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Guanine nucleotide binding proteins are heterotrimeric signal-transducing molecules comprising alpha, beta, and gamma subunits. GNAI1 represents the alpha subunit of an inhibitory complex. Guanine nucleotide-binding protein G(i) subunit alpha (GNAI1) functions to transmit information from cell surface receptors to intracellular effectors. GNAI1 binds guanine nucleotide, can hydrolyze GTP, and can interact with other proteins. GNAI1 is part of a complex that responds to beta-adrenergic signals by inhibiting adenylate cyclase. In addition, GNAI1 functions to open atrial potassium channels.

Chromogranin A is a 439 amino acid protein which is encoded on chromosome 14 and is present in neuroendocrine cells throughout the body, including the neuroendocrine cells of the large and small intestine, adrenal medulla and pancreatic islets. It is an excellent marker for carcinoid tumors, phenochromocytomas, paragangliomas, and other neuroendocrine tumors.
Coexpression of chromogranin A and neuron specific enolase (NSE) is common in neuroendocrine neoplasms.

RNA binding motif protein 17 (RBM17) is a splice factor which binds to the single stranded 3'AG at the exon/intron border and promotes its utilization in the 2nd catalytic step. The RBM17 protein is involved in the regulation of alternative splicing and the utilization of cryptic splice sites. RBM17 protein also stimulates the utilization of a cryptic splice site created by the beta-110 mutation in the HBB gene. The ensuing frameshift leads to sickle cell anemia.

CRH is a powerful stimulator of synthesis and secretion of preopiomelanocortin-derived peptides. CRH concentration in the human peripheral circulation is usually low. The concentration rises during pregnancy and fall back quickly after parturition. Maternal plasma CRH most likely originates from the placenta. Human plasma has a CRH-binding protein that inactivates CRH and can inhibit inappropriate pituitary-adrenal stimulation in pregnancy.

Non-Metastatic Cells 2 or NME2, is a protein, that acts as a nucleoside diphosphate kinase. This protein is of a heterodimeric structure and has 152 aa A & B polypeptide chains that builds the whole protein. Erythrocyte NDP kinase beta subunit has an identical structure to NME2. NDP kinases linked to nucleoside triphosphates synthesis and it appears as though NME2 takes part in regulating signal transduction.

Lysostaphin, an endopeptidase specific for the cell wall peptidoglycan of staphylococci, is an extremely potent anti-staphylococcal agent. Lysostaphin is used as a research and diagnostic tool. Because it lyses staphylococci efficiently, it is widely used when preparing staphylococcal DNA or other cellular components for genetic and biochemical studies and for the preparation of protoplasts for transformation. Preparation and analysis of bacterial DNA has become a powerful tool used by clinical and other microbiologists in epidemiological studies aimed at tracing sources of infection or bacterial contamination.

Crk-like protein (CRKL) is a protein kinase containing SH2 and SH3 (src homology) domains which activates the RAS and JUN kinase signaling pathways and transforms fibroblasts in a RAS-dependent manner. CRKL is a substitute of the BCR-ABL tyrosine kinase, it also has a role in fibroblast transformation by BCR-ABL, and has oncogenic potential.

CRYGC is a member of the beta/gamma-crystallin family. Mammalian lens crystallins are distributed into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Gamma-crystallins are a homogeneous group of extremely symmetrical, monomeric proteins usually missing connecting peptides and terminal extensions and are differentially regulated after early development. Three pseudogenes (gamma-E,F,G) and four gamma-crystallin genes (gamma-A,B,C,D) are structured in a genomic sector as a gene cluster. Gamma-crystallins are involved in cataract formation as a result of aging or mutations in specific genes. Mutations in CRYGC result in cataract Coppock-like (CCL) and cataract autosomal dominant (ADC).

S100b is a member of the S100 family of proteins which are a family of EF-hand calcium binding proteins that exist mostly as dimers of the 20 currently identified individual S100 monomers. The S100B homodimer is expressed in cells of the central nervous system, glial cells and in certain peripheral cells e.g. Schwann cells, melanocytes, adipocytes and chondrocytes. S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. S100 proteins are involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21; however, S100b is located at 21q22.3. The determination of S100B in serum levels may be used to monitor the extent of brain injury and malignant melanoma. S100b proteins may have a role in Neurite extension, proliferation of melanoma cells, stimulation of Ca2+ fluxes, inhibition of PKC-mediated phosphorylation, astrocytosis and axonal proliferation, and inhibition of microtubule assembly. Chromosomal rearrangements and altered expression of the S100b gene are implicated in several neurological, neoplastic, and other types of diseases, including Alzheimer's disease, Down's syndrome, epilepsy, amyotrophic lateral sclerosis, melanoma, and type I diabetes.

MMADHC is a mitochondrial protein which takes part in an early step of vitamin B1 2 metabolism. Vitamin B12 (cobalamin) is vital for regular development and existence in humans. Mutations in MMADHC can result in methylmalonic aciduria and homocystinuria type cblD, a cobalamin metabolism syndrome which is characterized by decreased levels of the coenzymes methylcobalamin and adenosylcobalamin.

Peptidyl-prolyl cis-trans isomerase F, mitochondrial (Cyclophilin-F) accelerates the folding of proteins. Cyclophilin-F catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and involved in regulation of the mitochondrial permeability transition pore (mPTP). Cyclophilin-F, in cooperation with mitochondrial TP53, is involved in activating oxidative stress-induced necrosis. Cyclophilin-F is also involved in modulation of mitochondrial membrane F1F0 ATP synthase activity and regulation of mitochondrial matrix adenine nucleotide levels. Furthermore, Cyclophilin-F has anti-apoptotic activity independently of mPTP and in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis.

