"Bioss"

Supplier: Bioss

The human insulin receptor is a heterotetrameric membrane glycoprotein consisting of disulfide linked subunits in a beta-alpha-alpha-beta configuration. The beta subunit (95 kDa) possesses a single transmembrane domain, whereas the alpha subunit (135 kDa) is completely extracellular. The insulin receptor exhibits receptor tyrosine kinase (RTK) activity. RTKs are single pass transmembrane receptors that possess intrinsic cytoplasmic enzymatic activity, catalyzing the transfer of the gamma phosphate of ATP to tyrosine residues in protein substrates. RTKs are essential components of signal transduction pathways that affect cell proliferation, differentiation, migration and metabolism.Included in this large protein family are the insulin receptor and the receptors for growth factors such as epidermal growth factor, fibroblast growth factor and vascular endothelial growth factor. Receptor activation occurs through ligand binding, which facilitates receptor dimerization and autophosphorylation of specific tyrosine residues in the cytoplasmic portion. The interaction of insulin with the alpha subunit of the insulin receptor activates the protein tyrosine kinase of the beta subunit, which then undergoes an autophosphorylation that increases its tyrosine kinase activity. Three adapter proteins, IRS1, IRS2 and Shc, become phosphorylated on tyrosine residues following insulin receptor activation. These three phosphorylated proteins then interact with SH2 domain containing signaling proteins.

Supplier: Bioss

LRSAM1 is an E3 ubiquitin-protein ligase that mediates monoubiquitination of TSG101 at multiple sites, leading to inactivation of the ability of TSG101 to sort endocytic (EGF receptors) and exocytic (HIV-1 viral proteins) cargos. It selectively regulates cell adhesion molecules and plays a role in receptor endocytosis and viral budding. LRSAM1 contains a RING-type zinc finger, 5 leucine-rich repeats and 1 SAM (sterile alpha motif) domain. The coiled coil domains interact with the SB domain of TSG101. The PTAP motifs mediate the binding to UEV domains. There are 3 isoforms produced by alternative splicing.

Supplier: Bioss

HN1

Supplier: Bioss

Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins involved in cell cycle progression, signal transduction and transcription. Specifically recognizes phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. Degradation of CDKN1B/p27kip also requires CKS1. Recognizes target proteins ORC1, CDT1, RBL2, KMT2A/MLL1, CDK9, RAG2, FOXO1, UBP43, and probably MYC, TOB1 and TAL1. Degradation of TAL1 also requires STUB1. Recognizes CDKN1A in association with CCNE1 or CCNE2 and CDK2. Promotes ubiquitination and destruction of CDH1 in a CK1-Dependent Manner, thereby regulating cell migration.

Supplier: Bioss

DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. Exhibits potent antiviral activity against vif-deficient HIV-1. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination-independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single-or double-stranded RNA. Exhibits antiviral activity also against simian immunodeficiency viruses (SIVs), hepatitis B virus (HBV), equine infectious anemia virus (EIAV), xenotropic MuLV-related virus (XMRV) and simian foamy virus (SFV). May inhibit the mobility of LTR and non-LTR retrotransposons.

Supplier: Bioss

CCDC153

Supplier: Bioss

May be involved in the regulation of cellular proliferation and/or differentiation.

Supplier: Bioss

Degradation in endoplasmic reticulum proteins, also designated Derlins or DERtrins, are crucial for the degradation of misfolded endoplasmic reticulum (ER) luminal proteins. Derlin proteins are multi-pass membrane proteins localizing to the ER. Derlins are involved in transferring misfolded proteins from the ER to the cytosol, where the misfolded proteins are destroyed in an ubiquitin-dependent manner by the proteasome. In the case of cytomegalovirus infection, Derlin-1, as opposed to Derlins-2 and -3, is involved in the export of MHC class I heavy chains from the ER via its interaction with the viral protein US11. Derlins may also be important for cell proliferation.

Supplier: Bioss

Fatty acid elongase specific to C12-C16 saturated and monoinsaturated fatty acids.

