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Asialoglycoprotein Receptor 2 (ASGR2) is a hetero-oligomeric protein comprised of major and minor subunits, encoded by different genes. ASGR2 is a subunit of the asialoglycoprotein receptor; it is the less abundant minor subunit. The ASGR2 receptor is a transmembrane protein, which has a crucial role in serum glycoprotein homeostasis by mediating the endocytosis and lysosomal degradation of glycoproteins with exposed terminal galactose or N-acetylgalactosamine residues.

Argininosuccinate lyase (ASL) is a member of the lyase 1 family. ASL is an enzyme which catalyzes the reversible breakdown of Argininosuccinate (ASA) yielding the amino acids arginine and fumarate. ASL which is located in the liver cytosol is the 4th enzyme of the urea cycle and involved in the biosynthesis of arginine in all species and the production of urea in ureotelic species. While Argininosuccinate synthetase (ASS) catalyzes the formation of argininosuccinate from citrulline and aspartate, ASL breaks down the newly formed argininosuccinate into L-arginine and fumarate. L-arginine continues within the urea cycle to form urea and orinthine, whereas fumarate can enter the citric acid cycle. ASL gene Mutations result in the autosomal recessive disorder argininosuccinic aciduria, or argininosuccinic acid lyase deficiency.

ASMT is a member of the methyltransferase superfamily. ASMT participates in melatonin biosynthesis. ASMT Expressed in brain, retina and pineal gland, ASMT utilities to catalyze the final reaction in the synthesis of melatonin, particularly the conversion of S-adenosyl-L-methionine and N-acetylserotonin to S-adenosyl-Lhomocysteine and melatonin.

ArsA Arsenite Transporter, ATP-Binding, Homolog 1 (ASNA1) is a part of the arsA ATPase family. ASNA1 is the human homolog of the bacterial arsA gene. ArsA ATPase is the catalytic component of a multisubunit oxyanion pump In E.coli, which is in charge for resistance to arsenicals and antimonials. ASNA1 is also a main component of a transmembrane domain (TMD) recognition complex (TRC) which is involved in the post-translational delivery of tail-anchored (TA) proteins from the cytosol to the endoplasmic reticulum (ER).

ArsA Arsenite Transporter, ATP-Binding, Homolog 1 (ASNA1) is a part of the arsA ATPase family. ASNA1 is the human homolog of the bacterial arsA gene. ArsA ATPase is the catalytic component of a multisubunit oxyanion pump In E.coli, which is in charge for resistance to arsenicals and antimonials. ASNA1 is also a main component of a transmembrane domain (TMD) recognition complex (TRC) which is involved in the post-translational delivery of tail-anchored (TA) proteins from the cytosol to the endoplasmic reticulum (ER).

The AsnRS enzyme is a member of the ligases family, specifically those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. An asparagine-tRNA ligase is an enzyme which catalyzes the chemical reaction: ATP + L-asparagine + tRNAAsn AMP + diphosphate + L-asparaginyl-tRNAAsn. The three substrates of the AsnRS enzyme are ATP, L-asparagine, and tRNA(Asn), whereas its three products are AMP, diphosphate, and L-asparaginyl-tRNA(Asn).

Asparagine synthetase (ASNS) is a cytoplasmic enzyme that turns aspartate toasparagine and functions mostly in mammalian organs. ASNS is responsible for cell growthand its mRNA content is associated with changes in the cell cycle. ASNS may also play a role as a biomarker for ovarian cancer.

Aspartoacylas or ASPA, is a protein, found in several tissues such as skeletal muscle, cerebral white matter, kidney, liver & lungs. ASPA is a homodimer that catalyses the deacetylation of Nacetylaspartic acid. In order to create L-aspartate & acetate.

