"Bioss"

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The Thrombospondin proteins, Thrombospondins 1-4 and Thrombospondin 5 (also designated COMP), compose a family of glycoproteins that are involved in cell-to-cell and cell-to-matrix signaling. These extracellular, cell-surface proteins form complexes of both homo- and heteromultimers. Spondin-2, or Mindin, is also designated DIL-1 for its differential expression in cancerous and non-cancerous lung cells. Full-length SPON2 cDNA encodes a 331 amino acid protein with a domain arrangement similar to zebrafish F-Spondin and Mindin-1/Mindin-2: an FS1 domain, an FS2 domain, a hydrophobic signal sequence in the N-terminus and a Thrombospondin type I repeat. Immunoblot analysis demonstrates expression of dimers and oligomers in a concentration-dependent manner under nonreducing conditions.

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This gene belongs to the Ras oncogene family, whose members are related to the transforming genes of mammalian sarcoma retroviruses. The products encoded by these genes function in signal transduction pathways. These proteins can bind GTP and GDP, and they have intrinsic GTPase activity. This protein undergoes a continuous cycle of de- and re-palmitoylation, which regulates its rapid exchange between the plasma membrane and the Golgi apparatus. Mutations in this gene cause Costello syndrome, a disease characterized by increased growth at the prenatal stage, growth deficiency at the postnatal stage, predisposition to tumor formation, mental retardation, skin and musculoskeletal abnormalities, distinctive facial appearance and cardiovascular abnormalities. Defects in this gene are implicated in a variety of cancers, including bladder cancer, follicular thyroid cancer, and oral squamous cell carcinoma. Multiple transcript variants, which encode different isoforms, have been identified for this gene. [provided by RefSeq].

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General activator of RNA polymerase which utilises different TFIIIB complexes at structurally distinct promoters. The isoform 1 is involved in the transcription of tRNA, adenovirus VA1, 7SL and 5S RNA. Isoform 2 is required for transcription of the U6 promoter.

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Pancreatic lipase, is involved in the hydrolysis of dietary triglycerides to fatty acids in the intestine. This hydrolysis, which is initiated in the stomach by gastric lipase, is essential for the intestinal absorption of long-chain triglyceride fatty acids.

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Streptococcus suis serotype 2 (SS2) infection has become a public health concern due to its zoonotic capability to cause severe infections in slaughterhouse workers and those who handle infected pork.

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Anti-C7orf63 Rabbit Polyclonal Antibody

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Anti-PALB2 Rabbit Polyclonal Antibody

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Hexosaminidase B is the beta subunit of the lysosomal enzyme beta-hexosaminidase that, together with the cofactor GM2 activator protein, catalyzes the degradation of the ganglioside GM2, and other molecules containing terminal N-acetyl hexosamines. Beta-hexosaminidase is composed of two subunits, alpha and beta, which are encoded by separate genes. Both beta-hexosaminidase alpha and beta subunits are members of family 20 of glycosyl hydrolases. Mutations in the alpha or beta subunit genes lead to an accumulation of GM2 ganglioside in neurons and neurodegenerative disorders termed the GM2 gangliosidoses. Beta subunit gene mutations lead to Sandhoff disease (GM2-gangliosidosis type II). [provided by RefSeq, Jul 2008].

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RNF35 belongs to the TRIM/RBCC family.

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Encoding over 300 genes, chromosome 18 contains about 76 million bases. Trisomy 18, or Edwards syndrome, is the second most common trisomy after Downs syndrome. Symptoms of Edwards syndrome include low birth weight, a variety of physical development defects, heart deformations and breathing difficulty. Translocation between chromosome 18 and 14 is the most common translocation in cancers, and occurs in follicular lymphomas. Niemann-Pick disease, hereditary hemorrhagic telangiectasia and erythropoietic protoporphyria are associated with chromosome 18. The TGFβ modulators, Smad2, Smad4 and Smad7 are encoded by chromosome 18. The C18orf54 gene product has been provisionally designated C18orf54 pending further characterization.

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Diversin, also known as ANKRD6 (ankyrin repeat domain 6), is a 727 amino acid protein that contains eight ankyrin repeats and belongs to the ankyrin repeat domain protein family. Members of the ankyrin repeat domain family facilitate protein-protein interactions and function as adaptors of signaling pathways. Expressed in a developmentally-regulated manner and at highest levels in the brain, Diversin is believed to play a role in brain development. Via its ankyrin repeats, Diversin can directly interact with Dvl (dishevelled), an interaction that is essential for the activation of noncanonical Wnt signaling. In addition, Diversin contains a C-terminal domain that binds Axin/Conductin and a casein kinase-binding domain in its central region that specifically binds casein kinase Ié. Through the action of these additional domains, Diversin may also facilitate canonical Wnt signaling. Due to alternative splicing events, three Diversin isoforms exist.

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Eukaryotic RNA polymerase II mediates the synthesis of mature and functional messenger RNA. This is a multistep process, called the transcription cycle, that includes five stages: preinitiation, promoter, clearance, elongation and termination. Elongation is thought to be a critical stage for the regulation of gene expression. ELL (11-19 lysine-rich leukemia protein), also designated MEN, functions as an RNA polymerase II elongation factor that increases the rate of transcription by suppressing transient pausing by RNA polymerase II. It is also thought to regulate cellular proliferation. ELL is abundantly expressed in peripheral blood leukocytes, skeletal muscle, placenta and testis, with lower expression in spleen, thymus, heart, brain, lung, kidney, liver and ovary. ELL3 is a 397 amino acid nuclear protein that functions as an RNA polymerase II elongation factor that increases the rate of transcription by suppressing transient pausing by RNA polymerase II. Though similar to ELL and ELL2, ELL3 is exclusively expressed in testis.

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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. RNF10 (ring finger protein 10), also known as RIE2, is an 811 amino acid protein that localizes to the cytoplasm and contains one RING-type zinc finger. Existing as multiple alternatively spliced isoforms, RNF10 interacts with MOX-2 and is thought to regulate its transcription in schwann cells, possibly playing a role in myelin formation. The gene encoding RNF10 maps to human chromosome 12, which encodes over 1,100 genes and comprises approximately 4.5% of the human genome. Chromosome 12 is associated with a variety of diseases and afflictions, including hypochondrogenesis, achondrogenesis, Kniest dysplasia, Noonan syndrome and Trisomy 12p, which causes facial developmental defects and seizure disorders.

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MP1 (MEK partner 1) functions as a scaffolding protein in the mitogen activated protein (MAP) kinase signaling pathway. Growth factor induced MAP kinase activation is selectively mediated by the extracellular signal-regulated kinase (ERK) cascade. MAPBPIP (mitogen-activated protein-binding protein-interacting protein), also known as p14 and late endosomal/lysosomal MP1-interacting protein, functions as an adaptor protein augmenting the regulation of the MAP kinase cascade. Partner proteins MAPBPIP and MP1 are structurally almost identical each with a five-stranded -sheet flanked between a two-helix and one-helix layer. MAPBPIP compels the recruitment of MP1 to late endosomes where they form a very stable heterodimeric complex required for ERK activation on endosomes. Knockdown of the individual proteins in the MP1/MAPBPIP complex resulted in decreased expression of the partner proteins which implies greater stability of the heterodimeric complex than either MP1 or MAPBPIP individually. Early research suggests the MP1-MAPBPIP-MEK-1 signaling complex may be critical in the regulation of tissue homeostasis.

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Anti-VSIG4 Rabbit Polyclonal Antibody

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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.