hydrolase 2 family. Lysophospholipases are enzymes that act on biological membranes to regulate the multifunctional lysophospholipids. APT-1 performs on biological membranes to regulate the multifunctional lysophospholipids. It hydrolyzes lysophosphatidylcholine in both monomeric and micellar forms. It hydrolyzes fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS; in addition, it also has depalmitoylating activity and low lysophospholipase activity.

Human protein N-terminal glutamine amidohydrolase (WDYHV1) is an enzyme that in humans is encoded by the WDYHV1 gene, belongs to the NTAQ1 family.WDYHV1 mediates the side-chain deamidation of N-terminal glutamine residues to glutamate, which is an important step in N-end rule pathway of protein degradation. Conversion of the resulting N-terminal glutamine to glutamate renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. However,it does not act on substrates with internal or C-terminal glutamine andnon-glutamine residues in any position. With the exception of proline, all tested second-position residues on substrate peptides do not greatly influence the activity. In contrast, a proline at position 2, virtually abolishes deamidation of N-terminal glutamine.

DCX (doublecortin, N-GST chimera)contains 2 doublecortin domains and belongs to the doublecortin family. It is highly expressed in neuronal cells of fetal brain, but not expressed in other fetal tissues. In the adult, it is highly expressed in the brain frontal lobe, but very low expression in other regions of brain, and not detected in heart, placenta, lung, liver, skeletal muscles, kidney and pancreas. DCX is a microtubule-associated protein required for initial steps of neuronal dispersion and cortex lamination during cerebral cortex development. It may act by competing with the putative neuronal protein kinase DCAMKL1 in binding to a target protein. DCX may in that way participate in a signaling pathway that is crucial for neuronal interaction before and during migration, possibly as part of a calcium ion-dependent signal transduction pathway. It may be part with LIS-1 of a overlapping, but distinct, signaling pathways that promote neuronal migration. Defects in DCX are the cause of lissencephaly X-linked type 1 and subcortical band heterotopia X-linked.

Expression system: HEK293 Cells
Length: 25-242, Extracellular Domain
Activity: Not Tested

Expression system: E. coli
Length: 2-135, Full Length of Mature Protein
Activity: Not Tested

Expression system: HEK293 Cells
Length: 22-226, Partial
Activity: ELISA

Expression system: HEK293 Cells
Length: 31-239, Extracellular Domain
Activity: Not Tested

Expression system: E. coli
Length: 1-193, Full Length
Activity: Not Tested

Expression system: E. coli
Length: 102-176, Partial
Activity: Not Tested

Expression system: E. coli
Length: 132-357, Partial
Activity: Not Tested

72 kDa type IV collagenase also known as matrix metalloproteinase-2 (MMP-2) and gelatinase A is an enzyme that in humans is encoded by the MMP2 gene.It belongs to the matrix metalloproteinase (MMP) family. Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases that degrade components of the extracellular matrix (ECM) and play essential roles in various physiological processes such as morphogenesis, differentiation, angiogenesis and tissue remodeling, as well as pathological processes including inflammation, arthritis, cardiovascular diseases, pulmonary diseases and tumor invasion. MMP-2 is ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, atherosclerotic plaque rupture, as well as degrading extracellular matrix proteins. MMP-2 can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. MMP-2 cleaves KISS at a Gly-|-Leu bond and appears to have a role in myocardial cell death pathways.

Angiopoietin-like protein 1 (ANGPTL1) has been reported to suppress migration and invasion in lung and breast cancer, acting as a novel tumor suppressor candidate. Downregulation of tumor suppressor signaling plays an important role in the pathogenesis of hepatocellular carcinoma (HCC).The downregulation of the angiopoietin-like protein ANGPTL1 is associated with vascular invasion, tumor thrombus, metastasis, and poor prognosis in HCC. Ectopic expression of ANGPTL1 in HCC cells effectively decreased their in vitro and in vivotumorigenicity, cell motility, and angiogenesis. shRNA-mediated depletion of ANGPTL1 exerted opposing effects. ANGPTL1 promoted apoptosis via inhibition of the STAT3 Bcl-2-mediated antiapoptotic pathway and decreased cell migration and invasion via downregulation of transcription factors SNAIL and SLUG. Furthermore, ANGPTL1 inhibited angiogenesis by attenuating ERK and AKT signaling and interacted with integrin α1β1 receptor to suppress the downstream FAK Src-JAK-STAT3 signaling pathway. Taken together, these results suggest ANGPTL1 as a prognostic biomarker and novel therapeutic agent in HCC. ANGPTL1 expression was down-regulated in CRC tissues and inversely correlated with poor survival. ANGPTL1 repressed migration and invasion of CRC cells, and microRNA-138 was involved in this process. Angiopoietin-like protein 1 (ANGPTL1) has been shown to act as a tumor suppressor by inhibiting angiogenesis, cancer invasion, and metastasis.

