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(R)-Pyrrolidine-3-carboxamide+hydrochloride
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(R)-Pyrrolidine-3-carboxamide+hydrochloride
Catalog Number:
(10265-932)
Supplier:
Bioss
Description:
Humanin, an endogenous anti-apoptotic peptide against Alzheimer disease-related insults, consists of 24 amino acids. The secreted protein is a neuroprotective factor against death induced by several different types of Alzheimer's disease genes. Humanin protects neuronal cells from damage caused by Alzheimer's disease genes, specifically APP (amyloid precursor protein). Humanin acts as a ligand for formyl peptide receptor-like 1 (FPRL1) with APP and utilizes its neuroprotective effects by inhibiting FPRL1 access to APP. The peptide prevents Bax translocation from cytosol to mitochondria. Humanin expression levels may be dependent on defects in energy production in muscles with mitochondrial abnormalities. The peptide has been detected in muscles of patients with the mitochondrial disease chronic progressive external ophthalmoplegia (CPEO). Humanin is mainly expressed in the kidney, heart, liver, testis and skeletal muscles.
Catalog Number:
(10246-848)
Supplier:
Bioss
Description:
Gigaxonin, also refered to as giant axonal neuropathy, GAN1, or KLHL16, controls protein degradation and is essential for neuronal function and survival. Gigaxonin is a member of the cytoskeletal BTB/kelch repeat family and influences cytoskeletal organization and dynamics, playing a large role in neurofilament architecture. The amino terminal BTB domain of gigaxonin binds to the ubiquitin-activating enzyme E1, while the carboxy-terminal kelch repeat domain interacts directly with the light chain of microtubule-associated protein 1B (MAP1B), and tags it for degredation. Overexpression of MAP1B may lead to neuronal cell death, whereas a reduction of MAP1B significantly improves the survival rate of neurons. Mutations in the Gigaxonin gene result in human giant axonal neuropathy (GAN), an autosomal recessive neurodegenerative disorder characterized by axonal degeneration caused by cytoskeletal abnormalities, including accumulated intermediate filaments.
Catalog Number:
(10304-960)
Supplier:
Bioss
Description:
The MAGUK (membrane-associated guanylate kinase homologs) family of proteins contain multiple protein-binding domains and are involved in cell junction organization, tumor suppression, and signaling. The MAGUK family is divided into four subfamilies: DLG-like, ZO1-like, p55-like and LIN2-like. MPP7 (MAGUK p55 subfamily member 7), also known as palmitoylated membrane protein 7, is a 576 amino acid protein that belongs to the MAGUK family and assists in the assembly of protein complexes. A peripheral membrane protein that exists as a heterodimer, MPP7 enhances tight junction formation and epithelial cell polarity. MPP7 contains one SH3 domain, a guanylate kinase-like domain, two L27 domains and a single PDZ (DHR) domain. The gene encoding MPP7 maps to human chromosome 10p11.23
Catalog Number:
(10330-794)
Supplier:
Bioss
Description:
The matrix metalloproteinases (MMPs) are a family of at least eighteen secreted and membrane bound zincendopeptidases. Collectively, these enzymes can degrade all the components of the extracellular matrix, including fibrillar and non fibrillar collagens, fibronectin, laminin and basement membrane glycoproteins. In general, a signal peptide, a propeptide, and a catalytic domain containing the highly conserved zinc binding site characterizes the structure of the MMPs. In addition, fibronectin like repeats, a hinge region, and a C terminal hemopexin like domain allow categorization of MMPs into the collagenase, gelatinase, stomelysin and membrane type MMP subfamilies. All MMPs are synthesized as proenzymes, and most of them are secreted from the cells as proenzymes. Thus, the activation of these proenzymes is a critical step that leads to extracellular matrix breakdown. MMPs are considered to play an important role in wound healing, apoptosis, bone elongation, embryo development, uterine involution, angiogenesis and tissue remodeling, and in diseases such as multiple sclerosis, Alzheimer's, malignant gliomas, lupus, arthritis, periodontis, glumerulonephritis, atherosclerosis, tissue ulceration, and in cancer cell invasion and metastasis.MMP17 has been reported to be elevated in several tumor cell lines, and is constituitively produced by some normal cell lines. Treatment of cells with Concanavolin A or the phorbol ester TPA stimulates production of MMP17 in some cell types, and the enzyme can be recovered in cell lysates. Shed forms of MMP17 have also been reported.
