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GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for this gene. Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.

HOXB13 is a transcription factor and a member of the homeobox gene family which are extremely conserved in vertebrates and vital for vertebrate embryonic development. HOXB13 is involved in fetal skin development and cutaneous regeneration. In mice, a similar gene displayed temporal and spatial colinearity in the main body axis of the embryo, however it was not expressed in the secondary axes, implying that it has a roles in body patterning along the axis.

The OmpA protein is one of the main outer-membrane proteins of a large array of Gram-negative bacteria such as A.salmonicida, Shigella dysenteriae and E.coli.OmpA’s major physiological functions include maintenance of the structural integrity and morphology of the cells and porin activity, as well as a role in conjugation and bacteriophage binding.Achromogenic atypical Aeromonas salmonicida is the causative agent of goldfish ulcer disease.Virulence of this bacterium is associated with the production of a paracrystalline outer membrane A-layer protein.The species specific structural gene for the monomeric form of A-protein was cloned into a pET-3d plasmid in order to express and produce a recombinant form of the protein in E.coli BL21(DE3). The induced protein was isolated from inclusion bodies by a simple solubilization-renaturation procedure and purified by ion exchange chromatography on Q-Sepharose to over 95% pure monomeric protein.Recombinant A-protein was compared by biochemical, immunological and molecular methods with the A-protein isolated from atypical A.salmonicida bacterial cells by the glycine and the membrane extraction methods.

UCN119B is a member of the PDE6D/unc-119 family. UCN119B has a large number of photoreceptors of the retina. Additionaly, UCN119B has a strong homology with the C. elegans unc119 and is able to functionally complement the C. elegans unc119 mutation gene.

ERO1-like protein alpha (ERO1L) is an essential oxidoreductase, which oxidizes proteins and is necessary for the folding of immunoglobulins. ERO1L covalently binds with PDI (protein disulfide-isomerase) and jointly they generate disulfide bonds between proteins in the endoplasmic reticulum. ERO1L is stimulated by hypoxia, proposing that ERO1L is regulated through the HIF (hypoxia inducible transcrip-tion factor) pathway. At low levels ERO1L is ubiquitously expressed, however at high levels it is expressed in the upper digestive tract and esophagus. In addition, ERO1L is involved in the release of the unfolded cholera toxin from reduced P4HB/PDI in case of infection by V.cholerae, thus having a role in retrotranslocation of the toxin. Furthermore, ERO1L plays an important role in ER stress-induced, CHOP-dependent apoptosis by activating the inositol 1,4,5-trisphosphate receptor IP3R1.

LRRC59 controls nuclear import of exogenous FGF1 by enabling interaction with the nuclear import mechanism and by transporting cytosolic FGF1 to and through the nuclear pores. LRRC59 is essential for nuclear import of FGF1, but not that of FGF2.

MCL1 is a member of the Bcl-2 family. MCL1 takes part in the control of apoptosis against cell existence, and in the preservation of viability but not of proliferation. Alternative splicing happens at this locus and two transcript variants encoding different isoforms are known. Isoform 1 is the longer gene product and it increases cell existence by inhibiting apoptosis. Isoform 2 is a shorter gene product which indorses apoptosis and is death-inducing.

Synaptobrevin 2 which is an 18 kDa integral membrane protein localized to the cytoplasmic surface of synaptic vesicle, consists of a proline-rich N-terminal region, a highly conserved hydrophilic domain, followed by a transmembrane anchor and a C-terminal. Synaptobrevin 2 is predominantly expressed in Langerhans islets and glomerular cells. The N-terminal domain of the protein (residues 1-89) forms a specific SNARE complex with the target membrane-associated t- or Q-SNAREs syntaxin 1 and SNAP-25.