Aspartoacylase is a homodimer which catalyzes the deacetylation of N-acetylaspartic acid (NAA) (a protein whose hydrolysis is crucial to maintenance of intact white matter) to generate acetate and L-aspartate. Aspartoacylase (ASPA) is expressed in the liver, lung and kidney tissue, as well as in the skeletal muscle and in cerebral white matter. NAA is ample in the brain where hydrolysis by aspartoacylase is believed to aid maintain white matter. In other tissues ASPA functions as a scavenger of NAA from body fluids. ASPA gene mutations cause Canavan disease (CAND or spongy degeneration of the brain).

ASPH hydroxylates an Asp or Asn residue in EGF domains. ASPH is involved in calcium homeostasis. ASPH is expressed from two promoters and goes through extensive alternative splicing. The encoded set of ASPH proteins share varying quantities of overlap near their N-termini although have considerable differences in their C-terminal domains resulting in distinct functional properties. The longest isoforms (a and f) include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the EGF domain, including protein C, coagulation factors VII, IX, and X, and the complement factors C1R and C1S. Further isoforms diverge mainly in the C-terminal sequence and lack the hydroxylase domain, and some have been localized to the endoplasmic and sarcoplasmic reticulum.

Aspartate Beta-Hydroxylase Domain Containing 1, also known as ASPHD1 is a part of the aspartyl/asparaginyl beta-hydroxylase family. ASPHD1 is a protein coding gene.

Aspartic Peptidase, Retroviral-Like 1 (ASPRV1) is a protein which contains one peptidase A2 domain. ASPRV1 undergoes autocleavage which is essential for activation of the protein. ASPRV1 is expressed mostly in the granular layer of the epidermis and inner root sheath of hair follicles and localized to membrane region. In the psoriatic skin, ASPRV1 is expressed throughout the stratum corneum. In the ulcerated skin, ASPRV1 is expressed in the stratum granulosum of intact epidermis; however it is virtually nonexistent from ulcerated regions. In addition, ASPRV1 is expressed in differentiated areas of squamous cell carcinomas but not in the undifferentiated tumors.

Alveolar Soft Part Sarcoma Chromosome Region, Candidate 1 (ASPSCR1) contains a UBX domain and interacts with glucose transporter type 4 (GLUT4). ASPSCR1 is a tether, which sequesters the GLUT4 in intracellular vesicles in muscle and fat cells, and redistributes the GLUT4 to the plasma membrane. Translocation t(X;17)(p11;q25) of this ASPSCR1 with transcription factor TFE3 gene ends with a ASPSCR1-TFE3 fusion protein in alveolar soft part sarcoma and in renal cell carcinomas.

ASRGL1 is a 308 amino acid protein which is a member of the Ntn-hydrolase family. ASRGL1 is an autoantigenic protein which is present in the mid-piece of sperm after obstruction of the male reproductive tract. ASRGL1 is expressed highly in the testis, but is also expressed in the brain, kidney and gastrointestinal tissues. High levels of ASRGL1 are also detected in ovarian, uterine and mammary tumors in comparison with normal tissues of the same origin.

ASS1 is involved in the urea cycle, which is a sequence of chemical reactions that is localized in liver cells. The urea cycle processes excess nitrogen that is generated as the body uses proteins. The surplus nitrogen is used to create a molecule called urea, which is excreted from the body in urine.

ASS1 is involved in the urea cycle, which is a sequence of chemical reactions that is localized in liver cells. The urea cycle processes excess nitrogen that is generated as the body uses proteins. The surplus nitrogen is used to create a molecule called urea, which is excreted from the body in urine.

Astroviruses are the main cause of gastroenteritis in children and elderly adults. Astroviruses are associated with 5–9% of cases of gastroenteritis in young children. The virus is found in faecal matter and in epithelial intestinal cells. Astrovirus’s main transmission is by contaminated food or water.

Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity.
Bovine Transferrin is a crucial component for the cultivation of mammalian cells in- vitro. Bovine Transferrin is Critical for long-term cells growth in-vitro. Bovine Transferrin is used as detoxificant in media by binding contaminating metal ions. Bovine Transferrin is often used as a nutrient in fermentation media for recombinant protein and biopharmaceutical production. Additional common uses of Bovine Transferrin are Molecular weight, Affinity purification of anti-human transferrin antibodies and also as receptor mediated transfection of molecules such as DNA, into cells.

Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity.
Human Transferrin is a crucial component for the cultivation of mammalian cells in-vitro. Human Transferrin is Critical for long-term cells growth in-vitro. Human Transferrin is used as detoxificant in media by binding contaminating metal ions. Human Transferrin is often used as a nutrient in fermentation media for recombinant protein and biopharmaceutical production. Additional common uses of Human Transferrin areMolecular weight, Affinity purification of anti-human transferrin antibodies and also as receptor mediated transfection of molecules such as DNA, into cells.

ATF1, a cyclic-AMP dependent transcription factor, is expressed in a large selection of cell types and can dimerize with CREB. MSK1 and MSK2 protein kinases are essential for the stress-induced phosphorylation of transcription factors CREB and ATF1 in primary embryonic fibroblasts. Epidermal growth factor induction of c-jun expression needs ATF1 and MEF2 sites in the c-jun promoter.

ATF3 belongs to the mammalian activation transcription factor/cAMP responsive element-binding (CREB) protein family of transcription factors. ATF3 binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AC][AG]-3'), a sequence present in numerous viral and cellular promoters. Multiple transcript variants encoding two different isoforms are known for this gene. The longer isoform represses transcription from promoters with ATF binding elements instead of activating it. The shorter isoform (deltaZip2) which stimulates transcription by sequestering inhibitory co-factors away from the promoter has no leucine zipper protein-dimerization motif and does not bind to DNA.

Activating transcription factor 4 (ATF4) is a member of a family of DNA-binding proteins which includes the AP-1 family of transcription factors, cAMP-response element binding proteins and CREB-like proteins. The ATF4 gene encodes a transcription factor which was initially identified as a widely expressed mammalian DNA binding protein that could bind a tax-responsive enhancer element in the LTR of HTLV-1.

Ubiquitin-like-conjugating enzyme ATG10 (ATG10) is a 220 amino acid protein which localizes to the cytoplasm and has a role in autophagy, specifically acting as an E2-like enzyme providing Atg recognition sites during autophagosome synthesis. ATG10 functions as an E2-like enzyme which catalyzes the conjugation of ATG12 to ATG5, which is required for autophagy. In addition, ATG10 interacts with ATG12 in human embryonic kidney cells in the presence of ATG7. ATG10 probably serves as an ATG5-recognition molecule. Furthermore, ATG10 has a role in adenovirus-mediated cell lysis.

Autophagy Related 3 (ATG3) is a conjugating enzyme essential for the cytoplasm to vacuole transport (Cvt), autophagy, and mitochondrial homeostasis. ATG3 is localizes to the cytoplasm and is expressed in tissues with predominant levels found in kidney, placenta, liver, heart and skeletal muscle. ATG3 catalyzes a reaction which is necessary for autophagy. That reaction is the formation of the Atg8-phosphatidylethanolamine (ATG-PE) conjugate.

Autophagy Related 3 (ATG3) is a conjugating enzyme essential for the cytoplasm to vacuole transport (Cvt), autophagy, and mitochondrial homeostasis. ATG3 is localizes to the cytoplasm and is expressed in tissues with predominant levels found in kidney, placenta, liver, heart and skeletal muscle. ATG3 catalyzes a reaction which is necessary for autophagy. That reaction is the formation of the Atg8-phosphatidylethanolamine (ATG-PE) conjugate.

