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YWHAB belongs to the 14-3-3 family of proteins which are in charge for signal transduction by binding to phosphoserine-containing proteins. YWHAB is found in both plants and mammals. YWHAB protein interacts with RAF1 and CDC25 phosphatases,thus linking mitogenic signaling and the cell cycle machinery. YWHAB is an adapter protein involved in the regulation of a large spectrum of both general and specialized signaling pathway. YWHAB binds to a large number of proteins by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner.

Alpha crystallins are composed of two gene products ; alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20). They act as molecular chaperones and hold them in in large soluble aggregates. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional function of a-crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-B is expressed widely in many tissues and organs and occurs in many neurological diseases.

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.

The Melanoma Inhibitory protein (MIA) was identified as an inhibitor of in vitro growth of malignant melanoma cells. The protein contains a SH3 domain.
MIA acts as a potent tumor cell growth inhibitor for malignant melanoma cells and some other neuroectodermal tumors, including gliomas, in an autocrine fashion. In a study of human melanoma cell lines with different metastatic capacity MIA mRNA expression appeared to be inversely correlated with pigmentation. MIA has been shown to represent a very sensitive and specific serum marker for systemic malignant melanoma that might be useful for staging of primary melanomas, detection of progression from localized to metastatic disease during follow-up, and monitoring therapy of advanced melanomas.

Maltose Binding Protein (MBP) is a part of the maltose/maltodextrin system of Eschericia coli bacteria, which is responsible for the uptake and efficient catabolism of maltodextrins. It is a complex regulatory and transport system involving many proteins and protein complexes.
Maltose binding protein MalE,MBP, is part of the maltodextrin transport system in E. coli. The maltodextrins diffuse through the LamB pore located in the outer membrane into the periplasm. The sugar is bound to MalE which prevents it to diffuse back outside. MalE passes the sugar to a complex of MalF and MalG in the cytoplasmic membrane where active tranport is mediated by the ATPase MalK. MBP molecular weight is 40,622 dalton. There are two domains in the protein with similar secondary structure (central pleated sheets are surrounded by helices) . The domains are connected by three bridges, between the domains is a deep groove in which the sugar is bound. All hydroxyl groups of the sugar are fixed by sidechains of the protein by hydrogen bonds. Some water molecules are part of the hydrogen bridge network.

DERF1 is a thiol protease that hydrolyzes proteins, with a preference for Phe or basic residues. DERF1 is a C1 peptidase family member. DERF1 has extensive endopeptidase specificity. DERF1 causes an allergic reaction in humans. Common symptoms of mite allergy are bronchial asthma, allergic rhinitis and conjunctivitis.

Overexpression of the HIF1AN is linked with tumor aggressiveness in pancreatic endocrine tumors. HIF1AN hydroxylates Notch ICD at two residues that are crucial for the function of Notch ICD as a transactivator within cells and during neurogenesis and myogenesis. HIF1AN is commonly expressed in invasive breast carcinoma. The hypoxic response and survival recommends that tumour regulation of HIF1AN is an additional important mechanism for HIF pathway activation. HIF1AN is an asparaginyl hydroxylase enzyme that controls the transcriptional activity of hypoxia-inducible factor. FIH1 is a part of the Fe2+ and 2-oxoglutarate-dependent dioxygenase superfamily, FIH1 is protein that hydoxylates a specific asparagine residue (Asn-803) within the HIF1A C-terminal transactivation domain. In normoxia, the HIF1AN-mediated hydroxylation of the HIF1? transactivation domain which results in blockage of the HIF1A-p300/CBP interaction and represses transcriptional activity of HIF1A targeted genes.

Nucleolar protein 3 (NOL3) is primarily expressed in the muscle and is appears in the nucleoplasm and concentrated in nucleoli. NOL3 is an anti-apoptotic protein which down-regulates the enzymatic activities of caspase 2, caspase 8 and tumor protein p53. NOL3 is highly expressed in the heart and skeletal muscle. NOL3 is identified at low levels in the placenta, liver, kidney and pancreas. The NOL3 mRNA and protein levels are stimulated by neuronal activity, which is vital in order to promote neuroplasticity, thus indicating a potential role for NOL3 in activity-dependent changes in dendrite function. NOL3 localizes to the cytoskeleton of neuronal cells and seems to colocalize with F-Actin, though it may connect with an actin-associated protein instead of directly with F-Actin.

The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.

Glycinin Ara h 3 is a seed storage protein, 11 S globulin and trypsin inhibitor from peanut. Each subunit of the hexamer is composed of an acidic and a basic chain derived from a single precursor and linked by a disulfide bond. Ara h 3 and Ara h 4 are isoforms. Glycinin is the source of sulfur-containing amino acids in seed meals and it exists in the seeds of many leguminous and non-leguminous plants.

