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Btc is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. The effects of betacellulin are probably mediated by the egf receptor and other related receptors.

Defensins form a family of microbicidal and cytotoxic peptides made by neutrophils. Members of the defensin family are highly similar in protein sequence. This gene encodes defensin, beta 103A, which has broad spectrum antimicrobial activity and may play an important role in innate epithelial defense.

Leucine Aminopeptidase 3 also known as LAP3 is a member of the peptidase M17 family. LAP3 is implicated in the processing as well as regular turnover of intracellular proteins. LAP3 catalyzes the removal of unsubstituted N-terminal amino acids from different peptides. LAP3 is responsible of releasing an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but could be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are as well readily hydrolyzed; however rates on arylamides are exceedingly low.

BAT1 belongs to the DEAD box family of RNA-dependent ATPases that mediate ATP hydrolysis during pre-mRNA splicing. UAP56 protein is a vital splicing factor which is needed for connecting U2 small nuclear ribonucleoprotein with pre-mRNA, as well as takes a key part in mRNA export from the nucleus to the cytoplasm. Mutations in this protein may be connected to rheumatoid arthritis.

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.

SURA is a PPIase enzyme and chaperone of Escherichia coli and other Gram-negative bacteria. SURA is a key player in the biogenesis of beta-barrel outer membrane proteins and is involved in cell envelope homeostasis and cell envelope functions. SURA is necessary for the survival of E.coli in stationary phase and needed for pilus biogenesis.

BLMH is affiliate to the papain superfamily of the cysteine protease and the peptidase C1 family. BLMH is a cytoplasmic cysteinepeptidase usually found as a homohexamer. BLMH shields normal and malignant cells from the glycopeptide antitumor drug BLM. BLMH catalyzes the inactivation of the antitumor drug BLM (a glycopeptide) by hydrolyzing the carboxyamide bond of its B-aminoalaninamide moiety and in addition demonstrates general aminopeptidase activity.

Serine racemase (SRR) is an enzyme which generates D-serine from L-serine. D-serine functions as a neuronal signaling molecule by activating NMDA receptors in the brain. Mammalian SRR is a pyridoxal 5'-phosphate dependent enzyme which catalyzes both the racemization of L-serine to D-serine and also the elimination of water from L-serine, producing pyruvate and ammonia. The SRR enzyme is physiologically stimulated by divalent cations (e.g., magnesium) and is allosterically activated by the magnesium/ATP complex.

The proteasome is a multicatalytic proteinase complex with an extremely organized ring-shaped 20S core structure. The core structure consists of 4 rings of 28 non-identical subunits; 2 rings consist of 7 alpha subunits and 2 rings consist of 7 beta subunits. Proteasomes are spread all over the eukaryotic cells in large quantities and cleave peptides in an ATP/ubiquitin-dependent procedure in a non-lysosomal pathway. A vital role of a modified proteasome, the immunoproteasome, is the handling of class I MHC peptides.

Chitinase is a digestive enzyme which breaks down glycosidic bonds in chitin. Due to chitin being a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods), chitinases are usually found in organisms that either need to remake their own chitin or to dissolve and digest the chitin of fungi or animals. Chitinivorous organisms include many bacteria genuses such as Aeromonas, Bacillus, Vibrio, among others, which may be pathogenic or detritivorous. Chitinase expression is mediated by the NPR1 gene and the salicylic acid pathway, both of which are involved in resisting fungal and insect attack. Human chitinases appear in gastric juices. They are likely to be digestive chitinases, for catabolic activity. Chitinase activity is identified systemically in humans, in the blood, and possibly cartilage. Chitinase has been related to allergies, asthma in particular has been linked to enhanced chitinase expression levels, also dust mites and mold spores which are both chitin covered.

The Defensin family are highly similar in their protein sequence and are microbicidal & cytotoxic peptides made by neutrophils. Beta Defensin-1 is an antimicrobial peptide having the resistance of epithelial surfaces to microbial colonization. Beta Defensin-1 has close proximity to Defensin Alpha-1 and has been implicated in the pathogenesis of cystic fibrosis.
Skin of patients having atopic dermatitis patients and mycosis fungoides (non-lesional and lesional) show lower human Beta Defensin-1 mRNA expression and higher human Beta Defensin-2 and human Beta Defensin-3 mRNA expression.
Beta Defensin is highly expressed by epithelial cells.
Beta-defensin 1 may play a role in the pathogenesis of severe sepsis.