Cysteine protease ATG4B (ATG4B) belongs to the autophagin protein family. Autophagy is the manner by which endogenous proteins and damaged organelles are destroyed intracellularly. Autophagy is vital for cell homeostasis and cell remodeling during differentiation, metamorphosis, non-apoptotic cell death, and aging. ATG4B is a cysteine protease necessary for autophagy, which cleaves the C-terminal part of either MAP1LC3, GABARAPL2 or GABARAP, allowing the liberation of form I. A subpopulation of form I is then transformed to a smaller form (form II). Form II, with an exposed C-terminal glycine, is deemed to be the phosphatidylethanolamine (PE)-conjugated form, and is capable of binding to autophagosomes. Reduced levels of autophagy are seen in some malignant tumors; therefore autophagy may have a role in controlling the unregulated cell growth linked to cancer.

ATG5 is a member of the autophagy-related (ATG) genes family. Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents. ATG5 protein is essential for autophagy. It conjugates to ATG12 and associates with isolation membrane to form autophagosomes. In addition ATG5 takes a vital part in the apoptotic process and it is expressed relatively late in the apoptotic process, downstream of caspase activity.

ATOH1 activates E box-dependent transcription in collaboration with TCF3/E47, but the activity is entirely provoked by the negative regulator of neurogenesis HES1. ATOH1 takes part in the differentiation of divisions of neural cells by activating E box-dependent transcription.

Atosiban is the first oxytocin antagonist to be specifically developed for the treatment of preterm labor. Atosiban has a specific mode of action, inhibiting oxytocin-induced uterine contractions by blocking oxytocin receptors in the uterus. Extensive clinical investigations have shown Atosiban to be at least as effective as current tocolytic agents. In addition, due to its novel and specific mode of action, Atosiban has a markedly improved maternal side effects profile compared with conventional therapies.

ATOX1 is a metal transport protein that is part of the ATX1 family. ATOX1 is a copper chaperone that takes part in cellular antioxidant defense and can bind and deliver cytosolic copper to the copper ATPase proteins in the trans-Golgi network for later incorporation to the ceruloplasmin. ATOX1 plays a role as an antioxidant against superoxide and hydrogen peroxide, and consequently, takes an important part in cancer carcinogenesis. Because of ATOX1 cytogenetic location, the gene can be a good a candidate gene for 5q-syndrome.

ATPaseTransporting Beta 1 (ATP1B1) is a part of the family of Na+/K+ and H+/K+ ATPases beta chain proteins, and the subfamily of Na+/K+ -ATPases. Na+/K+ -ATPase is an essential membrane protein accountable for establishing and maintaining the electrochemical gradients of Na and K ions over the plasma membrane. These gradients are vital for osmoregulation, for sodium-coupled transport of a range of organic and inorganic molecules, and for electrical excitability of muscle and nerve. ATP1B1is combined of 2 subunits, a large catalytic subunit (alpha) and a smaller glycoprotein subunit (beta). The beta subunit regulates the number of sodium pumps transported to the plasma membrane through assembly of alpha/beta heterodimers. ATP1B1 is a beta 1 subunit.

ATPase Transporting Beta 1 (ATP1B1) is a part of the family of Na+/K+ and H+/K+ ATPases beta chain proteins, and the subfamily of Na+/K+ -ATPases. Na+/K+ -ATPase is an essential membrane protein accountable for establishing and maintaining the electrochemical gradients of Na and K ions over the plasma membrane. These gradients are vital for osmoregulation, for sodium-coupled transport of a range of organic and inorganic molecules, and for electrical excitability of muscle and nerve. ATP1B1is combined of 2 subunits, a large catalytic subunit (alpha) and a smaller glycoprotein subunit (beta). The beta subunit regulates the number of sodium pumps transported to the plasma membrane through assembly of alpha/beta heterodimers. ATP1B1 is a beta 1 subunit.

ATPaseTransporting Beta 2 (ATP1B2) is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na+ and K+ ions across the plasma membrane. The precise function of the beta-2 subunit is not known. The ATP1B2 protein is composed of 3 subunits: alpha (catalytic), beta and gamma.

