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RPS24 is a member of the S24E family of ribosomal proteins. RPS24 is situated in the cytoplasm. Numerous transcript variations encoding different isoforms were identified for this gene. There are multiple processed pseudogenes of this gene distributed all over the genome just like other genes encoding ribosomal proteins. Alterations in RPS24 cause Diamond-Blackfan anemia.

The recombinant Protein A/G/L is a genetically engineered protein which combines the IgG binding profiles of all Protein A, Protein G and Protein L. Protein A/G/L is a gene fusion product. Recombinant fusion protein A/G/L is comprised of 5 Ig-binding regions of protein L (B1-B2-B3-B4-B5), 5 IgG binding domains from Protein A (E-D-A-B-C) and 2 Ig-binding region of protein G (C1-C3). The recombinant Protein A/G/L is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G/L binds to IgG from humans, mice, rats, cows, goats, sheep, rabbits, guinea pigs, pigs, dogs and cats.

ATOX1 is a metal transport protein that is part of the ATX1 family. ATOX1 is a copper chaperone that takes part in cellular antioxidant defense and can bind and deliver cytosolic copper to the copper ATPase proteins in the trans-Golgi network for later incorporation to the ceruloplasmin. ATOX1 plays a role as an antioxidant against superoxide and hydrogen peroxide, and consequently, takes an important part in cancer carcinogenesis. Because of ATOX1 cytogenetic location, the gene can be a good a candidate gene for 5q-syndrome.

Processing of Precursor 4 (POP4) is a member of the eukaryotic/archaeal RNase P protein component 1 family. POP4 is one of the protein subunits of the small nucleolar ribonucleoprotein complexes: the endoribonuclease for mitochondrial RNA processing complex and the ribonuclease P complex. POP4 is confined to the nucleus and associates promptly with the RNA component of this complexes.POP4 is participating in processing of precursor RNAs.

Inhibins are dimeric peptide hormones produced by female ovarian granulose cells and male Sertoli cells as well as a variety of other tissues. Inhibins have two isoforms, A and B, with the same alpha subunit but different beta subunits. Inhibin A is a dimer of alpha and beta A subunits, inhibin B is a dimer of alpha and beta B subunits.
Inhibins are thought to inhibit the production of follicle-stimulating hormone (FSH) by the pituitary gland. In addition, Inhibins are also thought to play a role in the control of gametogenesis, and embryonic and fetal development.

GNAI2 is an alpha subunit of guanine nucleotide binding proteins (G proteins) and holds a guanine nucleotide binding site. GNAI2 takes part in the hormonal regulation of adenylate cyclase. GNAI2 has varies transcript variants encoding different isoforms yet only two full-length isoforms were identified up to date.

Ras-related protein Ral-A (RALA) is a member of the small GTPase superfamily, Ras family of proteins. RALA mediates a distinct downstream signaling pathway from Ras which facilitates cellular transformation. Furthermore, RALA is thought to be involved in various signaling cascades, including regulation of the cytoskeleton, vesicle trafficking, and endocytosis.

S100A2 belongs to the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100A2 may function as a modulator against excess calcium accumulation in normal human mammary epithelial cells and also have a role in suppressing tumor cell growth. S100A2 may have a tumor suppressor function. S100 family members are localized in the cytoplasm and/or nucleus of a wide range of cells, and are involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. Chromosomal rearrangements and altered expression of the S100A2 gene are implicated in breast cancer.

Type IV collagen is a major structural component of basement membranes. It is a multimeric protein composed of 3 alpha subunits, which are encoded by 6 different genes, alpha 1 through alpha 6. Each of these alpha subunits can form a triple helix structure with 2 other subunits to form type IV collagen. The Goodpasture syndrome is a condition in which autoantibodies bind to the collagen molecules in the basement membranes of alveoli and glomeruli. The epitopes that elicit these autoantibodies are restricted basically to the non-collagenous C-terminal domain of the protein. There are numerous alternative transcripts that appear to be unique to the human COL4A3 and alternative splicing is limited to the six exons that encode this C-terminal domain. COL4A3 is also linked to an autosomal recessive form of Alport syndrome. The mutations contributing to the Alport syndrome are also situated within the exons that encode this C-terminal region. COL4A3 is organized in a head-to-head conformation with another type IV collagen gene so that each gene pair shares a common promoter. Several exons of COL4A3 are interspersed with exons of an uncharacterized gene which is on the opposite strand.

