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Single-Stranded DNA Binding Protein 1 (SSBP) participates in mitochondrial biogenesis. SSBP binds preferentially and cooperatively to ss-DNA. The SSBP protein is involved in mitochondrial DNA replication and associates with mitochondrial DNA.

Single-Stranded DNA Binding Protein 1 (SSBP) participates in mitochondrial biogenesis. SSBP binds preferentially and cooperatively to ss-DNA. The SSBP protein is involved in mitochondrial DNA replication and associates with mitochondrial DNA.

Nucleic acid binding protein 1 is a part of the SOSS complex, amultiprotein complex which functions downstream of the MRN complex to promote DNA repair and G2/M checkpoint.In the SOSS complex, NABP1 acts as a sensor of single-stranded DNA which binds to single-stranded DNA, inparticular to polypyrimidines. The SOSS complex links with DNA lesions and affects diverse endpoints in the cellular DNA damage response including cell-cycle checkpoint activation, recombinational repair andmaintenance of genomic stability. NABP1 is essential for efficient homologous recombination-dependent repairof double-strand breaks (DSBs) and ATM-dependent signaling pathways.

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. Dnak(residues 508-638) of the substrate binding domain is a-helical and appears to act as a lid covering the substrate binding cleft. DnaK(amino acid 508-638) was purified to apparent homogeneity by using conventional column chromatography techniques. Additional amino acid (Met) is attached at N- terminus.

Inhibitor of DNA Binding 1 (ID1) is a helix-loop-helix protein which can form heterodimers with members of the basic HLH family of transcription factors. ID1 is lacking DNA binding activity and thus can inhibit the DNA binding and transcriptional activation ability of basic HLH proteins with which it interacts. ID1 participates in cell growth, senescence, and differentiation.

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.

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.

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.

Heterogeneous nuclear ribonucleoprotein A1 (HNRNPA1) is a member of the A/B subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). HNRNPA1 is involved in the packing of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and may control splice site selection. The HNRNPA1 protein may also have a role in HCV RNA replication. In addition, HNRNPA1 is believed to have a key role in the formation of specific myometrial protein species in parturition.
The hnRNP proteins have distinctive nucleic acid binding properties. HNRNPA1 has 2 repeats of quasi-RRM domains that bind to RNAs. HNRNPA1 is one of the most copious core proteins of hnRNP complexes and it is restricted to the nucleoplasm. The HNRNPA1 protein, along with other hnRNP proteins, is exported from the nucleus, most likely bound to mRNA, and is immediately re-imported. The M9 domain of HNRNPA1 functions as both a nuclear localization and nuclear export signal.

Inhibitor of DNA Binding 2 (ID2) is a part of the inhibitor of DNA binding family, whose members are transcriptional regulators that contain a helix-loop-helix (HLH) domain but not a basic domain. Members of the ID family inhibit the functions of basic helix-loop-helix transcription factors in a dominant-negative way by suppressing their heterodimerization partners through the HLH domains. ID2 play a role in negatively regulating cell differentiation and may be an inhibitor of tissue-specific gene expression.

Maltose Binding Protein is a member of the maltose/maltodextrin system of E.Coli, which is accountable for the uptake and efficient catabolism of maltodextrins. The maltose/maltodextrin is a complex regulatory and transport system involving many proteins and protein complexes.
MBP elevates the yield of its fusion partner in many cases and is often able to promote the solubility of polypeptides to which it is fused.

Maltose Binding Protein is a member of the maltose/maltodextrin system of E.Coli, which is accountable for the uptake and efficient catabolism of maltodextrins. The maltose/maltodextrin is a complex regulatory and transport system involving many proteins and protein complexes.
MBP elevates the yield of its fusion partner in many cases and is often able to promote the solubility of polypeptides to which it is fused.

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).