ATPaseTransporting Beta 2 (ATP1B2) is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na+ and K+ ions across the plasma membrane. The precise function of the beta-2 subunit is not known. The ATP1B2 protein is composed of 3 subunits: alpha (catalytic), beta and gamma.

ATPaseTransporting Beta 3 (ATP1B3) is a member of the X(+)/potassium ATPases subunit beta family. ATP1B3 is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na+ and K+ ions across the plasma membrane. The beta subunit controls, by way of assembly of alpha/beta heterodimers, the quantity of sodium pumps transported to the plasma membrane. The precise role of the beta-3 subunit is unknown.

ATP synthase subunit gamma, mitochondrial isoform L (liver) (ATP5C1) is a member of the ATPase gamma chain family. ATP5C1 catalyzes ATP synthesis by using an electrochemical gradient of protons across the inner membrane throughout oxidative phosphorylation. The catalytic portion of mitochondrial ATP synthase is comprised of 5 different subunits (alpha, beta, gamma, delta, and epsilon) gathered with a stoichiometry of 3 alpha, 3 beta, and a single representative of the other 3.

F-ATPase delta (ATP5D) catalyzes ATP synthesis, employing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. ATP synthase is composed of 2 linked multi-subunit complexes: F1-the soluble catalytic core and Fo- the membrane-spanning component, which comprise the proton channel. The catalytic portion of mitochondrial ATP synthase consists of five different subunits (alpha, beta, gamma, delta, and epsilon) assembled with a stoichiometry of 3 alphas, 3 betas, and a single representative of the other three. The proton channel consists of three main subunits-a, b, c. ATP5D is the delta subunit of the catalytic core.

ATP5F1 is a mitochondrial ATP synthase subunit catalyzes ATP synthesis, using an electrochemical gradient of protons all through the inner membrane for the duration of the oxidative phosphorylation. ATP synthase is comprised of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, including the proton channel. The catalytic segment of mitochondrial ATP synthase contains 9 subunits: 3 alpha, 3 beta, and one unit of gamma, delta, and epsilon. The proton route is known to have 9 subunits (a, b, c, d, e, f, g, F6 and 8).

ATP5H is a member of the ATPase d subunit family and encodes the d subunit of the F0 complex. Electron transport complexes of the respiratory chain create a proton gradient across the membrane which induces ATP5H to transform ADP to ATP. Two alternatively spliced isoforms of ATP5H, encoded by a gene that maps to human chromosome 17q25.1, are known. ATP5H is restricted to mitochondrial inner membrane.

ATP synthase subunit O (ATP5O) localizes to the mitochondria and catalyzes ATP synthesis. ATP5O is a component of the F-type ATPase found in the mitochondrial matrix. F-type ATPases are composed of a catalytic core and a membrane proton channel. ATP5O seems to be part of the connector connecting these two components and may be involved in transmission of conformational changes or proton conductance.

ATPase Transporting Lysosomal Accessory Protein 2 (ATP6AP2) is a protein associated with triphosphatases (ATPases). Proton-translocating ATPases have vital roles in energy conservation, secondary active transport, acidification of intracellular compartments, and cellular pH homeostasis. ATP6AP2 is linked with the transmembrane sector of the V-type ATPases, which have a transmembrane proton-conducting sector and an extramembrane catalytic sector. ATP6AP2 serves as a renin and prorenin cellular receptor; it mediates renin-dependent cellular responses by activating ERK1 and ERK2. ATP6AP2 is expressed in the brain, heart, placenta, liver, kidney and pancreas. ATP6AP2 is hardly detectable in the lung and skeletal muscles. ATP6AP2 is also expressed in the vascular structures and by syncytiotrophoblast cells in the mature fetal placenta.

