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Escherichia coli Hsp31 (HchA) is a homodimeric member of the ThiI/DJ-1/PfpI superfamily which combines molecular chaperone and aminopeptidase activities. HchA uses temperature-induced exposure of structured hydrophobic domains to capture and stabilize early unfolding protein intermediates under severe thermal stress.

MGP is vital for the regulation of calcification in the extracellular matrix, particularly in cartilage and arteries. The K-dependent vitamin MGP has five to six residues of Gla, a Ca2+ binding amino acid crucial for vitamin K-dependent gamma carboxylase for its formation. MGP is formed by COOH-terminal processing by carboxypeptidase B-like enzymatic activity and localized in the human bone.

The Melanoma Inhibitory protein (MIA) was identified as an inhibitor of in vitro growth of malignant melanoma cells. The protein contains a SH3 domain. MIA acts as a potent tumor cell growth inhibitor for malignant melanoma cells and some other neuroectodermal tumors, including gliomas, in an autocrine fashion. In a study of human melanoma cell lines with different metastatic capacity MIA mRNA expression appeared to be inversely correlated with pigmentation. MIA has been shown to represent a very sensitive and specific serum marker for systemic malignant melanoma that might be useful for staging of primary melanomas, detection of progression from localized to metastatic disease during follow-up, and monitoring therapy of advanced melanomas.

AnsA is a cytoplasmic asparaginase from E.coli involved in intracellular asparagine utilization. E.coli has 2 L-asparaginases: the cytoplasmic type I form (ansA) and the periplasmic type II form (ansB). AnsA (Type L asparaginase) is constitutively expressed and is obligatory for the growth of the bacteria on asparagine as the sole nitrogen source.

SNAP-25 is an necessary element of the core complex that is responsible for presynaptic vesicle trafficking. Thus, SNAP-25 is directly involved in the release of neurotransmitters and this protein exists as two alternative isoforms, SNAP25A and SNAP25B which differ by 9 amino acids in central portion of these proteins.

a-Synuclein (amino acids 1-140), an acidic neuronal protein of 140 amino acids, is extremely heat-resistant and is natively unfolded with an extended structure primarily composed of random coils. a-synuclein has been suggested to be implicated in the pathogenesis of Parkinson’s disease and related neurodegenerative disorders, and more recently, to be an important regulatory component of vesicular transport in neuronal cells. Moreover, recent studies have shown that a-synuclein has chaperone activity and that this activity is lost upon removing its C-terminal acidic tail (amino acids 96-140).

BAG1 binds to BCL2 and is also called BCL2-associated athanogene. BAG1 increases the anti-apoptotic effects of BCL2 and is characterizes as a link between growth factor receptors and anti-apoptotic mechanisms. BAG1 inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. BAG1 inhibits the pro-apoptotic function of PPP1R15A, and has anti-apoptotic activity. BAG1 enhances the anti-cell death function of BCL2 induced by various stimuli.

ENSA is an endogenous ligand for sulfonylurea receptor. ENSA reduces K(ATP) channel currents by inhibiting sulfonylurea from binding to the receptor and thus stimulates insulin secretion. Endosulfine Alpha is part of a conserved cAMP-regulated phosphoprotein (ARPP) family. Endosulfine Alpha is an endogenous ligand for the sulfonylurea receptor, ABCC8/SUR1. Endosulfine Alpha is an endogenous regulator of KATP channels. ENSA modulates insulin secretion through the interaction with KATP channel. ENSA is a candidate gene for type 2 diabetes. ENSA is expressed in a wide range of tissues including muscle, brain, and endocrine tissues.

Chemokine (C-C motif) ligand 11 (CCL11) is a small cytokine belonging to the CC chemokine family that is also known as eotaxin. CCL11 selectively recruits eosinophils by inducing their chemotaxis, and therefore, is implicated in allergic responses. The effects of CCL11 are mediated by its binding to a G-protein-linked receptor known as a chemokine receptor. Chemokine receptors for which CCL11 is a ligand include CCR2, CCR3 and CCR5. The gene for human CCL11 (scya11) is encoded on three exons and is located on chromosome 17.