Catalog Number:
(10417-750)
Supplier:
Bioss
Description:
Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase involved in various cellular processes such as regulation of the B-cell receptor (BCR) signalosome, oxidative stress-induced apoptosis, androgen receptor-dependent transcription regulation, insulin signaling and endothelial cells proliferation. Plays a key role in B-cell activation by regulating BCR-induced NF-kappa-B activation. Mediates the activation of the canonical NF-kappa-B pathway (NFKB1) by direct phosphorylation of CARD11/CARMA1 at 'Ser-559', 'Ser-644' and 'Ser-652'. Phosphorylation induces CARD11/CARMA1 association with lipid rafts and recruitment of the BCL10-MALT1 complex as well as MAP3K7/TAK1, which then activates IKK complex, resulting in nuclear translocation and activation of NFKB1. Plays a direct role in the negative feedback regulation of the BCR signaling, by down-modulating BTK function via direct phosphorylation of BTK at 'Ser-180', which results in the alteration of BTK plasma membrane localization and in turn inhibition of BTK activity. Involved in apoptosis following oxidative damage: in case of oxidative conditions, specifically phosphorylates 'Ser-36' of isoform p66Shc of SHC1, leading to mitochondrial accumulation of p66Shc, where p66Shc acts as a reactive oxygen species producer. Acts as a coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and specifically mediating phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag for epigenetic transcriptional activation that prevents demethylation of histone H3 'Lys-4' (H3K4me) by LSD1/KDM1A. In insulin signaling, may function downstream of IRS1 in muscle cells and mediate insulin-dependent DNA synthesis through the RAF1-MAPK/ERK signaling cascade. May participate in the regulation of glucose transport in adipocytes by negatively modulating the insulin-stimulated translocation of the glucose transporter SLC2A4/GLUT4.
Catalog Number:
(10486-616)
Supplier:
Bioss
Description:
SAS-6 (spindle assembly abnormal protein 6 homolog, HsSAS-6) is a 657 amino acid protein encoded by the human gene SAS6. SAS-6 is a component of the centrosome that contains one PISA (present in SAS-6) domain. LK4, SAS-6, CPAP and other centriole related proteins are required at different stages of procentriole formation and were associated with different centriolar structures. SAS-6 associates only transiently with nascent procentrioles, whereas CEP135 and CPAP form a core structure within the proximal lumen of both parental and nascent centrioles. SAS-6 is necessary for procentriole formation in human cell lines and is localized asymmetrically next to the centriole at the onset of procentriole formation. SAS-6 levels oscillate during the cell cycle; it is degraded in mitosis starting at anaphase, and it accumulates again at the end of the following G1 phase. The anaphase-promoting complex targets SAS-6 for degradation by the 26S Proteasome, and a KEN box in the C-terminus of SAS-6 is necessary for its degradation. Increased SAS-6 levels promoted the formation of multiple procentrioles forming next to a single centriole.
Catalog Number:
(10465-870)
Supplier:
Bioss
Description:
The death domain (DD) containing protein PIDD is a p53 target gene in an erythroleukemia cell line that undergoes G1 phase arrest and subsequent apoptosis after p53 expression. Independently, PIDD was also described as a DD-containing protein with unknown function. The N-terminal region of PIDD contains seven leucine-rich repeats (LRRs), a protein interaction motif found in various proteins with diverse functions, followed by two ZU-5 domains and a C-terminal DD. PIDD forms a complex with caspase-2 and the adaptor protein RAIDD. Increased PIDD expression results in spontaneous activation of caspase-2 and sensitization to apoptosis by genotoxic stimuli, via interaction with caspase-2 and CRADD/RAIDD. PIDD also promotes apoptosis downstream of p53 as component of the DNA damage/stress response pathway that connects p53/TP53 to apoptosis. PIDD has also been shown to interact with NEMO/IKBKG and RIP1 and enhance sumoylation and ubiquitination of NEMO/IKBKG, an important component for activation of the transcription factor NF-kappa-B.