Nucleobindin-2 (also known as NUCB2 or Nesfatin) is a EF-hand calcium-binding protein. Nucleobindin-2 takes part in calcium homeostasis and is a multifunctional protein that interacts with Ca(2+) nucleic acids & various regulatory proteins in different signaling pathways. NUCB2 (Nesfatin) is localized in neuronal perikarya and dendrites of mouse brain.

Nucleobindin-2 (also known as NUCB2 or Nesfatin) is a EF-hand calcium-binding protein. Nucleobindin-2 takes part in calcium homeostasis and is a multifunctional protein that interacts with Ca(2+) nucleic acids & various regulatory proteins in different signaling pathways. NUCB2 (Nesfatin) is localized in neuronal perikarya and dendrites of mouse brain.

Zinc Finger HIT-Type Containing 1 (ZNHIT1) is a member of the ZNHIT1 family and contains 1 HIT-type zinc finger. The ZNHIT1 protein is induced by DNA damage and appears to have a role in p53-mediated apoptosis induction. ZNHIT1 interacts with MAPK11 and MAPK14 and is a component of the chromatin-remodeling SRCAP complex composed of at least SRCAP, DMAP1, RUVBL1, RUVBL2, ACTL6A, YEATS4, ACTR6 and ZNHIT1. ZNHIT1 binds to NR1D2 and discharges it of its inhibitory effect on the transcription of APOC3 without affecting its DNA-binding activity.

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.

SDCBP2 has two class II PDZ domains. PDZ domains assist protein-protein interactions by attaching to the cytoplasmic C-terminus of transmembrane proteins, and PDZ-containing proteins mediate cell signaling and the organization of protein complexes. SDCBP2 attaches to phosphatidylinositol 4, 5-bisphosphate (PIP2) and take part in nuclear PIP2 arrangement and cell division.

S100A1 is a member of the S100 family of calcium binding proteins with EF-hand type Ca+2 binding motive. S100A1 (Calcium Binding Protein A1) is involved in the activation of sarcoplasmatic calcium release and the regulation of intermediate filament polymerization. S100A1 may function in stimulation of Ca2+-induced Ca2+ release, inhibition of microtubule assembly, and inhibition of protein kinase C-mediated phosphorylation. Reduced expression of S100A1 has been implicated in cardiomyopathies.
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.

Dysbindin domain-containing protein 1 (DBNDD1) is a member of the dysbindin family.

S100A8 is a part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a broad range of cells, and participate in the regulation of cellular processes such as cell cycle progression and differentiation. S100A8 plays a role in the inhibition of casein kinase and as a cytokine. S100A8 altered expression is related with cystic fibrosis disease. S100A8 is a calcium-binding protein that has antimicrobial activity against bacteria and fungi.S100A8 is crucial for resistance towards invasion by pathogenic bacteria. S100A8 up-regulates transcription of genes that are under the control of NF-kappa-B. S100A8 plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide. S100A8 endorses tubulin polymerization and promotes phagocyte migration and infiltration of granulocytes at sites of wounding. S100A8 takes part as a pro-inflammatory mediator in acute and chronic inflammation and up-regulates the release of IL8 and cell-surface expression of ICAM1.

Maltose Binding Protein is a member of the maltose/maltodextrin system of E.Coli, which is accountable for the uptake and efficient catabolism of maltodextrins. The maltose/maltodextrin is a complex regulatory and transport system involving many proteins and protein complexes.
MBP elevates the yield of its fusion partner in many cases and is often able to promote the solubility of polypeptides to which it is fused.

Purine-Rich Element Binding Protein B (PURB) is a single-stranded DNA-binding protein which takes part in the dendritic transport of a subset of mRNAs. PURB operates as repressor in myoblasts and fibroblasts in the control of vascular smooth muscle alpha-actin gene transcription. PURB binds preferentially to the single strand of the purine-rich element termed PUR, which is present at origins of replication and in gene flanking regions in various eukaryotes from yeasts through humans.

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.