Myelin Protein Zero-Like 1 (MPZL1) is a cell surface receptor, which is involved in signal transduction processes. MPZL1 recruits PTPN11/SHP-2 to the cell membrane and is a putative substrate of PTPN11/SHP-2. MPZL1 is a main receptor for concanavalin-A (ConA) and it is involved in cellular signaling induced by ConA, which most likely includes Src family tyrosine-protein kinases. MPZL1 Isoform 3 appears to have a dominant negative role by blocking tyrosine phosphorylation of MPZL1 induced by ConA. Isoform 1, but not isoform 2 and isoform 3, might be involved in regulation of integrin-mediated cell motility.

gAcrp30 globular protein, exists as a result of proteolytic processing of adiponectin. Adiponectin is manufactured and secreted solely by adipocytes, and is a highly obtained plasma protein, accounting for up to 0.05% of total serum protein. Similar to Adiponectin, gAcrp30 is able of lowering hyperglycemia and reversing INS resistance. In addition, gAcrp30 is an significant protein that is involved in promoting fat loss by signaling muscle to absorb and burn Free-Fatty Acids. AdipoR1 & AdipoR2 are the 2 signaling receptors for adiponectin and gAcrp30 that were recently been identified.

MAP3K12 Binding Inhibitory Protein 1 (MBIP) is a part of the ATAC complex which consists of histones H3 and H4 with a histone acetyltransferase activity. MBIP inhibits the MAP3K12 activity in order to induce the activation of the JNK/SAPK pathway.

Matrix Metalloproteinase-13 (MMP-13) is an enzyme that is a member of the MMP extracellular protease family. Extracellular protease enzymes, by virtue of their broad substrate specificities1, play a role in both normal and disease states of tissue proliferation. Among the targets of MMP-13 are collagen, gelatin, entactin, pro-TNF-a, and chemokine SDF-11-4.
MMP-13 is found in its latent form as a 52-56 kDa glycosylated proenzyme. Upon cleavage the 22-46 kDa5 MMP-1 becomes active in extracellular matrix remodeling.
Because of the prominent role that MMP-1 plays in cell migration and metastasis, it is an important target for inhibition screening.

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.

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.

Mmitochondrial import receptor subunit TOMM20 homolog (TOMM20) is a member of the Tom20 family. The Tom machinery consists of import receptors for the initial binding of cytosolically synthesized preproteins and a general import pore (GIP) for the membrane translocation of various preproteins into the mitochondria. TOMM20 acts as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates the movement of preproteins into the TOM40 translocation pore.

Mouse MIP-1 gamma is 75% identical in its amino acid compostion as compared to the rat specie. MIP-1 gamma is a CC chemokine localized in murine blood and a widespread range of murine tissues, without having an identified human homolog. MIP-1 gamma signals through the CCR1 receptor. MIP-1 gamma chemoattracts neutrophils and also inhibits colony formation of bone marrow myeloid immature progenitors. MIP-1 gamma has six cysteines including the four highly conserved cysteine residues present in CC chemokines.

HMGB2 belongs to the non-histone chromosomal high-mobility group protein family which are chromatin-associated and highly spread in the nucleus of higher eukaryotic cells. HMGB2 can successfully bend DNA and form DNA circles which indicates that HMGB2 facilitates cooperative interactions between cis-acting proteins by promoting DNA flexibility. Additionally, HMGB2 takes part in the final ligation step in DNA end-joining processes of DNA double-strand breaks repair and V(D)J recombination.

Homeodomain-only protein (HOPX) functions via its interaction with SRF, thus modulating the expression of SRF-dependent cardiac-specific genes and cardiac development. HOPX inhibits SRF-dependent transcription either by hindering SRF binding to DNA or by engaging histone deacetylase (HDAC) proteins which prevent transcription by SRF. HOPX is a homeodomain protein which lacks certain conserved residues required for DNA binding. HOPX overexpression causes cardiac hypertrophy.

PTX-2 or Pentraxin-2 is a phylogenetically conserved protein, commonly moving with homopentameric blood protein or with a protein that recognizes receptors of the innate immune system. The protein’s specific binding abilities may show that PTX-2 is specially bound in sites where injury accrued, therefore helps to eliminate damaged tissue by ways that are not phlogistics.

MUP1 is a subfamily of proteins appears highly in the urine and other secretions of various animals. MUP1 provides a minor range of identifying information regarding the donor animal, once detected by the vomeronasal organ of the receiving animal. MUP1 can as well act as protein pheromones themselves. MUP1has been shown to encourage aggression in male mice, and 1 specific Mup protein found in male mouse urine is sexually attractive to female mice.

MAP1LC3B is a member of the MAP1 LC3 family. MAP1LC3B is a subunit of neuronal microtubule-associated MAP1A and MAP1B proteins, that are involved in microtubule assembly and important for neurogenesis. In addition, MAP1LC3B takes part in formation of autophagosomal vacuoles and is expressed mainly in heart, testis, brain and skeletal muscle.