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Signal-Regulatory Protein Alpha, SIRPA belongs to the signal-regulatory-protein (SIRP) family, as well as theimmunoglobulin super family. The members of the SIRP family are receptor-type transmembrane glycoproteins which areinvolved in the negative regulation of receptor tyrosine kinase-coupled signaling processes. SIRPA can bephosphorylated by tyrosine kinases. The phospho-tyrosine residues of this PTP have been shown to recruit SH2domain containing tyrosine phosphatases (PTP), and perform as substrates of PTPs. SIRPA take part insignal transduction mediated by a variety of growth factor receptors. CD47 has been shown to be a ligand forSIRPA.

Calretinin is an intracellular calcium-binding protein belonging to the troponin C superfamily characterized by a structural motif described as the EF-hand domain. The immunohistochemical detection of calretinin in developing cerebellum is restricted to the later stages indicated by weak staining from week 21 of gestation, in Purkinje and basket cells and in neurons of the dentate nucleus. The intensity of staining increases as the cerebellum matures. In tumors, calretinin has been detected in mesotheliomas and some pulmonary adenocarcinomas.

OCIA domain-containing protein 2 (OCIAD2) is a protein-coding gene which localizes to endosomes and contains one Ovarian carcinoma immunoreactive antigen (OCIA) domain. Among the associated diseases with OCIAD2 are bronchiolo-alveolar adenocarcinoma, and ovarian mucinous neoplasm. OCIAD1 is an important paralog of this gene.

The bone morphogenetic proteins (BMPs) are a family of secreted signaling molecules that can induce ectopic bone growth. Many BMPs are part of the transforming growth factor-beta (TGFB) superfamily. BMPs were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. Based on its expression early in embryogenesis, the BMP encoded by this gene has a proposed role in early development. In addition, the fact that this BMP is closely related to BMP5 and BMP7 has lead to speculation of possible bone inductive activity.

Elongator Acetyltransferase Complex Subunit 4, also known as ELP4 is a protein coding gene which is a subunit of the RNA polymerase II elongator complex. ELP4 complements phenotypes of yeast ELP4 deletion mutants and is related to Rolandic epilepsy.

UMP-CMP kinase and deoxycytidylate kinase (CMPK1) is an enzyme which catalyzes the phosphoryl transfer from ATP to UMP, CMP and dCMP. This enzymatic reaction brings about the formation of ADP and the corresponding nucleoside diphosphate that are necessary for cellular nucleic acid synthesis. In addition, CMPK1 has a significant role in the activation of pyrimidine analogs, which are clinically useful anti-cancer and anti-viral drugs.

Ribosomal Protein L5, also known as RPL5 is a part of the ribosomal protein L18P family. RPL5 which binds 5S RNA is necessary for rRNA maturation and structure of the 60S ribosomal subunits.

Thiamin pyrophosphokinase 1 (TPK1) is a homodimer which catalyzes the phosphorylation of thiamine to thiamine pyrophosphate. TPK1 is found in the heart, kidney, testis, small intestine and peripheral blood leukocytes, and at very low levels in a variety of tissues. TPK1 gene defects cause the thiamine metabolism dysfunction syndrome type 5, episodic encephalopathy type (THMD5), which is an autosomal recessive metabolic disorder due to an inborn error of thiamine metabolism.

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.

rRNA-processing protein UTP23 homolog (UTP23) is a small subunit (SSU) processome component. The SSU processome is a complex involved in ribosome biogenesis and essential for pre-18S rRNA maturation. UTP23 is vital for the first 3 cleavage steps in 18S rRNA maturation. Furthermore, single-point mutations in the conserved putative active site of Utp24 but not Utp23 annul its function in ribosome biogenesis.

Dickkopf-related protein 1 (DKK1) antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by creating a ternary complex with the transmembrane protein KREMEN which promotes internalization of LRP5/6. DKKs have a significant role in vertebrate development, where they locally inhibit Wnt controlled processes for instance antero-posterior axial patterning, limb development, somitogenesis and eye formation. Furthermore, Dkks are involved in bone formation and bone disease, cancer and Alzheimer disease in Adults.

Alpha-synuclein or SNCA is a synuclein protein. SNCA mainly found in the brain, small concentration of the protein can also be located in other tissues such as heart and muscle. When looking in the brain tissue, SNCA is located in the end of the neuron, in an area called presynaptic terminal. In the presynaptic terminal SNCA has interaction with phospholipids & other proteins. Neurotransmitters are released from the synaptic vesicles in the Presynaptic terminals and act as messengers. Once released, the neurotransmitters send signals across the neurons that are crucial for the brain’s operation.

C1QBP having the accession number of NP_001203 binds to the globular "heads" of c1q thus inhibiting c1 activation. C1QBP interacts with a wide range of ligands and is implicated in cell signaling. C1QBP associates with C1r and C1s in order to yield the first component of the serum complement system. C1QBP protein has been identified as the p32 subunit of pre-mRNA splicing factor SF2, as well as a hyaluronic acid-binding protein.
C1QBP is a new marker of tumor cells and tumor-associated macrophages/myeloid cells in hypoxic/metabolically deprived areas of tumors.
Mitochondrial C1QBP is a critical mediator of p14ARF-induced apoptosis.
C1QBP functions as a chemotactic factor for immature dendritic cells, and migration is mediated through ligation of both C1QBP and cC1qR/CR.
C1QBP overexpression successfully blocks mRNA accumulation from the adenovirus major late transcription unit (MLTU) and stimulates RNA polymerase II carboxy-terminal domain phosphorylation in virus-infected cells.
C1QBP binds with Hepacivirus core protein on CD8+ and CD4+ positive t-cells and inactivates lck and akt.

