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Corticotropin Releasing Hormone Binding Protein or CRHBP is a hormone that stimulates the preopiomelanocortin-derived peptides secretion & synthesis. In general, the levels of CRHBP in the human plasma are relatively low. There are times when we can find high levels of the hormone, mainly in pregnancy, after parturition the levels drop back, the high levels are thought to be derived from the placenta. CRH-binding protein can be found in the plasma, this protein inactivates CRH, in order to avoid inappropriate pituitary-adrenal stimulation during gestation.

Four And A Half LIM Domains 2 (FHL2) belongs to the four-and-a-half-LIM-only protein family. Family members are comprised of 2 highly conserved, tandemly arranged, zinc finger domains with 4 highly conserved cysteines binding a zinc atom in each zinc finger. The FHL2 protein is assumed to play a part in the assembly of extracellular membranes. Furthermore, FHL2 is down-regulated during transformation of normal myoblasts to rhabdomyosarcoma cells and the FHL2 functions as a link between presenilin-2 and an intracellular signaling pathway.

FtsJ RNA Methyltransferase Homolog 2 (FTSJ2) belongs to the S-adenosylmethionine-binding protein family. FTSJ2 is a nucleolar protein and which is involved in cell cycle control and DNA repair and the processing and modification of rRNA. FTSJ2 is extensively expressed, with the highest expression in the muscle, placenta, and heart.

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

TSR2 is part of the TSR2 family. TSR2 is involved in 20S pre-rRNA processing. Among the diseases which are associated with TSR2 are blepharospasm and diamond-blackfan anemia.

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.

Growth hormone receptor, also known as GHR is part of the cytokine receptor family. GHR binds 2 receptor molecules and in this manner induces signal transduction through receptor dimerization. Furthermore, at high concentrations, growth hormone performs as an antagonist since there is a large difference in affinities at the respective binding sites. The antagonist action can be enhanced further by reducing binding in the low affinity binding site.

Basic transcription factor 3 (BTF3), which is a member of the NAC-beta family, forms a stable complex with RNA polymerase II. The BTF3 protein is vital for the initiation of transcription.

MED7 is a member of the Mediator complex subunit 7 family. The activation of gene transcription is a multistep course which is initiated by factors which identify transcriptional enhancer sites in DNA and collaborate with co-activators to direct transcriptional initiation by the RNA polymerase II apparatus. The gene encode a subunit of the CRSP (cofactor required for SP1 activation) complex, that, together with TFIID, is needed for effective activation by SP1. Additionally, MED7 is also an element of other multisubunit complexes e.g. thyroid hormone receptor-(TR-) associated proteins that cooperate with TR and enables TR function on DNA templates in conjunction with initiation factors and cofactors.

Interleukin-18 Binding Protein (IL18BP) serves as an inhibitor of the proinflammatory cytokine, IL18. IL18BP binds IL18, inhibits the binding of IL18 to its receptor, and consequently inhibits IL18-induced IFN-gamma production, resulting in reduced T-helper type 1 immune responses. The IL18BP protein is constitutively expressed and secreted in mononuclear cells. Elevated levels of IL18BP protein are detected in the intestinal tissues of patients with Crohn's disease.

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.

FK506 Binding Protein 5 (FKBP5) belongs to the immunophilin protein family, which has a role in immunoregulation and basic cellular processes involving protein folding and trafficking. FKBP5 is a cis-trans prolyl isomerase, which binds to the immunosuppressants FK506 and rapamycin. FKBP5 is an immunophilin protein with PPIase and co-chaperone activities. FKBP5 is assumed to mediate calcineurin inhibition. FKBP5 is a component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). In addition, FKBP5 interacts functionally with mature hetero-oligomeric progesterone receptor complexes along with the 90 kDa heat shock protein and P23 protein.

CRABP2 NCBI Accession No: NP_001869 regulates the access of retinoic acid to the nuclear retinoic acid receptors. CRABP2 is involved in a regulatory feedback mechanism that controls the action of retinoic acid on cell differentiation. CRABP2 is involved in the conversion of vitamin A into its intracellular active form retinoic acid, which regulate the genes responsible for lipid metabolism and adipocyte differentiation. CRABP2 gene is located on chromosome 1q21-23 and this region has been linked with related disorders such as familial combined hyperlipidemia (FCHL) and type 2 diabetes mellitus. CRABP proteins are of low molecular weight having an important function in retinoic acid-mediated regulation of human skin growth and differentiation.

