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Description:
Defensins form a family of microbicidal and cytotoxic peptides made by neutrophils. Members of the defensin family are highly similar in protein sequence. This gene encodes defensin, beta 4, an antibiotic peptide which is locally regulated by inflammation.
Description:
Membrane Receptors Transforming growth factor beta is a multifunctional cytokine known to modulate several tissue development and repair processes, including cell differentiation, cell cycle progression, cellular migration, adhesion, and extracellular matrix production. There are 3 forms encoded by separate genes TGFB1, TGFB2, and TGFB3. The diverse effects of TGF beta are mediated by the TGF beta receptors and cell surface binding proteins. In addition to type I TGF beta receptor (TGFBR1) and type II (TFGBR2), type III (TGF beta III receptor) has been identified. It is a glycoprotein that binds TGF beta and exists in both a membrane bound and a soluble form. It may serve as a receptor accessory molecule in both the TGF beta and fibroblast growth factor systems. TGF beta III receptor lacks a recognizable signaling domain and has no clearly defined role in TGF beta signaling. Endothelial cells undergoing epithelial mesenchymal transformation express TGF beta III receptor, and TGF beta III receptor specific antisera inhibits mesenchyme formation and migration. Misexpression of TGF beta III receptor in nontransforming ventricular endothelial cells conferrs transformation in response to TGFB2. These results support a model where TGF beta III receptor localizes transformation in the heart and plays an essential, nonredundant role in TGF beta signaling. TGF beta III receptor, or beta glycan, can function as an inhibin coreceptor with ActRII. TGF beta III receptor binds inhibin with high affinity and enhances binding in cells coexpressing ActRII and TGF beta III receptor. Inhibin forms crosslinked complexes with both recombinant and endogenously expressed TGF beta III receptor and ActRII. TGF beta III receptor confers inhibin sensitivity to cell lines that otherwise respond poorly to this hormone.
Description:
This gene encodes a member of the NF-kappa-B inhibitor family, which contain multiple ankrin repeat domains. The encoded protein interacts with REL dimers to inhibit NF-kappa-B/REL complexes which are involved in inflammatory responses. The encoded protein moves between the cytoplasm and the nucleus via a nuclear localization signal and CRM1-mediated nuclear export. Mutations in this gene have been found in ectodermal dysplasia anhidrotic with T-cell immunodeficiency autosomal dominant disease. [provided by RefSeq, Aug 2011].
Description:
Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20) family. They act as molecular chaperones although they do not renature proteins and release them in the fashion of a true chaperone; instead they hold them in large soluble aggregates. Post-translational modifications decrease the ability to chaperone. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is expressed widely in many tissues and organs. Elevated expression of alpha-B crystallin occurs in many neurological diseases; a missense mutation cosegregated in a family with a desmin-related myopathy. [provided by RefSeq, Jul 2008].
Description:
Inhibits the activity of dimeric NF-kappa-B/REL complexes by trapping REL dimers in the cytoplasm through masking of their nuclear localization signals. On cellular stimulation by immune and proinflammatory responses, becomes phosphorylated promoting ubiquitination and degradation, enabling the dimeric RELA to translocate to the nucleus and activate transcription.
Description:
Membrane Receptors Transforming growth factor beta is a multifunctional cytokine known to modulate several tissue development and repair processes, including cell differentiation, cell cycle progression, cellular migration, adhesion, and extracellular matrix production. There are 3 forms encoded by separate genes TGFB1, TGFB2, and TGFB3. The diverse effects of TGF beta are mediated by the TGF beta receptors and cell surface binding proteins. In addition to type I TGF beta receptor (TGFBR1) and type II (TFGBR2), type III (TGF beta III receptor) has been identified. It is a glycoprotein that binds TGF beta and exists in both a membrane bound and a soluble form. It may serve as a receptor accessory molecule in both the TGF beta and fibroblast growth factor systems. TGF beta III receptor lacks a recognizable signaling domain and has no clearly defined role in TGF beta signaling. Endothelial cells undergoing epithelial mesenchymal transformation express TGF beta III receptor, and TGF beta III receptor specific antisera inhibits mesenchyme formation and migration. Misexpression of TGF beta III receptor in nontransforming ventricular endothelial cells conferrs transformation in response to TGFB2. These results support a model where TGF beta III receptor localizes transformation in the heart and plays an essential, nonredundant role in TGF beta signaling. TGF beta III receptor, or beta glycan, can function as an inhibin coreceptor with ActRII. TGF beta III receptor binds inhibin with high affinity and enhances binding in cells coexpressing ActRII and TGF beta III receptor. Inhibin forms crosslinked complexes with both recombinant and endogenously expressed TGF beta III receptor and ActRII. TGF beta III receptor confers inhibin sensitivity to cell lines that otherwise respond poorly to this hormone.
Description:
The Golgi complex plays a key role in the sorting and modification of proteins exported from the endoplasmic reticulum. The protein encoded by this gene is a type II Golgi-resident protein. It may process proteins synthesized in the rough endoplasmic reticulum and assist in the transport of protein cargo through the Golgi apparatus. [provided by RefSeq, Jul 2008].