Catalog Number:
(10480-248)
Supplier:
Bioss
Description:
Chromosome 1 is the largest human chromosome spanning about 260 million base pairs and making up 8% of the human genome. There are about 3,000 genes on chromosome 1, and considering the great number of genes there are also a large number of diseases associated with chromosome 1. Notably, the rare aging disease Hutchinson-Gilford progeria is associated with the LMNA gene which encodes lamin A. When defective, the LMNA gene product can build up in the nucleus and cause characteristic nuclear blebs. The mechanism of rapidly enhanced aging is unclear and is a topic of continuing exploration. The MUTYH gene is located on chromosome 1 and is partially responsible for familial adenomatous polyposis. Stickler syndrome, Parkinsons, Gaucher disease and Usher syndrome are also associated with chromosome 1. A breakpoint has been identified in 1q which disrupts the DISC1 gene and is linked to schizophrenia. Aberrations in chromosome 1 are found in a variety of cancers including head and neck cancer, malignant melanoma and multiple myeloma.
Catalog Number:
(10407-222)
Supplier:
Bioss
Description:
Involved in bile acid metabolism. In liver hepatocytes catalyzes the second step in the conjugation of C24 bile acids (choloneates) to glycine and taurine before excretion into bile canaliculi. The major components of bile are cholic acid and chenodeoxycholic acid. In a first step the bile acids are converted to an acyl-CoA thioester, either in peroxisomes (primary bile acids deriving from the cholesterol pathway), or cytoplasmic at the endoplasmic reticulum (secondary bile acids). May catalyze the conjugation of primary or secondary bile acids, or both. The conjugation increases the detergent properties of bile acids in the intestine, which facilitates lipid and fat-soluble vitamin absorption. In turn, bile acids are deconjugated by bacteria in the intestine and are recycled back to the liver for reconjugation (secondary bile acids). May also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids. In vitro, catalyzes the hydrolysis of long- and very long-chain saturated acyl-CoAs to the free fatty acid and coenzyme A (CoASH), and conjugates glycine to these acyl-CoAs.
Catalog Number:
(10417-870)
Supplier:
Bioss
Description:
Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and second messenger diacylglycerol. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. PKC family members also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play a distinct role in cells. The protein encoded by this gene is one of the PKC family members. This protein kinase has been reported to be involved in many different cellular functions, such as B cell activation, apoptosis induction, endothelial cell proliferation, and intestinal sugar absorption. Studies in mice also suggest that this kinase may also regulate neuronal functions and correlate fear-induced conflict behavior after stress. Alternatively spliced transcript variants encoding distinct isoforms have been reported.
Catalog Number:
(10475-968)
Supplier:
Bioss
Description:
Involved in vesicular transport in the osteoclast (By similarity). May have a role in sialyl-lex-mediated transduction of apoptotic signals.Tissue specificity: Expressed in placenta, liver, prostate, thymus, spleen, ovary, colon, colon carcinoma and peripheral blood lymphocytes (PBL). Weakly expressed in brain, lung, kidney, and testis. No expression in heart, skeletal muscle, pancreas and small intestine. Predominantly expressed in the breast carcinoma cell line MCF-7.Involvement in disease:Defects in PLEKHM1 are the cause of osteopetrosis autosomal recessive type 6 (OPTB6); also known as autosomal recessive osteopetrosis intermediate form. Osteopetrosis is a rare genetic disease characterized by abnormally dense bone, due to defective resorption of immature bone. The disorder occurs in two forms: a severe autosomal recessive form occurring in utero, infancy, or childhood, and a benign autosomal dominant form occurring in adolescence or adulthood. Autosomal recessive osteopetrosis is usually associated with normal or elevated amount of non-functional osteoclasts.
Catalog Number:
(10423-990)
Supplier:
Bioss
Description:
Serine-threonine kinase which transduces inflammatory and cell-death signals (programmed necrosis) following death receptors ligation, activation of pathogen recognition receptors (PRRs), and DNA damage. Upon activation of TNFR1 by the TNF-alpha family cytokines, TRADD and TRAF2 are recruited to the receptor. Phosphorylates DAB2IP at 'Ser-728' in a TNF-alpha-dependent manner, and thereby activates the MAP3K5-JNK apoptotic cascade. Ubiquitination by TRAF2 via 'Lys-63'-link chains acts as a critical enhancer of communication with downstream signal transducers in the mitogen-activated protein kinase pathway and the NF-kappa-B pathway, which in turn mediate downstream events including the activation of genes encoding inflammatory molecules. Polyubiquitinated protein binds to IKBKG/NEMO, the regulatory subunit of the IKK complex, a critical event for NF-kappa-B activation. Interaction with other cellular RHIM-containing adapters initiates gene activation and cell death. RIPK1 and RIPK3 association, in particular, forms a necrosis-inducing complex.
