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Ganciclovir (GCV) is a pro-drug nucleoside analog that is activated by phosphorylation. It is useful in the study of gene therapy in cancer research.
Ganciclovir is a synthetic analogue of 2'-deoxy-guanosine. It is initially phosphorylated to a deoxyguanosine triphosphate (dGTP) analogue. This mechanism competitively inhibits the integration of dGTP by viral DNA polymerase, resulting in the termination of elongation of viral DNA. Upon expression of a viral suicide gene encoding thymidine kinase, the non-toxic pro-drug is converted to a phosphorylated active analog and is incorporated into the DNA of replicating eukaryotic cells, causing death of the malignant dividing cell. The cell cycle is irreversibly arrested at the G2-M checkpoint. Gap junction involvement in the ganciclovir bystander effect has been studied. Ganciclovir has been used to study loss of telomeres and to evaluate sensitivity of viruses to antiviral treatments.
Ganciclovir is used in molecular biology for selection against random recombination events when homologous recombination of a gene of interest is required.

IGFBP6 plays a role in lipoprotein assembly and dietary cholesterol absorption. in addition to its acyltransferase activity, it may act as a ligase. may provide cholesteryl esters for lipoprotein secretion from hepatocytes and intestinal mucosa.

CACYBP (calcyclin binding protein) participates in calcium-dependent ubiquitination and subsequent proteosomal degradation of target proteins. CACYBP acts as a molecular bridge in ubiquitin E3 complexes. CACYBP is involved in the ubiquitin-mediated degradation of beta-catenin.

Complement Component 4 Binding Protein, Beta (C4BPB) belongs to a superfamily of proteins composed primarily of tandemly arrayed short consensus repeats of approximately 60 amino acids. C4BPB has a regulatory role in the coagulation system also, mediated via the beta-chain binding of protein S, a vitamin K-dependent protein which functions as a cofactor of activated protein C. A single, unique beta-chain of the C4BPB assembles with 7 identical alpha-chains into the principal isoform of C4BPB, which is a multimeric protein that controls activation of the complement cascade via the classical pathway. C4BPB binds as a cofactor to C3b/C4b inactivator (C3bINA), which subsequently hydrolyzes the complement fragment C4b. In addition, C4BPB accelerates the degradation of the C4bC2a complex (C3 convertase) by detaching the complement fragment C2a. Furthermore, C4BPB interacts with anticoagulant protein S and with serum amyloid P component.

Retinol Binding Protein-4 or RBP4, is the retinol currier protein in the plasma. RBP4 takes part on the conversion of retinol to the stable and soluble retinol complex in the plasma. RBP4 carries retinol from the liver tissue where its store to peripheral tissues. RBP-retinol complex has interactions with transthyretin in the plasma, thus prevents its loss by filtration in the kidney.

Fibrinogen Beta Chain 9 (FGB) is the beta component of fibrinogen, a blood-borne glycoprotein composed of 3 pairs of nonidentical polypeptide chains. When vascular injury accrues, fibrinogen is cleaved by thrombin to form fibrin which is found in abundance in blood clots.

S100A11 is a member of the S100 family of proteins which contains two EF-hand calcium-binding motifs and is thought to be involved in the regulation of a number of cellular processes including cell cycle progression and differentiation. S100A11 may function in motility, invasion and tubulin polymerisation. S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21. Chromosomal rearrangements and altered expression of S100A11 have been implicated in tumor metastasis.

PEBP1 (Phosphatidylethanolamine binding protein 1) belongs to the phosphatidylethanolamine-binding protein family and a serine protease inhibitor that inhibits thrombin, neuropsin. PEBP1 plays a key modulatory part in several protein kinase signaling cascades. PKC phosphorylates PEBP1, resulting in the release of Raf-1 and activation of MEK and ERK. PEBP1 is expressed in many tissues and implicated in the regulation of such physiological processes as membrane biosynthesis, spermatogenesis, neural development, and metastasis suppression.
PEBP1 binds ATP, opioids and phosphatidylethanolamine, however it has lower affinity for phosphatidylinositol and phosphatidylcholine. PEBP1 may also be involved in the function of the presynaptic cholinergic neurons of the CNS. PEBP1 increases the production of choline acetyltransferase although not acetylcholinesterase. Furtheremore, PEBP1 functions in potentially sequestering toxic compounds, including locostatin which may have harmful effects on cells.
Loss of PEBP1 expression may have a significant role as prognostic marker in Gastrointestinal stromal tumors. In addition, PEBP1 is found differentially expressed in the Wernicke's Area from schizophrenia patients. PEBP1 is also, an invasion suppressor protein in nasopharyngeal carcinoma.