Casein kinase I gamma 2 isoform (CSNK1G2), a member of the large casein kinase I (CKI) subfamily, protein kinase superfamily. It may affect the development of brain, and associate with vesicular trafficking and neurotransmitter releasing from small synaptic vesicles. The CKI family includes several other isoforms (alpha, beta, gamma, and delta). Dishevelled (Dsh), another positive component of the Wnt pathway, becomes phosphorylated in response to Wnt signals. All the CKI isoforms, with the exception of gamma, increase the phosphorylation of Dsh in vivo. Casein kinase 1 gamma (CK1gamma, or CSNK1G) is associated with the cell membrane and binds to LRP. CK1gamma was found to be needed for Wnt signaling through Wnt receptor LRP. CSNK1G2 inhibits Smad3-mediated TGF-beta responses including induction of target genes and cell growth arrest, and this inhibition is dependent on CSNK1G2 kinase activity. The overexpression of CSNK1G2 in human cancers, may act as an oncoprotein during tumorigenesis. In addition, as an MTA1s-binding protein, CSNK1G2 could further potentiate the estrogen receptor (ER) corepressive function of MTA1s.

Dual specificity tyrosine-phosphorylation-regulated kinase 3, also known as Regulatory erythroid kinase, REDK and DYRK3, is a nucleus protein which belongs to theprotein kinase superfamily, CMGC Ser Thr protein kinase family and MNB DYRK subfamily. DYRKs are an emerging family of dual-specificity kinases that play key roles in cell proliferation, survival, and development. DYRK3 contains oneprotein kinase domain. Isoform 1 and isoform 2 of DYRK3 are highly expressed in testis and in hematopoietic tissue such as fetal liver, and bone marrow. Isoform 2 of DYRK3 is the predominant form in testis. Isoform 1 of DYRK3 is the predominant form in fetal liver and bone marrow. Isoform 1 and isoform 2 are present at low levels in heart, pancreas, lymph node, and thymus. DYRK3 is a negative regulator of EPO-dependent erythropoiesis. It may place an upper limit on red cell production during stress erythropoiesis. DYRK3 inhibits cell death due to cytokine withdrawal in hematopoietic progenitor cells. It may also act by regulating CREB CRE signaling. DYRK3 proved to effectively inhibit NFAT (nuclear factor of activated T cells) transcriptional response pathways and to co-immunoprecipitate with NFATc3. DYRK3 attenuates (and possibly apportions) red cell production selectively during anemia.

GFER is a hepatotrophic growth factor and flavin-linked sulfhydryl oxidase which belongs to the Erv1 ALR family of proteins. GFER is widely expressed in various human tissues. They are two isoforms of this protein. Isoform 1 could regenerate the redox-active disulfide bonds in CHCHD4 MIA40, a chaperone essential for disulfide bond formation and protein folding in the mitochondrial intermembrane space. The reduced form of CHCHD4 MIA40 forms a transient intermolecular disulfide bridge with GFER ERV1, resulting in regeneration of the essential disulfide bonds in CHCHD4 MIA40, while GFER ERV1 becomes re-oxidized by donating electrons to cytochrome c or molecular oxygen. Isoform 2 may act as an autocrine hepatotrophic growth factor promoting liver regeneration. GFER could also induce the expression of S-adenosylmethionine decarboxyl-ase and ornithine decarboxylases (ODC). S-adenosylmethionine decarboxyl-ase and ornithine decarboxylases play an important role in the synthesis of polyamines.

SMAD Family Member 4 (SMAD4) is a cytoplasmic protein that belongs to the Dwarfin SMAD family. SMAD4 contains one MH1 (MAD homology 1) domain and one MH2 (MAD homology 2) domain. It is the component of the heterotrimeric SMAD2 SMAD3-SMAD4 complex that forms in the nucleus and is required for the TGF-mediated signaling. SMAD4 promotes binding of the SMAD2 SMAD4 FAST-1 complex to DNA and provides an activation function required for SMAD1 or SMAD2 to stimulate transcription. SMAD4 may act as a tumor suppressor. It positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator. Mutations or deletions in SMAD4 have been shown to result in pancreatic cancer, juvenile polyposis syndrome, and hereditary hemorrhagic telangiectasia syndrome.

Expression system: HEK293 Cells
Length: 30-224, Full Length of Mature Protein
Activity: Not Tested

Expression system: Baculovirus Insect Cells
Length: 1-325, Full Length
Activity: Not Tested