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TAR DNA Binding Protein (TARDBP) was initially recognized as a transcriptional repressor which binds to chromosomally integrated TAR DNA and represses HIV-1 transcription. In addition, TARDBP has been detected in individuals diagnosed with chronic traumatic encephalopathy as well, which is a condition that often imitates ALS andhas been related with athletes who have experienced multiple concussions and other types of head injury.TARDBP has been shown to bind both DNA and RNA, it has multiple functions in transcriptional repression, pre-mRNAsplicing and translational regulation.

RAD51D is a member of the RAD51 protein family whose members are extremely similar to bacterial RecA and Saccharomyces cerevisiae Rad51. RAD51 protein family members take part in the homologous recombination and repair of DNA. RAD51D forms a complex with several other members of the RAD51 family which catalyzes homologous pairing between single- and double-stranded DNA, and participates in the early stage of recombinational repair of DNA.

MAPKSP1 is a scaffold protein which operates in the extracellular signal-regulated kinase (ERK) cascade. MAPKSP1 protein is restricted to late endosomes by the mitogen-activated protein-binding protein-interacting protein, and binds specifically to MAP kinase kinase MAP2K1/MEK1, MAP kinase MAPK3/ERK1, and MAP kinase MAPK1/ERK2.

RANBP1 is a member of a family of proteins which bind Ran GTPase. Ran GTPase is vital for cell cycle control, mRNA processing, nuclear transport, mitotic spindle assembly, and postmitotic nuclear re-assembly and nuclear architecture maintenance. RANBP1 does not stimulate GTPase activity of RAN however RANBP1 does distinctly raise GTP hydrolysis by the RanGTPase-activating protein (RanGAP1). Additionally, RANBP1 operates as a negative regulator of RCC1 by inhibiting RCC1-stimulated guanine nucleotide release from RAN.

Protein A is a cell wall protein deriving from Staphylococcus aureus which exhibits unique binding properties for IgG from a variety of mammalian species and for some IgM and IgA as well. It binds with the Fc region of immunoglobulins through interaction with the heavy chain. It couples to a wide variety of reporter molecules including fluorescent dyes, enzyme markers, biotin, colloidal gold and radioactive iodine without affecting the antibody binding site. Recombinant Protein A was developed to increase the specificity of the molecule for IgG and is widely used both in research and bioprocessing. The recombinant protein A is produced by expressing a modified protein A gene in E.coli. A specific purification process with strict quality control was taken to get the recombinant protein A with the purity of more than 98% , no human IgG affinity step is used during validated fermentation and purification and devoid of bacterial contaminant found normally in native Protein A. (Free of Staphylococcus endotoxins and hemolysin).

Protein A is a cell wall component produced by several strains of Staphylococcus aureus. The recombinant Protein A is genetically engineered protein and holds 5 IgG-binding regions of protein A. Recombinant Protein A functions basically the same as native Protein A and is perfect for purification of polyclonal or monoclonal IgG antibodies. Protein A binds to human IgG1, IgG2 and IgG4, mouse IgG2a, IgG2b and IgG3 and rat IgG2c. Protein A also binds to total IgG from rabbit, pig, dog, cat, and guinea pig.

Fibroblast Growth Factor Binding Protein 1, also known as FGFBP1 is a secreted fibroblast growth factor carrier protein. FGFBP1 plays a vital part in cell proliferation, differentiation and migration by binding to fibroblast growth factors and potentiating their biological effects on target cells. In addition, FGFBP1 also takes part in tumor growth as an angiogenic switch molecule, furthermore an expression of FGFBP1 has been associated with more than a few types of cancer as well as pancreatic and colorectal adenocarcinoma.

CAB39 protein and STE20-related adaptor-alpha pseudo kinase, form a regulatory complex that is able of stimulating the activity of the LKB1 tumor suppressor protein kinase. CAB39 takes part as a scaffolding component of the STK11/STRAD complex and regulates STK11 activity and cellular localization.

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.

Calcium-binding protein 7 (CABP7) contains 2 EF-hand domains. CABP7 negatively regulates Golgi-to-plasma membrane trafficking by interacting with PI4KB and inhibiting its activity. The CaBP family of EF-hand containing small Ca (2+)-binding proteins has lately emerged as significant regulators of multiple targets essential to normal neuronal function in the mammalian central nervous system.

RAD51D is a member of the RAD51 protein family whose members are extremely similar to bacterial RecA and Saccharomyces cerevisiae Rad51. RAD51 protein family members take part in the homologous recombination and repair of DNA. RAD51D forms a complex with several other members of the RAD51 family which catalyzes homologous pairing between single- and double-stranded DNA, and participates in the early stage of recombinational repair of DNA.