ATPase Transporting, Lysosomal V1 Subunit F (ATP6V1F) is a component of vacuolar ATPase (V-ATPase); it is a multi-subunit enzyme, which mediates acidification of eukaryotic intracellular organelles. V-ATPase dependent organelle acidification is required for such intracellular processes as protein sorting, zymogen activation, receptor-mediated endocytosis, and synaptic vesicle proton gradient generation. V-ATPase is comprised of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain contains 3 A and 3 B subunits, 2 G subunits as well as the C, D, E, F, and H subunits. The V1 domain has the ATP catalytic site. The V0 domain consists of 5 different subunits: a, c, c', c', and d.

ATPase inhibitory factor 1 (ATPIF1) attaches to the C-terminal region of a beta subunit of the F1-ATPase at low pH values and, through interference of the beta and gamma subunit interaction, ATPIF1 controls the activity of the F1 (the hydrophilic catalytic core), F0 (the membrane embedded protein channel) ATPase. ATPIF1 overexpression in a number of human carcinomas additionally reinforces its participation in oncogenesis and offers insight into the transformed metabolism of cancer cells, including the reprogramming of energy metabolism in relation to glycolysis. Endogenous F1F(o)-ATPase inhibitor curbing ATP depletion when the mitochondrial membrane potential drops below a threshold and the F1F(o)-ATP synthase begins hydrolyzing ATP to pump protons out of the mitochondrial matrix.

Ataxin 3 is otherwise known as Machado-Joseph disease protein 1. Machado–Joseph disease is a hereditary autosomal dominant neurodegenerative disorder. ATXN3 contains trinucleotide CAG repeats in the coding region, and the expansion of these repeats from the normal 13-36 to 68-79 causes the Machado-Joseph disease. ATXN3 is a poly-ubiquitin-binding protein whose cellular turnover is regulated by its catalytic activity.
In addition, ATXN3 is a proteasome-associated factor which mediates the degradation of ubiquitinated proteins. ATXN3 folds reversibly using a single intermediate; partial destabilization of ATXN3 by chemical denaturation causes the formation of fibrillar aggregates by the non-pathological variant.
Ataxin-3 interacts with the major histone acetyltransferases cAMP-response-element binding protein (CREB)-binding protein, p300, and p300/CREB-binding protein-associated factor and hinders transcription by these coactivators.

Mitochondrial methylglutaconyl-CoA hydratase (AUH) is involved in the amino acid degradation pathway by catalyzing the conversion of 3-methylglutaconyl-CoA to 3-hydroxy-3-methylglutaryl-CoA and water. AUH Human is expressed as a single mRNA species of 1.8 kb, and translated as a 40kDa precursor protein which is consequently processed to a 32kDa mature form. AUH has a very low enoyl-CoA hydratase activity. The AUH protein binds to the AU-rich element (ARE), which is a common element found in the 3' UTR of rapidly decaying mRNA such as c-fos, c-myc and granulocyte/ macrophage colony stimulating factor. AU-rich elements are involved in directing RNA to rapid degradation and deadenylation. In addition, AUH is homologous to enol-CoA hydratase, which is an enzyme involved in fatty acid degradation, and has been shown to have intrinsic hydratase enzymatic activity. AUH is therefore a bifunctional chimera between RNA binding and metabolic enzyme activity.

AURKA (Aurora Kinase A) belongs to the mitotic serine/threonine kinases family. AURKA is a cell cycle-regulated kinase which may be involved in microtubule formation and/or stabilization at the spindle pole during chromosome segregation. AURKA is found at the centrosome in interphase cells and at the spindle poles in mitosis. Since the AURKA expression is cell-cycle regulated, it is low in G1/S, it accumulates during G2/M, and it decreases rapidly after. AURKA is involved in important processes during mitosis and meiosis whose proper function is essential for healthy cell proliferation. In addition, AURKA plays an essential role in tumourigenesis and is overexpressed in various types of cancers. AURKA is strongly expressed in the testis, colon, ovarian, prostate, neuroblastoma, breast and cervical cancer cell lines and weakly in skeletal muscle, thymus and spleen. AURKA interacts with its substrates BORA and ARHGEF2, as well as with TACC1 and CPEB1.
Defects in the AURKA gene cause numerical centrosome aberrations including aneuploidy. AURKA overexpression has been linked to chromosomal instability in colorectal cancer. AURKA expression may have a prognostic significance in ovarian carcinoma.