Thyroid Hormone Receptor Interactor 10 (TRIP10) is a part of the F-BAR family of proteins which is expressed in a variety of tissues, including kidney, brain, liver, lung, heart and pancreas. The F-BAR family of proteins contains an N-terminal, alpha-helical, region which is hydrophobic and related to the Bin Amphiphysin Rvs (BAR) protein family. TRIP10 is vital for the coordination of membrane tubulation with Actin cytoskeletal reorganization during endocytosis.

ADP-ribosylation factor-like protein 9 (ARL9) is a member of to 2 novel subfamilies coding for small GTPases that were found to be highly conserved among eukaryotes.

TEN1 is part of a complex that binds to single-stranded DNA and is necessary in order to protect telomeres from DNA degradation (CST complex). The CST complex binds single-stranded DNA with high affinity in a sequence-independent mode, while isolated subunits bind DNA with low affinity by themselves. Further to telomere protection, the CST complex has most likely a more general part in DNA metabolism at non-telomeric sites.

MBP is a major component of the myelin sheath of oligodendrocytes and Schwann cells in the nervous system, although, MBP-related transcripts are also present in the bone marrow and the immune system. These mRNAs emerge from the long MBP gene which holds three additional exons located upstream of the classic MBP exons. The Golli mRNAs contain three exons unique to Golli-MBP, spliced in-frame to one or more MBP exons. The second family of transcripts contains only MBP exons and produces the well characterized myelin basic proteins. MBP transcription unit is an essential part of the Golli transcription unit and the arrangement is important for the function and/or regulation of these genes.

Guanine Nucleotide Binding Protein Gamma 12, also known as GNG12 belongs to the Guanine nucleotide-binding proteins (G proteins) which are involved as a modulator or transducer in a variety of transmembrane signaling systems. In addition, the beta as well as gamma chains are essential for the GTPase activity, for replacement of GDP by GTP, and also for G protein-effector interaction.

40S ribosomal protein S5 (RPS5) is a ribosomal protein, which is a member of the ribosomal protein S7P family.Ribosomes, which are the organelles that catalyze protein synthesis, composed of a small subunit and a large subunit that comprise of over 80 distinct ribosomal proteins. RPS5 is a 204 amino acid component of the 40S complex. RPS5 proteins exist as multiple processed pseudogenes which are scattered throughout the genome. RPS5 is expressed at varying amounts in colorectal cancer cells, proposing a possible role in carconigenesis.

Axin interactor, dorsalization-associated (AIDA) operates as a ventralizing factor during embryogenesis. AIDA inhibits axin-mediated JNK activation by binding axin and disrupting axin homodimerization. That in turn antagonizes a Wnt/beta-catenin-independent dorsalization pathway activated by AXIN/JNK-signaling.

BETV6.0102 allergen is one of Isoflavone reductases which were found in pear, orange, apple, mango, lychee and other plants. Isoflavone reductases are plant defense proteins which induced by plant stress, e.g. high salinity, freeze or drought.

The Sec61 complex is the key component of the protein translocation apparatus of the ER (endoplasmic reticulum) membrane. Oligomers of the Sec61 complex construct a transmembrane channel where proteins are translocated across and incorporated into the ER membrane. This complex consists of 3 membrane proteins- alpha, beta, and gamma. The SEC61B gene encodes the beta-subunit protein. The Sec61 subunits are also detected in the post-ER compartment, suggesting that these proteins can get out of the ER and recycle back.

ARL15 is a member of the ARF family which are essential in eukaryotic vesicular trafficking pathways and have a vital part in the activation of phospholipase D. ARL15 variants influence levels of Acrp30, an adipocyte-derived protein that is extremely genetic and inversely related to the prospect of type 2 diabetes mellitus and coronary heart disease.