Serratia marcescens secretes an endonuclease that has exceptionally high specific activity to the medium that surrounds it. The Benzonase Nuclease is mainly used for elimination of nucleic acid contamination from purified proteins, downstream processing, reduction of viscosity etc. Nucleic acid contaminants are caused by nuclease released to the medium. The DNA is being destroyed by the release of the S. marcescens nuclease and it acts as the killer gene for the auto destruction of microorganisms.

Enteropeptidase or enterokinase is an enzymeinvolved in human digestion. It is produced by cells in the duodenum wall, and is secreted from duodenum's glands, the crypts of Lieberk?hn, whenever ingested food enters the duodenum from the stomach. Enteropeptidase has the critical job of turning trypsinogen(a zymogen) to trypsin, indirectly activating a number of pancreaticdigestive enzymes.
Enteropeptidase is a serine proteaseenzyme(EC3.4.21.9). Enteropeptidase is a part of the Chymotrypsin-clan of serine proteases, and is structurally similar to these proteins.

SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1?/CXCL12a and SDF-1?/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor.
The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively.

Alpha and Beta Defensins are cationic peptides with antimicrobial activity against Gram-negative and Gram-positive bacteria, fungi and enveloped viruses. These 2-6kDa proteins have vital roles in innate immune system. Mammalian Defensins are classified into alpha, beta and theta categories, based on their size and pattern of disulfide bonding. Beta-Defensins contain a six-cysteine motif which forms 3 intra-molecular disulfide bonds. Since beta-defensins are cationic peptides, they can therefore interact with the membrane of invading microbes, which are negative due to lipopolysaccharides (LPS) and lipoteichoic acid (LTA) found in the cell membrane. In addition, they can affect the stability of the membrane.

L-lactate dehydrogenase (lldD) is present in a various organisms, including plants and animals. lldD is an oxidoreductase which catalyses the interconversion of pyruvate and lactate with concurrent interconversion of NADH and NAD+. Seeing that lldD can catalyze the oxidation of hydroxybutyrate, it is occasionally called Hydroxybutyrate Dehydrogenase (HBD).

Defensins are cationic peptides with a large spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The Alpha defensins are differentiated from the Beta-defensins by the pairing of their 3 disulfide bonds.
4 human Beta-defensins have been identified to date; BD-1, BD-2, BD-3 and BD-4.
Beta-defensins are expressed on some leukocytes and at epithelial surfaces.
In addition to their direct antimicrobial activities, they are chemoattractant towards immature dendritic cells and memory T cells. The beta-defensin proteins are expressed as the C-terminal portion of precursors and are released by proteolytic cleavage of a signal sequence and, in the case of BD-1 (36 a.a.), a propeptide region. Beta-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. Beta-Defensins are 3-5 kDa peptides ranging in size from 33-47 amino acid residues.

Core 1 Beta3-Gal-T1 also known as,C1GALT1 creates the common core 1 O-glycan structure, Gal-beta-1-3GalNAc-R, by the transfer of Gal from UDP-Gal to GalNAc-alpha-1-R. Core 1 is a precursor for lots of extended mucin-type O-glycans on cell surface and secreted glycoproteins. Studies in mice have shown that this gene takes a main role in angiogenesis, thrombopoiesis and kidney homeostasis.

Cathepsin-A (CTSA) is a protective protein which is crucial for both the activity of beta-galactosidase and neuraminidase, CTSA associates with these enzymes and exerts a protective function required for their stability and activity. The CTSA protein is also a carboxypeptidase and can deamidate tachykinins. CTSA is a component of the lysosomal multienzyme complex along with beta-galactosidase and sialidase Neu1. CTSA is a multicatalytic enzyme with deamidase and esterase in addition to carboxypeptidase activities.

Btc is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. The effects of betacellulin are probably mediated by the egf receptor and other related receptors.

LCAT is an extracellular cholesterol esterifying enzyme, lecithin-cholesterol acyltransferase. The esterification of cholesterol is required for cholesterol transport. LCAT is a essential enzyme in the extracellular metabolism of plasma lipoproteins.

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.

SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1?/CXCL12a and SDF-1?/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor.
The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively.

DNA polymerase beta (POLB) is a member of the DNA polymerase type-X family. In eukaryotic cells, POLB performs base excision repair necessary for DNA maintenance, replication, recombination, and drug resistance. POLB has 2 separate domains; the larger is the polymerase domain itself, whereas a small basic N-terminal domain contains an AP lyase activity which excises the abasic sugar-phosphate residue at the strand break. POLB fills single nucleotide gaps in DNA produced by the base excision repair pathway of mammalian cells. POLB overexpression, as seen in some human tumors, could convene an increase in spontaneous mutagenesis.