Aurora Kinase B (AURKB) belongs to a family of mitotic serine/threonine kinases. AURKB connects with chromosomes for the period of prophase prior to relocalizing to the spindle at anaphase. AURKB localizes to microtubules near kinetochores, specifically to the specialized microtubules called K-fibers. AURKB controls chromosome segregation through the control of microtubule-kinetochore attachment and cytokinesis. AURKB is required for kinetochore localization of BUB1 and SGOL1. AURKB expression during the G2/M phase transition is firmly coordinated with histone H3 phosphorylation, while overexpression is seen in many kinds of cancers. AURKB phosphorylates ''Ser-10'' and ''Ser-28'' of histone H3 during mitosis. AURKB is a component of the CPC (chromosomal passenger complex), which is a complex that acts as a key regulator of mitosis. High level expression of AURKB is seen in the thymus, which is also expressed in the spleen, lung, testis, colon, placenta and fetal liver. AURKB is expressed during S and G2/M phase and expression is up-regulated in cancer cells during M phase.

Aurora Kinase B (AURKB) belongs to a family of mitotic serine/threonine kinases. AURKB connects with chromosomes for the period of prophase prior to relocalizing to the spindle at anaphase. AURKB localizes to microtubules near kinetochores, specifically to the specialized microtubules called K-fibers. AURKB controls chromosome segregation through the control of microtubule-kinetochore attachment and cytokinesis. AURKB is required for kinetochore localization of BUB1 and SGOL1. AURKB expression during the G2/M phase transition is firmly coordinated with histone H3 phosphorylation, while overexpression is seen in many kinds of cancers. AURKB phosphorylates 'Ser-10' and 'Ser-28' of histone H3 during mitosis. AURKB is a component of the CPC (chromosomal passenger complex), which is a complex that acts as a key regulator of mitosis.
High level expression of AURKB is seen in the thymus, which is also expressed in the spleen, lung, testis, colon, placenta and fetal liver. AURKB is expressed during S and G2/M phase and expression is up-regulated in cancer cells during M phase.

Avidin is a tetrameric protein of 4 identical subunits (homotetramer) each of which can bind to biotin with a high degree of affinity and specificity. Avidin molecular weight in its tetrameric form is estimated to be between 66-69 kDa. Avidin is produced in the oviducts of birds, reptiles and amphibians and is subsequently deposited in the whites of their eggs. In the chicken egg white, avidin makes up roughly 0.05% of total protein (approximately 1.8 mg per egg). 10% of Avidin’s molecular weight is ascribed to carbohydrate content which is composed of four to five mannose and three N-acetylglucosamine residues. Avidin has at least three distinctive oligosaccharide structural type which are similar in structure and composition. The dissociation constant (KD) of avidin is approximately 10-15M, making it one of the strongest known non-covalent bonds.

Avidin is a tetrameric protein of 4 identical subunits (homotetramer) which can bind to biotin with a high degree of affinity and specificity. The estimated molecular weight of Avidin in its tetrameric form is between 66-69 kDa. Avidin is produced in the oviducts of birds, reptiles and amphibians and is subsequently deposited in the whites of their eggs. In the chicken egg white, avidin makes up roughly 0.05% of total protein (approximately 1.8 mg per egg). 10% of Avidin’s molecular weight is ascribed to carbohydrate content which is composed of 4-5 mannose and 3 N-acetylglucosamine residues. Avidin has at least three distinctive oligosaccharide structural type which are similar in structure and composition. The dissociation constant (KD) of avidin is approximately 10-15M, making it one of the strongest known non-covalent bonds.