Catalog Number:
(10466-450)
Supplier:
Bioss
Description:
TID1 is a human homolog of the Drosophila tumor suppressor lethal tumerous imaginal discs and encodes two mitochondrial matrix localized splice variants of human Tid1 designated hTid1S and hTid1L. These proteins are the conserved members of the DnaJ family of proteins which act as cochaperons for mitochondrial Hsp70. They contain a conserved tetrahedrical J domain which binds to Hsp70 chaperones and activates their ATPase activity. Expression of hTid1L increases apoptosis induced by DNA damaging agents as mitomycin C and TNF alpha. A J domain mutant of hTid1L can dominantly suppress apoptosis and in sharp contrast the J domain mutant of hTid1S increases apoptosis. Expression of hTid1S and hTid1L affects cytochrome c release from the mitochondria and caspase 3 activation, while activation of caspase 8 is unaffected. It is strongly suggested that these two splice variants exert their anti and pro apoptotic effects through discrete substrates and activities. Hence the relative abundance of these proteins or their substrates may allow the mitochondria to dampen or enhance the apoptotic signals.
Catalog Number:
(10352-108)
Supplier:
Bioss
Description:
Brutons tyrosine kinase (BTK) is a member of the BTK/Tec family of cytoplasmic tyrosine kinases. Like other BTK family members, it contains a pleckstrin homology (PH) domain, Src homology SH3 and SH2 domains. BTK plays an important role in B cell development. Activation of B cells by various ligands is accompanied by BTK membrane translocation mediated by its PH domain binding to phosphatidylinositol-3,4,5-trisphosphate. The membrane located BTK is active and associated with transient phosphorylation of two tyrosine residues, Tyr551 and Tyr223. Tyr551 in the activation loop is transphosphorylated by the Src family tyrosine kinase, leading to autophosphorylation at Tyr223 within the SH3 domain, which is necessary for full activation. The activation of BTK is negatively regulated by PKC beta through phosphorylation of BTK at Ser180, which results in reduced membrane recruitment, transphosphorylation and subsequent activation. The PKC/BTK inhibitory signal is likely to be a key determinant of the B cell receptor signaling threshold to maintain optimal BTK activity.
Catalog Number:
(10669-648)
Supplier:
Bioss
Description:
The RING-type zinc finger motif is present in a number of viral and eukaryotic proteins and is made of a conserved cysteine-rich domain that is able to bind two zinc atoms. Proteins that contain this conserved domain are generally involved in the ubiquitination pathway of protein degradation. RNF180 (ring finger protein 180), also known as Rines, is a 592 single-pass membrane protein that contains a single RING-type zinc finger. Expressed as three alternatively spliced isoforms, RNF180 is well conserved among vertebrates. RNF180 is expressed in brain, kidney, testis and uterus and localizes to the endoplasmic reticulum. RNF180 is an E3 ubiquitin ligase involved in the ubiquitin-proteasome pathway. RNF180 is encoded by a gene located on human chromosome 5, which contains 181 million base pairs and comprises nearly 6% of the human genome. Deletion of the p arm of chromosome 5 leads to Cri du chat syndrome, while deletion of the q arm, or of chromosome 5 altogether, is common in therapy-related acute myelogenous leukemias and myelodysplastic syndrome.
Catalog Number:
(10363-062)
Supplier:
Bioss
Description:
Mediates the nuclear export of cellular proteins (cargos) bearing a leucine-rich nuclear export signal (NES) and of RNAs. In the nucleus, in association with RANBP3, binds cooperatively to the NES on its target protein and to the GTPase RAN in its active GTP-bound form (Ran-GTP). Docking of this complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the cargo from the export receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Involved in U3 snoRNA transport from Cajal bodies to nucleoli. Binds to late precursor U3 snoRNA bearing a TMG cap. Several viruses, among them HIV-1, HTLV-1 and influenza A use it to export their unspliced or incompletely spliced RNAs out of the nucleus. Interacts with, and mediates the nuclear export of HIV-1 Rev and HTLV-1 Rex proteins. Involved in HTLV-1 Rex multimerization.
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