STX6 is a member of the syntaxin family and has 1 t-SNARE coiled-coil homology domain. STX6 takes part in intracellular vesicle transferring. STX6 binds EEA1 and Interacts with VPS45A, MARCH2, MARCH3 and GOPC. It is found in a complex comprising STX6, STX12, VAMP4 and VTI1A.

Suppressor of fused homolog (SUFU) is a member of the SUFU family. SUFU is a negative regulator of the hedgehog signaling pathway. SUFU interacts with GLI1, GLI3 and PEX26. Defects in the SUFU gene are a cause of medulloblastoma.

IL3 is a potent growth promoting cytokine. This cytokine is capable of supporting the proliferation of a broad range of hematopoietic cell types. It is involved in a variety of cell activities such as cell growth, differentiation and apoptosis. This cytokine has been shown to also possess neurotrophic activity, and it may be associated with neurologic disorders.

TBCEL, is a factor that is in charge of the microtubule cytoskeleton in determining cell behavior. TBCEL plays a role as a regulator of tubulin stability. While widely expressed in testis, TBCEL is also present in several tissues at a much lower level. TBCEL comprises of seven LRR (leucine-rich) repeats, one LRRCT domain and one ubiquitin-like domain. The gene that translates TBCEL consists of 66,704 bases and maps to human chromosome 11q23.3. Chromosome 11 houses over 1,400 genes and consist of nearly 4% of the human genome. Jervell and Lange-Nielsen syndrome, Jacobsen syndrome, Niemann-Pick disease, hereditary angioedema and Smith-Lemli-Opitz syndrome are associated with defects in genes that map to chromosome 11.

IL-36gamma belongs to the IL-1 family which includes IL-1b, IL-1a, IL-1ra, IL-18, IL-36 Ra (IL-1F5), IL-36a (IL-1F6), IL-36b (IL-1F8), IL-37 (IL-1F7) and IL-1F10. ). The IL-1 family members display a 12 b-strand, b-trefoil configuration, and are thought to have ascended from a mutual ancestral gene. IL-36g is an 18-22 kDa, 169aa intracellular and secreted protein which holds no signal sequence, no prosegment and no potential N-linked glycosylation sites. Human IL-36g shares 58%- 69% aa sequence homology with mouse, rat, bovine and equine IL-36g, and 23 - 57% aa sequence homology with other family members. The IL-36g receptor is a mixture of IL-1 Rrp2, mostly located in epithelia and keratinocytes, and the extensively expressed IL-1 RAcP. All IL-36 (a, b and g) activate N F-?B and MAPK pathways in an IL-1 Rrp2 dependent reaction. Additionally, IL-36g induces production of inflammatory cytokines and chemokines like CXCL8/IL-8.

Proteins of the TFF family are characterized by obtaining a minimum of 1 copy of the trefoil motif, a 40-amino acid domain that contains 3 conserved disulfides. Trefoil Factors are stable secretory proteins expressed in gastrointestinal mucosa which protect the mucosa from insults, stabilize the mucus layer and affect healing of the epithelium.TFF2 inhibits gastric acid motility & secretion. TFF2 stabilizes glycoproteins in the mucus gel through interactions with carbohydrate side chains.

CALR is a multifunctional protein that acts as a main Ca(2+)-binding (storage) protein in the lumen of the endoplasmic reticulum. Calreticulin is localized in the nucleus, and participates in transcription regulation. Calreticulin binds to the synthetic peptide KLGFFKR, which is nearly identical to an amino acid sequence in the DNA-binding domain of the superfamily of nuclear receptors. CALR binds to antibodies in specific sera of systemic lupus and Sjogren patients which have anti-Ro/SSA antibodies, it is well conserved among species, and it is positioned in the endoplasmic and sarcoplasmic reticulum where it binds calcium. The amino terminus of CALR interacts with the DNA-binding domain of the glucocorticoid receptor and prevents the receptor from binding to its specific glucocorticoid response element. CALR reduces the binding of androgen receptor to its hormone-responsive DNA element and inhibits androgen receptor and retinoic acid receptor transcriptional activities in vivo, as well as retinoic acid-induced neuronal differentiation. Therefore, CALR acts as a significant modulator of the regulation of gene transcription by nuclear hormone receptors.

