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Description:
Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion.
Description:
Cathelicidins are a family of antimicrobial proteins found in the peroxidase-negative granules of neutrophils. Along with the family of proteins known as defensins, cathelicidins participate in the first line of defense by preventing local infection and systemic invasion of microbes. FALL-39 precursor (FALL-39 peptide antibiotic, cationic anti-microbial protein, CAMP, CAP-18, HSD26) is a cathelicidin anti-microbial protein that contains the antibacterial peptide LL-37 (amino acids 134-170). In contrast to the defensins, which are cysteine-rich peptides that fold in ∫-pleated sheets, LL-37 is a cysteine-free peptide that can adopt an amphipathic å-helical conformation. LL-37 binds to bacterial lipopolysaccharides (LPS) and is a potent chemotactic factor for recruiting mast cells to sites of inflammation. LL-37 is present in inflammatory skin diseases that include psoriasis, sub-acute lupus erthematosus, dermatitis and nickel contact hypersensitivity. It is not found in normal skin epidermis. The secreted protein is expressed primarily in bone marrow, testis and neutrophils. The mouse and rat ortholog, CRAMP (cathelin-related antimicrobial peptide), is also part of the cathelicidin family of host defense peptides. These include precursors of potent antimicrobial peptides that direct antimicrobial activity against various microbial pathogens and also activate mesenchymal cells during wound repair. CRAMP is expressed in testis, spleen, stomach and intestine.
Description:
Cathelicidins are a family of antimicrobial proteins found in the peroxidase-negative granules of neutrophils. Along with the family of proteins known as defensins, cathelicidins participate in the first line of defense by preventing local infection and systemic invasion of microbes. FALL-39 precursor (FALL-39 peptide antibiotic, cationic anti-microbial protein, CAMP, CAP-18, HSD26) is a cathelicidin anti-microbial protein that contains the antibacterial peptide LL-37 (amino acids 134-170). In contrast to the defensins, which are cysteine-rich peptides that fold in ∫-pleated sheets, LL-37 is a cysteine-free peptide that can adopt an amphipathic å-helical conformation. LL-37 binds to bacterial lipopolysaccharides (LPS) and is a potent chemotactic factor for recruiting mast cells to sites of inflammation. LL-37 is present in inflammatory skin diseases that include psoriasis, sub-acute lupus erthematosus, dermatitis and nickel contact hypersensitivity. It is not found in normal skin epidermis. The secreted protein is expressed primarily in bone marrow, testis and neutrophils. The mouse and rat ortholog, CRAMP (cathelin-related antimicrobial peptide), is also part of the cathelicidin family of host defense peptides. These include precursors of potent antimicrobial peptides that direct antimicrobial activity against various microbial pathogens and also activate mesenchymal cells during wound repair. CRAMP is expressed in testis, spleen, stomach and intestine.
Description:
Transcriptional repressor that modulates both activator-dependent and basal transcription. Involved in the generation and migration of neural crest cells. Plays a role in mediating RAF1-induced transcriptional repression of the TJ protein, occludin (OCLN) and subsequent oncogenic transformation of epithelial cells (By similarity). Represses BRCA2 expression by binding to its E2-box-containing silencer and recruiting CTBP1 and HDAC1 in breast cells. In epidermal keratinocytes, binds to the E-box in ITGA3 promoter and represses its transcription. Involved in the regulation of ITGB1 and ITGB4 expression and cell adhesion and proliferation in epidermal keratinocytes. Binds to E-box2 domain of BSG and activates its expression during TGFB1-induced epithelial-mesenchymal transition (EMT) in hepatocytes. Represses E-Cadherin/CDH1 transcription via E-box elements. Involved in osteoblast maturation. Binds to RUNX2 and SOC9 promoters and may act as a positive and negative transcription regulator, respectively, in osteoblasts. Binds to CXCL12 promoter via E-box regions in mesenchymal stem cells and osteoblasts. Plays an essential role in TWIST1-induced EMT and its ability to promote invasion and metastasis.