Recombinant Protein A/G fusion protein joins IgG binding domains of both Protein A and Protein G.
Protein A/G includes four Fc binding domains from Protein A and two from Protein G, yielding a final mass of 50.4 kDa. The binding dependency to pH of Protein A/G lower than Protein A, but has the additive properties of Protein A and G together. Protein A/G binds to all subclasses of human IgG, making it helpful for purifying polyclonal or monoclonal IgG antibodies whose subclasses have not been identifieed. Protein A/G binds to IgA, IgE, IgM and IgD. Protein A/G binds to all subclasses of mouse IgG excluding mouse IgA, IgM or serum albumin. This permits Protein A/G to be used in purification and detection of mouse monoclonal IgG antibodies, with no interference from IgA, IgM and serum albumin. Mouse monoclonal antibodies normally have a stronger affinity to the chimeric Protein A/G than to either Protein A or Protein G. Protein A/G also has been used for purification of macaque IgG.

The protein encoded by this gene is a member of the bone morphogenetic protein family which is part of the transforming growth factor-beta superfamily. The superfamily includes large families of growth and differentiation factors. Bone morphogenetic proteins were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. This particular family member plays an important role in the onset of endochondral bone formation in humans, and a reduction in expression has been associated with a variety of bone diseases, including the heritable disorder Fibrodysplasia Ossificans Progressiva. Alternative splicing in the 5' untranslated region of this gene has been described and three variants are described, all encoding an identical protein.

SNUPN is a nuclear import adaptor protein which is part of the Snurportin family.
SNUPN is Localized to the cytoplasm and nucleus and contains an N-terminal IBB domain and a trimethylguanosine (m3G)-cap binding domain. SNUPN binds specifically the terminal 2,2,7-m3G-cap at the 5'' end of U snRNPs and is involved in transport of U snRNPs into the nucleus through an association with Importin β.

Maltose Binding Protein (MBP) is a part of the maltose/maltodextrin system of Eschericia coli bacteria, which is responsible for the uptake and efficient catabolism of maltodextrins. It is a complex regulatory and transport system involving many proteins and protein complexes.
Maltose binding protein MalE,MBP, is part of the maltodextrin transport system in E. coli. The maltodextrins diffuse through the LamB pore located in the outer membrane into the periplasm. The sugar is bound to MalE which prevents it to diffuse back outside. MalE passes the sugar to a complex of MalF and MalG in the cytoplasmic membrane where active tranport is mediated by the ATPase MalK. MBP molecular weight is 40,622 dalton. There are two domains in the protein with similar secondary structure (central pleated sheets are surrounded by helices) . The domains are connected by three bridges, between the domains is a deep groove in which the sugar is bound. All hydroxyl groups of the sugar are fixed by sidechains of the protein by hydrogen bonds. Some water molecules are part of the hydrogen bridge network.

FKBP6 is part of the immunophilin protein family, and is involved in immunoregulation and basic cellular functions involving protein folding and trafficking. FKBP6 is widely expressed in all tissues, FKBP6 is present at utmost levels in testis, liver, kidney, skeletal muscle and heart. Deletion of FKBP6 contributes to hypercalcemia and growth delay in Williams-Beuren syndrome.

GDNF promotes the survival and differentiation of neurons in culture, and is able to prevent apoptosis of motor neurons induced by axotomy. The encoded protein is processed to a mature secreted form that exists as a homodimer. The mature form of the protein is a ligand for the product of the RET (rearranged during transfection) protooncogene. In addition to the transcript encoding GDNF, two additional alternative transcripts encoding distinct proteins, referred to as astrocyte-derived trophic factors, have also been described. Mutations in this gene may be associated with Hirschsprung disease.
GDNF enhances survival and morphological differentiation of neurons and increases their high-affinity uptake.

Calcium-binding protein P22 is a phosphoprotein that binds to the sodium-hydrogen exchangers (NHEs). CHP is an essential cofactor which maintains the physiological activity of NHE family members. CHP has protein sequence resemblance to calcineurin B and it is also identified to be an endogenous inhibitor of calcineurin activity.CHP is necessary for constitutive membrane traffic. CHP Inhibits GTPase-stimulated Na(+)/H(+) exchange. CHP inhibits calcineurin phosphatase activity. Required for activity of SLC9A1/NHE1.