Description:
The TRIM motif includes three zinc binding domains, a RING, a B box type 1 and a B box type 2, and a coiled-coil region. The protein localizes to both the cytoplasm and the nucleus. Its function has not been identified.
Description:
Nuclear receptor that binds and is activated by variety of endogenous and xenobiotic compounds. Transcription factor that activates the transcription of multiple genes involved in the metabolism and secretion of potentially harmful xenobiotics, drugs and endogenous compounds. Activated by the antibiotic rifampicin and various plant metabolites, such as hyperforin, guggulipid, colupulone, and isoflavones. Response to specific ligands is species-specific. Activated by naturally occurring steroids, such as pregnenolone and progesterone. Binds to a response element in the promoters of the CYP3A4 and ABCB1/MDR1 genes.
Description:
The TRIM motif includes three zinc binding domains, a RING, a B box type 1 and a B box type 2, and a coiled-coil region. The protein localises to both the cytoplasm and the nucleus. Its function has not been identified.
Description:
GLT25D2 is a 626 amino acid protein that localizes to endoplasmic reticulum lumen and belongs to the glycosyltransferase 25 family. Possessing beta-galactosyltransferase activity, GLT25D2 transports beta-galactose to hydroxylysine residues on collagen but lacks glucosyltransferase activity. GLT25D2 is expressed in skeletal muscle and brain, and is encoded by a gene located on human chromosome 1q25.3, a region associated with the hereditary prostate cancer (HPC1) locus. Human chromosome 1 spans 260 million base pairs, contains over 3,000 genes, comprises nearly 8% of the human genome and houses a large number of disease-associated genes, including those that are involved in familial adenomatous polyposis, Stickler syndrome, Parkinson’s disease, Gaucher disease, schizophrenia and Usher syndrome.
Description:
Gemin4 is a component of the SMN core complex which, while in the cytoplasm, plays an essential role in ribonucleoprotein (snRNP) assembly, including the biogenesis, delivery and recycling of snRNPs to the spliceosome. In the nucleus, where SMN is required for pre-mRNA splicing, Gemin4 concentrates next to coiled bodies in subnuclear structures called gems, that are highly enriched in splicosomal snRNPs, and in the nucleolus. Deletion or loss-of-function mutations in the SMN lead to the neurodegenerative disease spinal muscular atrophy (SMA). The human Gemin4 maps to chromosome 17p13.
Description:
Catalyzes the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates HIF1A at 'Pro-402' and 'Pro-564'. May function as a cellular oxygen sensor and, under normoxic conditions, may target HIF through the hydroxylation for proteasomal degradation via the von Hippel-Lindau ubiquitination complex.
Description:
Catalyzes the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates HIF1A at 'Pro-402' and 'Pro-564'. May function as a cellular oxygen sensor and, under normoxic conditions, may target HIF through the hydroxylation for proteasomal degradation via the von Hippel-Lindau ubiquitination complex.
Description:
Catalyzes the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates HIF1A at 'Pro-402' and 'Pro-564'. May function as a cellular oxygen sensor and, under normoxic conditions, may target HIF through the hydroxylation for proteasomal degradation via the von Hippel-Lindau ubiquitination complex.
Description:
Serine/threonine-protein kinase that acts as a regulatory link between the membrane-associated Ras GTPases and the MAPK/ERK cascade, and this critical regulatory link functions as a switch determining cell fate decisions including proliferation, differentiation, apoptosis, survival and oncogenic transformation. RAF1 activation initiates a mitogen-activated protein kinase (MAPK) cascade that comprises a sequential phosphorylation of the dual-specific MAPK kinases (MAP2K1/MEK1 and MAP2K2/MEK2) and the extracellular signal-regulated kinases (MAPK3/ERK1 and MAPK1/ERK2). The phosphorylated form of RAF1 (on residues Ser-338 and Ser-339, by PAK1) phosphorylates BAD/Bcl2-antagonist of cell death at 'Ser-75'. Phosphorylates adenylyl cyclases: ADCY2, ADCY5 and ADCY6, resulting in their activation. Phosphorylates PPP1R12A resulting in inhibition of the phosphatase activity. Phosphorylates TNNT2/cardiac muscle troponin T. Can promote NF-kB activation and inhibit signal transducers involved in motility (ROCK2), apoptosis (MAP3K5/ASK1 and STK3/MST2), proliferation and angiogenesis (RB1). Can protect cells from apoptosis also by translocating to the mitochondria where it binds BCL2 and displaces BAD/Bcl2-antagonist of cell death. Regulates Rho signaling and migration, and is required for normal wound healing. Plays a role in the oncogenic transformation of epithelial cells via repression of the TJ protein, occludin (OCLN) by inducing the up-regulation of a transcriptional repressor SNAI2/SLUG, which induces down-regulation of OCLN. Restricts caspase activation in response to selected stimuli, notably Fas stimulation, pathogen-mediated macrophage apoptosis, and erythroid differentiation.
UOM:
1 * 100 µl
Promotion
,BOSSBS-1703R-A750EA
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