Capping Protein (Actin Filament) Muscle Z-Line, Alpha 2 also known as CAPZA2 belongs the F-actin capping protein alpha subunit family. It is the alpha subunit of the barbed-end actin binding protein Cap Z. By capping the barbed end of actin filaments, Cap Z regulates the growth of the actin filaments at the barbed end. Among the diseases associated with CAPZA2 are endocarditis, and cervicitis.

Filamin is a large (270kd) dimeric actin crosslinking protein from a variety of sources, which helps to stabilize the 3D cortical actin network. The fundamental structure of filamin is well conserved and consists of an actin binding domain at the N-terminus followed by a C-terminal rod domain consisting of numerous repeat segments ranging from 4 in C. elegans to 24 in mammalian cells. Each repeat in the rod domain consists of roughly 100 residues and forms an immunoglobulin like fold. Such immunoglobulin folds have been found in a variety of proteins and are responsible for protein-protein interactions. Filamin Human actin-binding protein (ABP), aka filamin, crosslinks actin filaments into orthogonal networks in cortical cytoplasm and participates in the anchoring of membrane proteins for the actin cytoskeleton. Mammalian filamin interacts directly with at least 30 proteins such as transmembrane receptors, second messenger-associated proteins, protein kinases, phosphatases and cytoskeletal proteins and these interactions have been shown to require one or more of the repeat elements in the rod domain.

Centromere Protein U, also known as CENPU is a specialized chromatin domain, present throughout the cell cycle. CENPU performs as a platform on which the transient assembly of the kinetochore takes place during mitosis. CENPU plays a major role in the correct PLK1 localization to the mitotic kinetochores. A scaffold protein is responsible for the first recruitment and maintenance of the kinetochore PLK1 population until its degradation. CENPU is also implicated in transcriptional repression.

GNAQ, also known as Guanine nucleotide-binding protein belong to the G-alpha family. Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in a variety of transmembrane signaling systems. GNAQ regulates B-cell selection and survival and is essential in order to prevent B-cell-dependent autoimmunity. GNAQ also regulates chemotaxis of BM-derived neutrophils and dendritic cells, in vitro. GNAQ is an alpha subunit in the Gq class, couples aseven-transmembrane domain receptor to activation of phospolipase C-beta. Mutations at this locus have beenconnected with problems in platelet activation and aggregation. A related pseudogene to GNAQ exists on chromosome 2.

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).

PTGES3 takes part as a cochaperone and is involved in signal transduction.
PTGES3 is a molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexess. PTGES3 is necessary for appropriate functioning of the glucocorticoid and other steroid receptors.
PTGES3 localizes to genomic response elements in a hormone-dependent method and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexes.

Flagellin FliA (H), also known as RNA polymerase sigma factor for flagellar operon, Sigma F and Sigma-28, is a part of the FliA subfamily or sigma-70 factor family. This sigma factor controls the expression of flagella-related genes. Flagellin FliA (H) regulates the expression of genes involved in virulence. Flagellin FliA (H) is an initiation factors which endorses the attachment of RNA polymerase to specific initiation sites and are then released.

Kallikrein-15 (KLK15) is one of the 15 kallikrein subfamily members located in a cluster on chromosome 19. KLK15 contains numerous polyadenylation sites and alternative splicing results in multiple transcript variants encoding different isoforms. KLK15 is over expressed in prostate cancer and therefore uses as a diagnostic or prognostic marker for prostate cancer.