Dihydrofolate reductase (DHFR) is an enzyme that reduces dihydrofolic acid to tetrahydrofolic acid, with NADPH as electron donor that can be converted to the kinds of tetrahydrofolate cofactors applied in 1-carbon transfer chemistry. DHFR converts dihydrofolate into tetrahydrofolate, which is a methyl group shuttle required for the de novo synthesis of purines, thymidylic acid, and specific amino acids. Even though the functional DHFR gene is mapped to chromosome 5, numerous intronless processed pseudogenes or dihydrofolate reductase-like genes are identified on separate chromosomes. DHFR deficiency is associated with megaloblastic anemia. DHFR knockdown plays a role in the anticancer activity of 2-hydroxyoleic acid. DHFR gene insertion/deletion polymorphism is linked to variation in serum and red blood cell folate concentrations in women.

Annexin VII is a member of the annexin family of calcium-dependent phospholipid binding proteins. Annexin VII has molecular weight of approximately 51 kDa with a unique, highly hydrophobic N-terminal domain of 167 amino acids and a conserved C-terminal region of 299 amino acids. The latter domain is composed of alternating hydrophobic and hydrophilic segments. Structural analysis of the protein suggests that Annexin VII is a membrane binding protein with diverse properties including voltage-sensitive calcium channel activity, ion selectivity and membrane fusion.

DLD is an L protein of the mitochondrial glycine cleavage system which is also a component of the pyruvate dehydrogenase complex, the alpha-ketoglutarate dehydrogenase complex, and the branched-chain alpha-keto acide dehydrogenase complex. DLD mutations were found in patients with E3-deficient maple syrup urine disease and lipoamide dehydrogenase deficiency.

Rho GDP-dissociation inhibitor 1 (ARHGDIA) is a member of the RAS gene superfamily, which encodes small guanine nucleotide exchange (GTP/GDP) factors. ARHGDIA, which is localized to the cytoplasm, inhibits the dissociation of GDP from Rho proteins, thus preventing GTP from binding to and consequently activating Rho proteins. In humans, the ARHGDIA can be phosphorylated at Ser 101 by p21-activated kinase, an event that inhibits its activity and may result in positive feedback regulation of several ARHGDIA target proteins.

ARL11 (ADP-ribosylation factor-like protein 11) belongs to the ARF family of the Ras superfamily of small GTPases which are known to be involved in multiple regulatory pathways altered in human carcinogenesis. ARFs are highly conserved guanine nucleotide binding proteins which enhance the ADP-ribosyltransferase activity of choleratoxin. ARFs are important in eukaryotic vesicular trafficking pathways and they have a vital role in the activation of phospholipase D (PC-PLD). ARL11 is assumed to act as a tumor suppressor which may have a role in the regulation of apoptosis.

SlyD accessiton#: NP_755987 is a putative folding helper protein from the Escherichia coli cytosol, which has N-terminal prolyl isomerase domain of the FKBP type and a most likely unstructured C-terminal tail. SlyD is an important factor in the biosynthesis of the metal cluster in the [NiFe]-hydrogenase enzymes, and exhibits several activities including that of a peptidyl-prolyl isomerase.

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).

Superoxide dismutase Mn (soda) belongs to the iron/manganese superoxide dismutase family. SodA destroys radicals that are typically produced within the cells and which are toxic to biological systems. SodA works by catalyzing the dismutation of the superoxide radical O2- to O2 and H2O2, which are then metabolized to H2O and O2 by catalase and glutathione peroxidase.

SRGN is identified as a hematopoietic cell granule proteoglycan. Proteoglycans stored in the secretory granules of various hematopoietic cells also hold a protease-resistant peptide core, and is vital for neutralizing hydrolytic enzymes. SRGN is related to the macromolecular complex of granzymes and perforin that acts as a intermediary of granule-mediated apoptosis.

Sorcin (SRI) which is a 22kDa calcium-binding protein was originally identified in multidrug-resistant cells. Sorcin, which modulates excitation-contraction coupling in the heart, contributes to calcium homeostasis in the heart sarcoplasmic reticulum.

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.

Eotaxin-2, also called MPIF2 & Ckb6, is a novel CC chemokine produced by activated monocytes and T lymphocytes. Eotaxin-2 selectively chemoattracts cells expressing CCR3 including eosinophils, basophils, Th2 T cells, mast cells, and certain subsets of dendritic cells. Furthermore, Eotaxin-2 inhibits the proliferation of multipotential hematopoietic progenitor cells. The mature protein, which includes C-terminal truncation, contains 78 amino acids (92 amino acids for the mouse homolog, without C-terminal truncation).
CCL24 functions as a chemotactic chemokine for resting t-lymphocytes, and eosinophils. CCL24 has lower chemotactic activity for neutrophils but none for monocytes and activated lymphocytes. CCL24 is a strong suppressor of colony formation by a multipotential hematopoietic progenitor cell line and binds to CCR3.

Osteocrin is a recently identified secreted protein expression of which was only detected in bone, peaking just after birth and decreasing markedly with age. A 1280-bp mRNA encodes osteocrin producing a mature protein of 103 amino acids with a molecular mass of 11.4 kDa. In primary osteoblastic cell cultures osteocrin expression coincided with matrix formation then decreased in very mature cultures. Treatment of cultures with 1,25-dihydroxyvitamin D3 resulted in a rapid dose- dependent down-regulation of osteocrin expression, suggesting direct regulation. Chronic treatment of primary cultures with osteocrin-conditioned media inhibited mineralization and reduced osteocalcin and alkaline phosphatase expression. These results suggest that osteocrin represents a novel, unique vitamin D-regulated bone-specific protein that appears to act as a soluble osteoblast regulator.