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.

Prolactin is a pituitary hormone involved in the stimulation of milk production, salt and water regulation, growth, development and reproduction. The initial step in its action is the binding to a specific membrane receptor (prolactin receptor) which belongs to the superfamily of class 1 cytokine receptors. The function of the prolactin receptor is mediated, at least in part, by two families of signaling molecules: Janus kinases and signal transducers and activators of transcription. Prolactin (PRL) is a hormone involved in a variety of important functions including ion transport and osmoregulation, stimulation of milk, protein synthesis as well as the regulation of numerous reproductive functions. PRL exerts its influence on different cell types through a signal transduction pathway which begins with the binding of the hormone to a transmembrane PRL receptor. Immunoreactive PRL receptor, a member of the cytokine receptor family, varies in size (short and long forms) with tissue source and species, from ~40 kDa to 100 kDa. The PRL receptor consists of at least three separate domains: an extracellular region with 5 cysteines which contains the prolactin binding site, a single transmembrane domain and a cytoplasmic region, the length of which appears to influence ligand binding and regulate cellular function.

Alpha-2-Glycoprotein 1 Zinc-Binding or AZGP1 is a protein, part of the MHC class 1 protein family. AZGP1 is thought to connect to prolactin-inducible protein (PIP), and not to , B 2-microglobulin (MHC light chain). AZGP1 is secreted from epithelia and can be found in nearly all fluids of the body. In adipocytes, AZGP1 triggers lipid degradation, that leads to a broad fat lost that can be linked to progressive type of cancers.

Fatty acid binding protein 9 (FABP9) belongs to the fatty acid-binding proteins (FABPs) which are a family of small, extremely conserved, cytoplasmic proteins to bind long-chain fatty acids and other hydrophobic ligands. FABP9 is found in midpachytene spermatocytes and round spermatids, and comprises part of the perinuclear theca. FABP9 probably links intracellular membranes and signals abnormal sperm formation during spermatogenesis.

Ubiquitin thioesterase OTUB2 (OTUB2) is a member of the peptidase C65 family. OTUB2 functions as a hydrolase which can remove conjugated ubiquitin from proteins in vitro and may thus play a key regulatory role at the level of protein turnover by preventing degradation.

Ras GTPase-activating protein-binding protein 2 (G3BP2) is restricted to the plasma membrane and endocytic compartments and controls a fast endocytic recycling pathway. G3BP2 may be a scaffold protein which might be involved in mRNA transport.

Since April 2012, cases of the Middle East Respiratory Syndrome Coronavirus (MERS-CoV) have been identified in various countries. Coronaviruses are the cause of the common cold, SARS (severe acute respiratory syndrome) and other severe illnesses with high mortality rates, all are classified into coronavirus family. MERS-CoV is a new type of SARS found in the coronavirus family causing severe pneumonia with sudden and serious respiratory illness with high mortality rates as well. Since January 27th 2015, the WHO has reported 956 human cases, including 351 deaths. More cases of the new coronavirus strain are expected. Like in other coronaviruses, large surface spike glycoprotein is a central structural protein of this virus; it is located above the virion surface to bind and enter into the target cell. Spike protein has 2 domains- S1 and S2. The S1 domain is responsible for cellular tropism and interaction with target cell, while the S2 domain is responsible for membrane fusion. The C-terminal of S1 domain contains a receptor binding domain, and is also a potential target for vaccine development and an antigen for diagnosis.

TIAL1 belongs to a family of RNA-binding proteins, it has 3 RNA recognition motifs (RRMs), and binds adenine and uridine-rich elements in mRNA and pre-mRNAs of a extensive range of genes. TIAL1 regulates a variety of activities including translational control, splicing and apoptosis. TIAL1 different isoforms function differently with respect to post-transcriptional silencing.

S100A3 is part of S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm/nucleus of a broad range of cells, and takes part in the regulation of several cellular processes such as cell cycle progression and differentiation. S100A3 has the largest number of cysteines of all S100 proteins. S100A3 has high affinity for Zinc, and is widely expressed in human hair cuticle.

Mediator complex subunit 4 (MED4) is a component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. MED4 is a component of the vitamin D receptor-interacting protein (DRIP) complex which functions as a nuclear receptor coactivator. The DRIP complex is able to activate nuclear receptors in a ligand-dependent manner. MED4 functions as a link to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription apparatus. MED4 is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.