Migration And Invasion Enhancer 1 (MIEN1) is a member of the SelWTH family. MIEN1 enhances cell migration by stimulating filopodia formation at the leading edge of migrating cells and takes parts in regulation of apoptosis, probably via control of CASP3. MIEN1 participates in a redox-related process as well.

Leptin is a protein hormone. It is mainly produced in adipose cells that regulate energy homeostasis by restraining hunger. Leptin ties to nuclear receptors in the hypothalamus (arcuate nucleus). Similar to insulin resistance in type II diabetes, in obesity there is a decrease in the sensitivity towards leptin, ending in a failure to identify satiety, even in high levels of energy stores or leptin itself. Full-length cDNA encoding 2 leptin sequences (tLepA and tLepB) and 1 leptin receptor sequence (tLepR) exists in tilapia (Oreochromis niloticus). The full-length cDNA of tLepR is 3423 bp, encoding a protein of 1140 amino acid which contained all functionally important domains conserved among vertebrate leptin receptors. The cDNAs of tLepA and tLepB are 486 bp and 459 bp in length, encoding proteins of 161 aa and 152 aa, respectively. The three-dimensional structures of tLepA and tLepB demonstrates strong conservation of tertiary structure with that of human leptin comprised of 4 helixes.

Zinc-alpha-2-glycoprotein (ZAG) is found in body fluids such as serum, sweat, and seminal and breast cyst fluids. It is identical in amino acid sequence to tumor-derived lipid mobilizing factor (LMF), a protein associated with the dramatic loss of adipose body stores in cancer cachexia, and has been shown to stimulate lipolysis by adipocytes in vivo and in vitro. A role for ZAG has been proposed in the regulation of body weight, and age-dependent changes in genetically influenced obesity, and also it regulates melanin production by normal and malignant melanocytes. It has also recently been classified as a novel adipokine in that it is produced by both white and brown fat adipocytes and may act in a local autocrine fashion in the reduction of adiposity in cachexia. Controlling ZAG/LMF's activity could be life-saving in the management of certain cancers and other cachexiainducing conditions, and its possible normal role in body fat store homeostasis is deserving of understanding in its own right. ZAG exhibits a class I major histocompatibility complex (MHC) fold but is a soluble protein rather than being anchored to plasma membranes and does not associate with alpha-2-microglobulin in humans. Like antigen-presenting MHC class I proteins, ZAG has an open apical groove, and X-ray crystallography of human derived ZAG revealed an unidentifiable electron density in a similar position to that occupied by antigenic peptides in classical MHC proteins and glycolipids in isoforms of CD1. This presumptive ligand is not a peptide, and the groove is too small to hold a glycolipid such as is presented by CD1 isoforms. By analogy with all other MHC class I-related proteins that have an open apical groove [some do not ], occupancy by a ligand is probably crucial to ZAG's biological function. Despite all of the structural and biochemical evidence that ZAG binds a ligand, none has so far been found by extraction from protein isolated from biological fluids. This difficulty could be because the ligand is labile, heterogeneous, or readily lost during purification procedures. Knowing more about how ZAG interacts with the compounds it has been found to bind, both natural and artificial, will inform searches for the elusive ligand(s) and its/their role in ZAG's signaling function.

ANXA1 is part of the family of Ca(2+)-dependent phospholipid binding proteins which have a Mw between 35kDa-40kDa and are situated on the cytosolic face of the plasma membrane. ANXA1 protein has a Mw of 40kDa, with phospholipase A2 inhibitory activity to bind from two to four calcium ions with high affinity. Since phospholipase A2 is necessary for the biosynthesis of the potent mediators of inflammation, prostaglandins and leukotrienes, ANXA1 might have potential anti-inflammatory activity. ANXA1 promotes membrane fusion and iplays a role in exocytosis. The recognition of ANXA1 protein by immunocytochemical leads a simple, highly sensitive and specific assay for diagnosis of hairy cell leukemia.

VAMP5 is part of the vesicle-associated membrane protein (VAMP)/synaptobrevin family and the SNARE superfamily. VAMP5 is involved is vesicle trafficking events that are associated with myogenesis.