BPI fold containing family A Member 1 (BPIFA1) belongs to the short subfamily of PLUNC family proteins and have homology only to the Nterminal domains of BPI. BPIFA1 is a secreted protein which is expressed in the secretory ducts and submucosal glands of tracheobronchial tissues. BPIFA1 binds to LPS (lipopolysaccharide) in nasal lavage fluid (NLF) which alludes to its role in the inflammatory response of the upper airways after exposure to irritants. BPIFA1 may also serve as a potential molecular marker for detection of micrometastasis in non-small-cell lung cancer. Decreased levels of BPIFA1 are observed in the NLF of smokers and people who have been exposed to reactive epoxy chemicals, which indicats that long-term exposure to airway irritants damages the production of BPIFA1 in the upper respiratory tract.

Von Willebrand Factor A Domain Containing 2 (VWA2) is an extracellular matrix protein containing vWA-like domains. VWA2 contains a signal peptide sequence, an N-terminal VWA domain connected to 2 additional tandem vWA domains by a cysteine-rich sequence and an EGF-like domain. Also, another EGF-like domain is located at the C-terminus. Expression of VWA2 is induced in stage II, III and IV colon cancers and colon adenomas and is considered a novel serum marker for the diagnosis of early-stage colon cancer.

GAP43 is a phosphoprotein of the presynaptic membrane that takes part in synaptic reorganization and neural development. GAP43 is found in large quantities in neuronal growth cones all through the development and axonal regeneration. Additionally, GAP43 is involved in specific regions of the normal adult nervous system and has a vital part in the conservation mechanism of long-term potentiation (LTP).

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.

Amino-terminal enhancer of split (AES) is a member of the groucho/TLE family of proteins. AES can function as a homooligomer or as a heteroologimer with other family members in order to forcefully repress the expression of other family member genes. Furthermore, AES can repress NFkB-regulated gene expression and is believed to have a significant role in initiating and maintaining cell differentiation events. AES is similar in sequence to the amino terminus of Drosophila enhancer of split groucho, a protein which is involved in neurogenesis during embryonic development. The AES protein is expressed predominately in the fetal brain, liver, lung, heart and kidney and also in the adult muscle.

MYL7 protein is an atrial isoform of myosin regulatory light chain 2 (MYL2). Myosin is a hexamer containing 4 light chains and 2 heavy chains. MYL7 is mainly expressed in adult atrial muscle.

RBM3 belongs to the glycine-rich RNA-binding protein family and encodes a protein with one RNArecognition motif (RRM) domain. By cold shock and low oxygen tension the expression of this gene is induced. On chromosome 1 a pseudogene exists. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.Diseases associated with RBM3 include vaccinia, andcryptorchidism. GO annotations linked to this gene include RNA binding and ribosomal large subunit binding. An important paralog of this gene is RBMY1J.

Vanin 1 (VNN1) belongs to the vanin family of proteins, which share extensive sequence similarity with each other, and also with biotinidase. This family includes secreted and membrane-associated proteins, a few of which have been described to participate in hematopoietic cell trafficking. No biotinidase activity has been established for any of the vanin proteins; nevertheless, they possess pantetheinase activity, which may have a role in oxidative-stress response. VNN1 protein, like its mouse homolog, is probably a GPI-anchored cell surface molecule. The mouse VNN1 protein is expressed by the perivascular thymic stromal cells and regulates migration of T-cell progenitors to the thymus. VNN1 is an amidohydrolase which hydrolyzes specifically one of the carboamide linkages in D-pantetheine thus recycling pantothenic acid (vitamin B5).

Galectins are a family of animal lectins with an affinity for beta-galactosides. This family has at least 14 identified members. Galectins share similarities in the CRD (the carbohydrate recognition domain). Galectins are synthesized as cytosolic proteins. Though localized principally in the cytoplasm and lacking a classical signal peptide, galectins can also be stimulated to secretion by non-classical pathways or alternatively targeted to the nucleus. Galectins are involved in modulating cell-cell and cell-matrix interactions. Human Galectin-7 belongs to the prototypical Galectins containing a single CRD, which is initially identified in human epidermis as a monomer. The Galectin-7 expression is induced by tumor suppressor protein p53 and associated with apoptosis. Galectin-7 is a pro-apoptotic protein which functions intracellularlly upstream of JNK activation and mitochondrial cytochrome c release. The correlation of Galectin-7 with the UV-induced apoptosis of keratinocytes presents a critical mechanism in the maintenance of epidermal homeostasis. Human Galectin-7 is localized in both nucleus and cytoplasm.

