"Bioss"

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This gene is a member of the Tyr protein kinase family and the epidermal growth factor receptor subfamily. It encodes a single-pass type I membrane protein with multiple cysteine rich domains, a transmembrane domain, a tyrosine kinase domain, a phosphotidylinositol-3 kinase binding site and a PDZ domain binding motif. The protein binds to and is activated by neuregulins and other factors and induces a variety of cellular responses including mitogenesis and differentiation. Multiple proteolytic events allow for the release of a cytoplasmic fragment and an extracellular fragment. Mutations in this gene have been associated with cancer. Alternatively spliced variants which encode different protein isoforms have been described; however, not all variants have been fully characterized. [provided by RefSeq, Jul 2008].

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Tumor suppressor serine/threonine-protein kinase that controls the activity of AMP-activated protein kinase (AMPK) family members, thereby playing a role in various processes such as cell metabolism, cell polarity, apoptosis and DNA damage response. Acts by phosphorylating the T-loop of AMPK family proteins, thus promoting their activity: phosphorylates PRKAA1, PRKAA2, BRSK1, BRSK2, MARK1, MARK2, MARK3, MARK4, NUAK1, NUAK2, SIK1, SIK2, SIK3 and SNRK but not MELK. Also phosphorylates non-AMPK family proteins such as STRADA, PTEN and possibly p53/TP53. Acts as a key upstream regulator of AMPK by mediating phosphorylation and activation of AMPK catalytic subunits PRKAA1 and PRKAA2 and thereby regulates processes including: inhibition of signaling pathways that promote cell growth and proliferation when energy levels are low, glucose homeostasis in liver, activation of autophagy when cells undergo nutrient deprivation, and B-cell differentiation in the germinal center in response to DNA damage. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton. Required for cortical neuron polarization by mediating phosphorylation and activation of BRSK1 and BRSK2, leading to axon initiation and specification. Involved in DNA damage response: interacts with p53/TP53 and recruited to the CDKN1A/WAF1 promoter to participate in transcription activation. Able to phosphorylate p53/TP53; the relevance of such result in vivo is however unclear and phosphorylation may be indirect and mediated by downstream STK11/LKB1 kinase NUAK1. Also acts as a mediator of p53/TP53-dependent apoptosis via interaction with p53/TP53: translocates to the mitochondrion during apoptosis and regulates p53/TP53-dependent apoptosis pathways. In vein endothelial cells, inhibits PI3K/Akt signaling activity and thus induces apoptosis in response to the oxidant peroxynitrite (in vitro). Regulates UV radiation-induced DNA damage response mediated by CDKN1A.

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Ubiquitin-like modifier involved in formation of autophagosomal vacuoles (autophagosomes). Plays a role in mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation. Promotes primary ciliogenesis by removing OFD1 from centriolar satellites via the autophagic pathway.

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SLK is a member of the serine/threonine kinase subfamily, Ste20. This subfamily is comprised of several mammalian kinases which exhibit sequence similarity to the Saccharomyces cerevisiae serine/threonine kinase Ste20, a protein involved in relaying signals from G protein-coupled receptors to cytosolic MAP kinase cascades. Members of this subfamily include KHS, GLK, YSK1, HPK1, Krs-1, Krs-2, GC kinase, HGK and SLK. SLK is a ubiquitously expressed protein that localizes to the cytoplasm and contains an N-terminal protein kinase domain, a central coiled-coil domain and a C-terminal ATH domain. SLK is activated through cleavage by caspase-3. SLK indirectly associates with microtubules and plays an important role in cellular stress, cell motility, cell death and cytoskeletal dynamics.

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Anti-TFF2 Rabbit Polyclonal Antibody

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Cystatin A and cystatin B (also designated PME, CST6, STFB, CPI-B, stefin B and liver thiol proteinase inhibitor) are thiol protease inhibitors that form complexes with papain and the cathepsins B, H, and L. Cystatin A, a cytoplasmic protein, is one of the precursor proteins of the cornified cell envelope in keratinocytes and plays a role in epidermal development and maintenance. Cystatin B protects against intracellular proteases leaking out of lysosomes and is primarily expressed in heart, liver and kidney.

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Mapping to chromosome 21, the FASP1 gene (FAPP1-associated protein 1) encodes a 233 amino acid protein that is homologous to the fission yeast protein Mis18. In yeast, Mis18 is localized to the centrosome and forms a complex with Mis16 to maintain the deacetylated state of histones specifically in the central core of centromeres. FASP1, also known as Protein Mis18-alpha and C21orf45, is required for the recruitment of CENP-A to centrosomes and is thereby essential for normal chromosome segregation during mitosis. With expression in testis, FASP1 exists as a homodimer, a heterodimer with MIS18B or is present in a complex containing other Mis18 family members. FASP1 has been shown to bind to pp5644 in Hela cells, where overexpression of pp5644 leads to inhibited growth and colony formation.