Supplier: Bioss

Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.

Supplier: Bioss

Receptor that mediates the recognition, internalization and degradation of oxidatively modified low density lipoprotein (oxLDL) by vascular endothelial cells. OxLDL is a marker of atherosclerosis that induces vascular endothelial cell activation and dysfunction, resulting in pro-inflammatory responses, pro-oxidative conditions and apoptosis. Its association with oxLDL induces the activation of NF-kappa-B through an increased production of intracellular reactive oxygen and a variety of pro-atherogenic cellular responses including a reduction of nitric oxide (NO) release, monocyte adhesion and apoptosis. In addition to binding oxLDL, it acts as a receptor for the HSP70 protein involved in antigen cross-presentation to naive T-cells in dendritic cells, thereby participating in cell-mediated antigen cross-presentation. Also involved in inflammatory process, by acting as a leukocyte-adhesion molecule at the vascular interface in endotoxin-induced inflammation. Also acts as a receptor for advanced glycation end (AGE) products, activated platelets, monocytes, apoptotic cells and both Gram-negative and Gram-positive bacteria.

Supplier: Bioss

Alpha-lactalbumin is the B protein of lactose synthetase secreted by the mammary epithelial cells. It is a potent Ca2+-elevating and apoptosis-inducing agent with broad, yet selective, cytotoxic activity. Multimeric ?lactalbumin has been shown to kill all transformed, embryonic and lymphoid cells tested, but not mature epithelial elements. This suggests that milk contributes to mucosal immunity not only by furnishing antimicrobial molecules but also by policing the function of lymphocytes and epithelium. ?lactalbumin may be helpful in discovering the site of origin of metastatic breast tumors. Human lactalbumin contains 123 amino acid residues. Comparison of the 5' flanking sequences of the two Alpha-lactalbumin genes with those of five casein genes reveals the presence of a highly conserved region extending from position -140 to -110 in all seven sequences examined, suggesting a possible regulatory role in the hormonal control or tissue-specific expression of milk protein genes in the mammary gland.

Supplier: Bioss

Receptor potentially involved in both adhesion and signaling processes early after leukocyte activation. Plays an essential role in leukocyte migration (By similarity).

Supplier: Bioss

PIGA belongs to the glycosyltransferase 1 family and is necessary for the synthesis of N-acetylglucosaminyl-phosphatidylinositol, the very early intermediate in GPI-anchor biosynthesis. Defects in PIGA are the cause of paroxysmal nocturnal hemoglobinuria (PNH) which is an acquired hemolytic blood disorder characterized by chronic hemolysis with hemoglobinuria, increased tendency to venous thrombosis, and variable degrees of bone marrow failure.

Supplier: Bioss

MYBPC3 encodes the cardiac isoform of the thick-filament myosin-binding protein C. It is found in the crossbridge-bearing zone (C region) of A bands in vertebrate striated muscle. Regulatory phosphorylation of MYBPC3 by cAMP-dependent protein kinase (PKA) upon adrenergic stimulation may be linked to modulation of cardiac contraction. MYBPC3 binds F-Actin, MHC and native thin filaments, and modifies the activity of Actin-activated myosin ATPase. Mutations in the MYBPC3 gene lead mainly to truncation of the protein, which results in one cause of familial hypertrophic cardiomyopathy type 4 (CMH4), a heart disorder characterised by ventricular hypertrophy, which often involves the interventricular septum and is usually asymmetric. The MYBPC3 gene maps to chromosome 11p11.2.

Supplier: Bioss

NUP160 is 1 of up to 60 proteins that make up the 120 MD nuclear pore complex, which mediates nucleoplasmic transport. NUP160 forms part of the Nup160 subcomplex in the nuclear pore which is composed of NUP160, Nup133, Nup107 and Nup96. This complex plays a role in RNA export and in tethering Nup98 and Nup153 to the nucleus. NUP160 is involved in poly(A)+ RNA transport.