Description:
The protein encoded by this gene is a member of the MAPkinase family. MAP kinases, also known as extracellularsignal-regulated kinases (ERKs), act in a signaling cascade thatregulates various cellular processes such as proliferation,differentiation, and cell cycle progression in response to avariety of extracellular signals. This kinase is activated byupstream kinases, resulting in its translocation to the nucleuswhere it phosphorylates nuclear targets. Alternatively splicedtranscript variants encoding different protein isoforms have beendescribed. [provided by RefSeq, Jul 2008].
Description:
Plays a critical role in MHC class II antigen processing by stabilizing peptide-free class II alpha/beta heterodimers in a complex soon after their synthesis and directing transport of the complex from the endoplasmic reticulum to the endosomal/lysosomal system where the antigen processing and binding of antigenic peptides to MHC class II takes place. Serves as cell surface receptor for the cytokine MIF.
Description:
Carboxypeptidase A2 (CPA2) is one of three different isoforms of human pancreatic carboxypeptidase A. Carboxypeptidase A2 acts on aromatic C-terminal residues.
Description:
Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. Does not mediate the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis.
Description:
The large binding pocket can accommodate several single chain phospholipids and fatty acids, GM2A also exhibits some calcium-independent phospholipase activity (By similarity). Binds gangliosides and stimulates ganglioside GM2 degradation. It stimulates only the breakdown of ganglioside GM2 and glycolipid GA2 by beta-hexosaminidase A. It extracts single GM2 molecules from membranes and presents them in soluble form to beta-hexosaminidase A for cleavage of N-acetyl-D-galactosamine and conversion to GM3.
Description:
Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). GTP-binding protein that does not act as an allosteric activator of the cholera toxin catalytic subunit. Requires assistance from GTPase-activating proteins (GAPs) like RP2 and PDE6D, in order to cycle between inactive GDP-bound and active GTP-bound forms. Required for normal cytokinesis and cilia signaling.
Description:
Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). GTP-binding protein that does not act as an allosteric activator of the cholera toxin catalytic subunit. Requires assistance from GTPase-activating proteins (GAPs) like RP2 and PDE6D, in order to cycle between inactive GDP-bound and active GTP-bound forms. Required for normal cytokinesis and cilia signaling.
Description:
The three human RAS genes encode highly related 188 to 189 amino acid proteins, designated H-Ras, N-Ras and K-Ras4A and K-Ras4B (the two K-Ras proteins arise from alternative gene splicing). Ras proteins function as binary molecular switches that control intracellular signaling networks. Ras-regulated signal pathways control such processes as actin cytoskeletal integrity, proliferation, differentiation, cell adhesion, apoptosis, and cell migration. Ras and ras-related proteins are often deregulated in cancers, leading to increased invasion and metastasis, and decreased apoptosis.DIRAS1 displays low GTPase activity and exists predominantly in the GTP-bound form. It is highly expressed in heart and brain.
Description:
GBGT1 is a 347 amino acid single-pass type II membrane protein that belongs to the glycosyltransferase 6 family. Localizing to the golgi apparatus membrane, GBGT1 is widely expressed, with high levels found in placenta, ovary and peripheral blood leukocyte, and lower levels expressed in liver, thymus and testis. GBGT1 utilizes manganese as a cofactor, and assists in the addition of N-acetylgalactosamine (GalNAc) in alpha-1,3-linkage to various substrates, resulting in the formation of glycolipids. Glycolipids are present in most eukaryotic cells and may assist in the adherence of certain pathogens. Existing as two alternatively spliced isoforms, the gene encoding GBGT1 maps to human chromosome 9q34.2 and mouse chromosome 2 A3.
Description:
Rsk1 is a member of a family of 90kDa ribosomal protein S6 kinases, which includes Rsk1, Rsk2 and Rsk3. These are broadly expressed serine/threonine protein kinases activated in response to mitogenic stimuli, including extracellular signal regulated protein kinases Erk1 and Erk2. Rsk1 is activated by MAPK in vitro and in vivo via phosphorylation. Active Rsks appear to play a major role in transcriptional regulation by translocating to the nucleus and phosphorylating c Fos and CREB.
UOM:
1 * 100 µl
Promotion
,BOSSBS-5680R-A680EA
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