Ribosomal Protein L26 (RPL26) is a ribosomal protein which is a component of the 60S subunit (the large subunit of the ribosome). RPL26 is a part of the L24P family of ribosomal proteins which is located in the cytoplasm. There are numerous processed pseudogenes of RPL26 dispersed through the genome as usual for genes encoding ribosomal proteins.

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.

DR1 is a phosphoprotein that inhibits both basal and activated levels of transcription. DR1 is phosphorylated in vivo which affects its interaction with TBP. DR1 has a histone fold motif at the amino terminus, a TBP-binding domain, and a glutamine- and alanine-rich region. By selectively repressing polymerases II and III, DR1 alters the physiological balance of transcriptional output in favor of polymerase I.

FABP1 (Fatty acid binding protein1) encodes the fatty acid binding protein found in liver. FABP1 is composed of ten antiparallel beta strands that form a barrel with a bigger binding pocket than the other FABPs allowing it to accommodate two fatty acid. This protein binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm; it may be involved in intracellular lipid transport and metabolism.

PABPN1 is an highly expressed nuclear protein which has high affinity to nascent poly(A) tails. PABPN1 is essential for progressive and efficient polymerization of poly(A) tails at the 3' ends of eukaryotic transcripts and regulates the length of the poly(A) tail to about 250 nt. In its steady-state, PABPN1 is restricted to the nucleus however there are different poly(A) binding proteins which can be found in the cytoplasm. PABPN1 has a GCG trinucleotide repeat at the 5' end of the coding region. Expansion of this repeat from the normal 6 copies to 8-13 copies results in autosomal dominant oculopharyngeal muscular dystrophy (OPMD) disease. Associated pseudogenes were located on chromosomes 19 and X. Additionally, there is a read-through transcription between PABPN1 gene and the adjacent upstream BCL2L2 (BCL2-like 2) gene.

Ribosomal Protein S20 (RPS20) encodes a ribosomal protein which is a component of the 40S subunit. RPS20, which is located in the cytoplasm, is a part of the S10P family of ribosomal proteins. RPS20 is co-transcribed with the small nucleolar RNA gene U54, which is located in its second intron. There are multiple processed pseudogenes of RPS20 dispersed through the genome as typical for genes encoding ribosomal proteins.

LRP2 Binding Protein (LRP2BP) is a protein coding gene which plays a role as an adapter that controls LRP2 function. LRP2BP is noticed in a vesicular staining pattern close to the plasma membrane and through the cytoplasm.

TBCB is a member of the Microtubules family. Biosynthesis of functional microtubules include the involvement of a number of chaperones, termed Tubulin folding cofactors A (TBCA), B (TBCB), C (TBCC), D (TBCD) and E (TBCE), which operate on folding intermediates downstream of the cytosolic chaperon, known as TCP. The 244 amino acid cytoplasmic protein TBCB has one CAP-Gly domain and is universally expressed. TBCB takes part in the regulation of tubulin heterodimer dissociation and operates as a negative regulator of axonal growth.

Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity.
Human Transferrin is a crucial component for the cultivation of mammalian cells in-vitro. Human Transferrin is Critical for long-term cells growth in-vitro. Human Transferrin is used as detoxificant in media by binding contaminating metal ions. Human Transferrin is often used as a nutrient in fermentation media for recombinant protein and biopharmaceutical production. Additional common uses of Human Transferrin areMolecular weight, Affinity purification of anti-human transferrin antibodies and also as receptor mediated transfection of molecules such as DNA, into cells.

Protein A is a cell wall component produced by several strains of Staphylococcus aureus. The recombinant Protein A is genetically engineered protein and holds 5 IgG-binding regions of protein A. Recombinant Protein A functions basically the same as native Protein A and is perfect for purification of polyclonal or monoclonal IgG antibodies. Protein A binds to human IgG1, IgG2 and IgG4, mouse IgG2a, IgG2b and IgG3 and rat IgG2c. Protein A also binds to total IgG from rabbit, pig, dog, cat, and guinea pig.

Lactoferrin is a glycoprotein that belongs to the transferrin family of iron binding proteins. It is found in human breast milk as well as most epithelial surface secretions including tears, nasogastric, saliva, and bronchial. Lactoferrin binds 2 molecules of iron with very high affinity. Lactoferrin inhibits bacterial growth by withholding iron, its N-terminal region is an antimicrobial peptide. Lactotransferrin acts synergistically with lysozyme to potentiate the activity of both proteins. The multifunctional protein lactoferrin has many physiological possible roles. It is often referred to as an innate defense protein and frequently serves as the first line of defense in protection against pathogens. It has been shown to have the ability to bind iron, it is a natural anti-bacterial, anti-fungal and anti-viral, it is an antioxidant and it also has immunomodulatory properties. It has many beneficial properties, which make it a good candidate for a number of product applications. Considerable research is currently going on to explain the various suggested biological functions of lactoferrin.