EIF4EBP2 belongs to the eukaryotic translation initiation factor 4E binding protein family. Even though EIF4EBP2 protein binds eIF4E and inhibits translation initiation, growth factors can release this inhibition by a phosphorylation-dependent disruption. EIF4EBP2 mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase pathway. Regulation of this protein is associated to cell proliferation, cell differentiation and viral infection.

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.

Heat Shock Factor Binding Protein 1-Like 1 (HSBP1L1) is a part of a family of eukaryotic proteins known as nucleotide exchange factors for HSP 70. HSBP1L1 is a protein coding gene whose expression is regulated mainly at the transcription level.

Nucleotide Binding Protein 2, also known as NUBP2 is an adenosine triphosphate (ATP) as well as metal-binding protein which is essential for the assembly of cyotosolic iron-sulfur proteins. NUBP2 performs in a heterotetramer with nucleotide-binding protein 1 (NUBP1). Moreover, alternative splicing results in multiple transcript variants have been found for NUBP2.

Nob1 takes part in pre-rRNA processing and cleaves in a late cytoplasmic processing step a 20S rRNA intermediate at cleavage site D to create the mature 18S rRNA. In yeast, more than 200 protein and RNA cofactors are essential for ribosome assembly, and these are mostly conserved in eukaryotes. These factors oversee alteration and cleavage of the initial 35S precursor rRNA transcript into the mature 18S, 5.8S, and 25S rRNAs, folding of the rRNA, and binding of ribosomal proteins and 5S RNA.

HP-NAP protects DNA from oxidative damage by sequestering intracellular Fe2+ ion and storing it in the form of Fe3+ oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe2+ ions, thus preventing hydroxyl radical production by the Fenton reaction. HP-NAP is necessary for the survival in the presence of oxidative stress. Dps is also a virulence factor which activates neutrophils, mast cells and monocytes. HP-NAP binds to neutrophil-glycosphingolipids and to sulfated carbohydrates on mucin. HP-NAP might play a part in the accumulation of neutrophils and monocytes at the site of infection. HP-NAP induces superoxide anion generation, adhesion and chemotaxis of neutrophils, via a pertussis toxin-sensitive pathway involving MAP kinases.

CtBP was initially known as a cellular protein which cooperates with a C-terminal motif of adenovirus E1A oncoproteins. C-terminal-binding protein is extremely conserved in higher eukaryotes. Vertebrates hold two highly homologous CtBP proteins (CtBP1 and CtBP2) while invertebrates h a single CtBP. CtBP family proteins has a significant sequence homology with D-2-hydroxy acid dehydrogenases. In addition, CtBP proteins cooperates with numerous proteins and functions as a co-repressor of transcription.

Alpha & Gamma-Adaptin Binding Protein (AAGAB), which is also known as P34, takes part in membrane traffic and interacts with AP1G1 and AP2A1.AAGAB is highly expressed in skin and keratinocytes, with the highest levels in adrenal gland, rectum and thymus.

Cytosolic Fe-S cluster assembly factor NUBP1 isoform 1 (NUBP1) is Involved in the regulation of centrosome duplication similarity. NUBP1 is a component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. NUBP1 is necessary for maturation of extra mitochondrial Fe-S proteins. The NUBP1-NUBP2 heterotetramer constructs a Fe-S scaffold complex, mediating the de novo compilation of a Fe-S cluster and its transfer to target apoproteins.

Eukaryotic Translation Initiation Factor 4E-Binding Protein 3 (EIF4EBP3) belongs to the EIF4EBP family whose proteins bind to eukaryotic initiation factor 4E and regulate its assembly into EIF4F, the multi-subunit translation initiation factor that identifies the mRNA cap structure.

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.

Geminin is a 25 kDa nuclear protein, which inhibits DNA replication and is degraded during the mitotic phase of the cell cycle. Geminin controls replication by binding to the licensing factor Cdt1, and is involved in neural differentiation. In addition, Geminin directly interacts with Six3 and Hox homeodomain proteins during embryogenesis and inhibits their functions. Geminin can also promote DNA replication. Geminin has 2 roles in 2 different stages of the cell cycle: Geminin is a negative regulator of DNA replication during the “S phase” of the cell cycle. Inhibition of Geminin during the “S phase” (by RNAi) results in an additional round of replication of portions of the genome. During the “M phase” of the cell cycle (mitosis) Geminin stabilizes the replication factor Cdt1 promoting DNA replication during the next cell cycle. Moreover, inhibition of Geminin during mitosis (by RNAi) causes destabilization of Cdt1 protein and impairment of DNA replication during the next cell cycle. Geminin thus guarantees that only one round of replication occurs during each cell cycle. It was discovered that Geminin is overexpressed in a number of malignancies and cancer cell lines. This maintains the concept that Geminin has also a positive role in DNA replication and cell cycle progression. Geminin accumulates through S, G2 and M phases of the cell cycle but is absent during the G1 phase. During the metaphase/anaphase transition of mitosis Geminin levels decrease.