BIRC7 is a part of the inhibitor of apoptosis protein (IAP) family and contains a single copy of a baculovirus IAP repeat (BIR) as well as a RING-type zinc finger domain. The BIR domain is necessary for inhibitory activity & cooperates with caspases, while the RING finger domain sometimes increases anti-apoptotic activity but doesn’t inhibit apoptosis by itself. 2 transcript variants encoding diverse isoforms have been found for this gene. The 2 isoforms have dissimilar antiapoptotic characteristics, with isoform a protecting cells from apoptosis induced by staurosporine and isoform b defending cells from apoptosis induced by etoposide.
BIRC7 has direct contact with several caspases together with caspase-3, caspase-7, & caspase –9. BIRC7 inhibits the activation of caspase-9 induced by Apaf-1, cytochrome c, and dATP.

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.

RAET1E is a member of the MHC class I family. MHC class I family contains main histocompatibility complex (MHC) class I-related genes positioned in a cluster on chromosome 6q24.2-q25.3. RAET1E and RAET1G protein are different from other RAET1 proteins since they have type I membrane-spanning sequences at their C termini instead glycosylphosphatidylinositol anchor sequences.RAET1E acts as a ligand for NKG2D receptor, expressed on the surface of numerous types of immune cells, involves in innate adaptive immune reactions.RAET1E delivers signals to NK cells and advances tumor immune surveillance by inducing the growth of anti-tumor cytotoxic lymphocyte.

Collagen, a major component of the extracellular matrix, is a fibrous protein that provides tensile strength to tissues giving them structural integrity. Collagen and its derivative, gelatin, have been widely used in medical, pharmaceutical and consumer products for more than 100 years. The supply of these materials, created from animal remains, is both abundant and inexpensive. However, most formulations are not highly purified and have the potential to cause an inflammatory reaction in some product users. In addition, concerns have been raised over the last several years about the potential for contamination of bovine products with the agent that causes mad cow disease and its human variant, Creutzfeldt-Jakob Disease. Animal collagens are subject to extensive modifications that continue over the life of the molecule in the extracellular space. These differences influence both the extractability of collagens from tissue and the biophysical characteristics of these collagens. As a result, collagens isolated from tissues exhibit significant lot-to-lot variability and, as bulk materials, are often analytically intractable. Products that contain animal-derived collagen can induce potentially harmful inflammatory or immune responses in humans and pose risk of contamination with viruses or prions, potentially life-threatening pathogens. Recombinant collagens are essentially identical to the native collagen protein thereby reducing the risk of inflammation, immune response, and disease as compared to animal-sourced collagen.

Fractalkine soluble form is chemotactic for t-cells and monocytes, but not for neutrophils. Fractalkine membrane-bound form promotes adhesion of those leukocytes to endothelial cells. Fractalkine regulates leukocyte adhesion and migration processes at the endothelium and binds to CX3CR1. Natural Human Fractalkine is produced as a long protein (373-amino acid) with an extended mucin-like stalk and a chemokine domain on top. The mucin-like stalk permits it to bind to the cell surface. Fractalkine gene is located on human chromosome 16 along with some CC chemokines known as CCL17 and CCL22.

GroEL, HSP60 is a chaperonin located in the mitochondria which is responsible for the transportation & refolding of proteins from the cytoplasm directly into the mitochondrial matrix. GroEL is regulated by the HSP10 cochaperonin, which is a single heptameric protein ring having a molecular mass of 10 kDa which form a unique complex with HSP60. HSP10, GroES coordinates the ATPase activity of the HSP60 subunits in order to allow the release of bound polypeptide in a manner that is productive for its correct folding.