ULBP1 together with at least ULBP2 and ULBP3, is ligand for the NKG2D receptor. ULBPs stimulate various signaling pathways in primary NK cells, which result in cytokines and chemokines production. In CMV infected cells, ULBP1 cooperates with soluble CMV glycoprotein UL16 to inhibit the interaction with the NKG2D receptor providing a mechanism by which CMV infected cells escape the immune system. Additionally, UL16 retains ULBP1 to the ER and cis-Golgi apparatus to prevent it from reaching cell surface.

Polcalcin Aln g 4 (Aln G 4.0101) causes an allergic reaction in humans.

CHD4 is a member of a family of alleged chromodomain helicase-DNA-binding proteins. Biochemically, CHD4 is a component of the nucleosome transformation and deacetylase (NuRD) complex that takes part in transcription regulation. Autoantibodies targeting the CHD4 are a serologic feature of idiopathic inflammatory myopathies (IIM). In IIM Mi-2 antibodies are characterized by diagnostic sensitivity and specificity of approximately 4-18% and 98-100%, respectively. Moreover, anti-CHD4 antibodies are related to dermatomyositis (frequency up to 31%) and have a great positive predictive value for this type of disease subset. Anti-CHD4 are the only defined myositis-specific autoantibodies clearly focused to a nuclear target. An additional slightly outstanding feature of Mi-2 antibodies relates to their frequency in children, which is similar to that in adults.

SCGN is a secreted calcium-binding protein which is found in the cytoplasm. It is related to calbindin D-28K and calretinin. Secretagogin is involved in KCL-stimulated calcium flux and cell proliferation.
Secretagogin plays a role in human non-functional pituitary adenomas.

HIV-1, the causative agent of acquired immunodeficiency syndrome (AIDS), contains an RNA genome which produces a chromosomally integrated DNA during the replicative cycle. Activation of HIV-1 gene expression by the transactivator Tat is dependent on an RNA regulatory element (TAR) located downstream of the transcription initiation site. TARDBP is a transcriptional repressor which binds to chromosomally integrated TAR DNA and represses HIV-1 transcription. In addition, TARDBP regulates alternate splicing of the CFTR gene. A similar pseudogene is present on chromosome 20.

FKBP4 is part of the immunophilin protein family, which takes part in immunoregulation and necessary cellular processes concerning protein folding and trafficking. FKBP4 is a cis-trans prolyl isomerase that connects to the immunosuppressants FK506 and rapamycin. FKBP4 has high structural and functional similarity to FKBP1A, though, FKBP4 does not have immunosuppressant activity when complexed with FK506. FKBP4 is known to connect with phytanoyl-CoA alpha-hydroxylase. FKBP4 associates with HSP90 & HSP70 thus takes part in the intracellular trafficking of hetero-oligomeric forms of the steroid hormone receptors. FKBP4 highly associates with adeno-associated virus type 2 vectors (AAV) resulting in a considerable increase in AAV-mediated transgene expression in human cell lines. FKBP4 is involved in the optimal use of AAV vectors in human gene therapy.

DnaK, originally identified for its DNA replication by bacteriophage l in E. coli is the bacterial hsp70 chaperone. This protein is involved in the folding and assembly of newly synthesized polypeptide chains and in preventing the aggregation of stress-denatured proteins.The protein coding region of the substrate binding domain of DnaK (amino acids 385-638) was amplified by PCR and cloned into an E. coli expression vector. The substrate binding domain of DNAK was purified to apparent homogeneity by using conventional column chromatography techniques. Additional amino acid (Met) is attached at N- terminus.

The heat-shock response is elicited by exposure of cells to thermal and chemical stress and through the activation of HSFs (heat shock factors) results in the elevated expression of heat-shock induced genes. Heat shock factor binding protein-1 (HSBP1), is a 76-amino-acid protein that binds to heat shock factor 1(HSF1), which is a transcription factor involved in the HS response. During HS response, HSF1 undergoes conformational transition from an inert non-DNA-binding monomer to active functional trimers. HSBP1 is nuclear-localized and interacts with the active trimeric state of HSF1 to negatively regulate HSF1 DNA-binding activity. Overexpression of HSBP1 in mammalian cells represses the transactivation activity of HSF1. When overexpressed in C.elegans HSBP1 has severe effects on survival of the animals after thermal and chemical stress consistent with a role of HSBP1 as a negative regulator of heat shock response.