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Anti-KITLG Rabbit Polyclonal Antibody

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Gross cystic disease is a common premenopausal disorder in which gross cysts are the predominant pathologic lesion. It is characterized by production of a fluid secretion which accumulates in the breast cysts. Gross cystic disease fluid is a pathologic secretion from breast composed of several glycoproteins, including a unique 15 kDa monomer protein, GCDFP 15. The cells within the body that produce GCDFP 15 appear to be restricted primarily to those with apocrine function. Studies have found GCDFP 15 to be a highly specific and sensitive marker for breast cancer.

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Heterodimers between TCF3 and tissue-specific basic helix-loop-helix (bHLH) proteins play major roles in determining tissue-specific cell fate during embryogenesis, like muscle or early B-cell differentiation. Dimers bind DNA on E-box motifs: 5'-CANNTG-3'. Binds to the kappa-E2 site in the kappa immunoglobulin gene enhancer.

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May contribute to the regulation of translation during cell-cycle progression. May contribute to the regulation of cell proliferation.

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VAX2 is a 290 amino acid homeobox protein that plays a crucial role in development of the eye, particularly in the specification of the ventral optic vesicle and in establishment of a correct dorsoventral pattern. VAX2 acts as a transcription factor with VAX1 to cooperatively regulate retinal differentiation, neuroepithelial cell proliferation and axial polarization in the retina. Together, VAX1 and VAX2 repress transcription of Pax-6, a strong inducer of retinal development. VAX1 and VAX2 localize to the nucleus and contain one homeobox DNA-binding domain each.

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GEFT is a 580 amino acid cytoplasmic protein that is highly expressed in excitable tissues such as brain, heart and muscle, and weakly expressed in small intestine, colon, liver, placenta and lung. GEFT may play a role in actin cytoskeleton reorganization in different tissues since its activation induces formation of actin stress fibers. GEFT works as a guanine nucleotide exchange factor for the Rho family of small GTPases and links specifically to G alpha q/11-coupled receptors in Rho A activation. GEFT is an important regulator of processes involved in axon and dendrite formation. Involved in skeletal myogenesis, GEFT seems to be an exchange factor primarily for Rac 1 in neurons. Existing as two alternatively spliced variants, GEFT contains a DH (DBL-homology) domain and a PH domain.

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Hemostasis following tissue injury involves the deployment of essential plasma procoagulants (prothrombin, and factors X, IX, V, and VIII), which are involved in a blood coagulation cascade that leads to the formation of insoluble fibrin clots and the promotion of platelet aggregation (1-3). Coagulation factor IX (plasma thromboplastic component, F9, F.IX, HEMB) is a vitamin K-dependent, single chain serine protease that is synthesized in the liver and circulates as an inactive precursor (3,4). Factor XIa mediated proteolytic cleavage of factor IX generates factor IXa, an active serine protease composed of a 145 amino acid light chain and a 236 amino acid catalytic heavy chain, linked through disulfide bonds (5). Genetic alterations at the Factor IX locus such as point mutations, insertions and deletions, can lead to hemophilia B, also known as Christmas disease (6).

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This gene encodes a 105 kD protein which can undergo cotranslational processing by the 26S proteasome to produce a 50 kD protein. The 105 kD protein is a Rel protein-specific transcription inhibitor and the 50 kD protein is a DNA binding subunit of the NF-kappa-B (NFKB) protein complex. NFKB is a transcription regulator that is activated by various intra- and extra-cellular stimuli such as cytokines, oxidant-free radicals, ultraviolet irradiation, and bacterial or viral products. Activated NFKB translocates into the nucleus and stimulates the expression of genes involved in a wide variety of biological functions. Inappropriate activation of NFKB has been associated with a number of inflammatory diseases while persistent inhibition of NFKB leads to inappropriate immune cell development or delayed cell growth. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Sep 2009].

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Functions as a negative regulator of TGF-beta Signalling and thereby probably plays a role in cell proliferation, differentiation, apoptosis, motility, extracellular matrix production and immunosuppression. In the canonical TGF-beta pathway, ZFYVE9/SARA recruits the intracellular signal transducer and transcriptional modulators SMAD2 and SMAD3 to the TGF-beta receptor. Phosphorylated by the receptor, SMAD2 and SMAD3 then form a heteromeric complex with SMAD4 that translocates to the nucleus to regulate transcription. Through interaction with SMAD2 and SMAD3, LDLRAD4 may compete with ZFYVE9 and SMAD4 and prevent propagation of the intracellular signal.