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DBI, also known as Acyl-CoA-binding protein isoform 2, is a diazepam binding inhibitor, which is regulated by hormones. DBI participates in lipid metabolism and in the displacement of beta-carbolines & benzodiazepines, which modulate signal transduction at type A gamma-aminobutyric acid receptors located in brain synapses. Moreover, during adipocyte differentiation the expression of DBI is significantly induced. DBI preforms as an acyl-CoA pool former and regulates LCFA (long-chain fatty acids) metabolism in peripheral tissues.

ILK1 (Integrin-linked kinase) is a serine/threonine protein kinase, containing 4 ankyrin-like repeats. ILK1 regulates a number of biological properties which include: anchorage-independent cell cycle progression, tumor cell invasion and apoptosis. ILK1 can also be implicated in mediating cell architecture, adhesion to integrin substrates and anchorage-dependent growth in epithelial cells. Furthermore, ILK1 phosphorylates beta-1 and beta-3 integrin subunit on serine and threonine residues, but also AKT1 and GSK3B.
ILK1 interacts with the cytoplasmic domains of integrin ?1 and ?3 subunits in addition to several adaptors and signaling proteins, it also acts as a proximal receptor kinase regulating integrin-mediated signal transduction. ILK1 is a focal adhesion protein part of the complex ILK-PINCH. This complex is deemed to be one of the convergence points of integrin- and growth factor-signaling pathway. ILK1 is stimulated rapidly but briefly by both cell fibronectin interactions in a PI3-K-dependent manner, probably through the binding of PtdIns(3,4,5)P3 with a PH-like domain of ILK.
ILK1 over-expression has been documented in a wide variety of human malignancies.

CALR is a multifunctional protein that acts as a main Ca(2+)-binding (storage) protein in the lumen of the endoplasmic reticulum. Calreticulin is localized in the nucleus, and participates in transcription regulation. Calreticulin binds to the synthetic peptide KLGFFKR, which is nearly identical to an amino acid sequence in the DNA-binding domain of the superfamily of nuclear receptors. CALR binds to antibodies in specific sera of systemic lupus and Sjogren patients which have anti-Ro/SSA antibodies, it is well conserved among species, and it is positioned in the endoplasmic and sarcoplasmic reticulum where it binds calcium. The amino terminus of CALR interacts with the DNA-binding domain of the glucocorticoid receptor and prevents the receptor from binding to its specific glucocorticoid response element. CALR reduces the binding of androgen receptor to its hormone-responsive DNA element and inhibits androgen receptor and retinoic acid receptor transcriptional activities in vivo, as well as retinoic acid-induced neuronal differentiation. Therefore, CALR acts as a significant modulator of the regulation of gene transcription by nuclear hormone receptors.

Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. This I-domain containing alpha integrin combines with the beta 2 chain (ITGB2) to form a leukocyte-specific integrin referred to as macrophage receptor 1 ('Mac-1'), or inactivated-C3b (iC3b) receptor 3 ('CR3'). The alpha M beta 2 integrin is important in the adherence of neutrophils and monocytes to stimulated endothelium, and also in the phagocytosis of complement coated particles. Integrin alpha-m/beta-2 is implicated in various adhesive interactions of monocytes, macrophages and granulocytes as well as in mediating the uptake of complement-coated particles. CD-11b is identical with cr-3, the receptor for the ic3b fragment of the third complement component. CD-11b probably recognizes the r-g-d peptide in c3b. Integrin alpha-m/beta-2 is also a receptor for fibrinogen, factor x and icam1. it recognizes p1 and p2 peptides of fibrinogen gamma chain.

TREM2 is a membrane protein that forms a receptor signaling complex with TYROBP. TREM2 may be involved in chronic inflammation by triggering the production of constitutive inflammatory cytokines. Defects in the TREM2 gene are a source of polycystic lipomembranous osteodysplasia with sclerosing leukoencephalopathy (PLOSL).

CETN1 is an EF-hand type Ca2+-binding protein. CETN1 is localized to the centrosome of interphase cells, and reorganizes the region of the spindle poles during mitosis, reflecting the dynamic behavior of the centrosome during the cell cycle. CETN1 has a vital part in the determination of centrosome position and isolation, and in the course of microtubule separating.

FCGR3B, also known as CD16b belongs to the Ig super family. FCGR3B encodes a glycosylphosphatidylinositol (GPI)-anchored protein which is expressed constitutively by neutrophils. FCGR3B binds to complex or aggregated IgG and monomeric IgG. Different from III-A, FCGR3B cannot arbitrate antibody-dependent cytotoxicity and phagocytosis. FCGR3B operate to capture immune complexes in peripheral blood circulation that does not activate neutrophils.

COL4A3BP is a kinase that particularly phosphorylates the N-terminal region of the non-collagenous domain of the alpha 3 chain of type IV collagen, recognized as the Goodpasture antigen that is the outcome of an autoimmune reaction directed at COL4A3BP. One isoform of COL4A3BP participates in ceramide intracellular transport.

Alpha & Gamma-Adaptin Binding Protein (AAGAB), which is also known as P34, takes part in membrane traffic and interacts with AP1G1 and AP2A1.AAGAB is highly expressed in skin and keratinocytes, with the highest levels in adrenal gland, rectum and thymus.

VCAM1 is a member of the Ig superfamily. It is a cell surface sialoglycoprotein expressed by cytokine activated endothelium. VCAM-1 contains 6 or 7 immunoglobulin domains, and is expressed on both large and small vessels only after the endothelial cells are stimulated by cytokines. The protein has a number of functions including the regulation of leukocyte migration, leukocyte endothelial cell adhesion and signal transduction and may play a role in a number of inflammatory diseases (artherosclerosis and rheumatoid arthritis).

SDCBP2 has two class II PDZ domains. PDZ domains assist protein-protein interactions by attaching to the cytoplasmic C-terminus of transmembrane proteins, and PDZ-containing proteins mediate cell signaling and the organization of protein complexes. SDCBP2 attaches to phosphatidylinositol 4, 5-bisphosphate (PIP2) and take part in nuclear PIP2 arrangement and cell division.

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.

CD86 type I membrane protein is a member of the immunoglobulin superfamily which is expressed by antigen-presenting cells, and acts as the ligand for two proteins at the cell surface of T cells, CD28 antigen and cytotoxic T-lymphocyte-associated protein 4. CD86 binding with CD28 protein is a co-stimulatory signal for initiation of the T-cell. CD86 binding with CTLA-4 negatively regulates T-cell activation and diminishes the immune response.

CD47, functions in cell adhesions by performing as an adhesion receptor for THBS1 on platelets, furthermore CD47 plays a role in the modulation of integrins. In addition, CD47 takes a vital part in memory formation as well as synaptic plasticity in the hippocampus. Receptor for SIRPA avoids maturation of immature dendritic cells and inhibits cytokine production by mature dendritic cells. CD47 prevents premature elimination of red blood cells, and it is also implicated in membrane permeability changes induced following virus infection.

Calreticulin 3 (CALR3) belongs to the calreticulin (CRT) family which consists of calcium binding chaperones that are localized to the endoplasmic reticulum or sarcoplasmic reticulum in eukaryotes. CALR3, which is expressed mainly in testis, takes part in protein-folding, oligomeric assembly and quality control in the ER. CALR3 plays an important role as a cancer-testis antigen due to its frequent expression in many cancers.

The La protein is a 47 kDa polypeptide that frequently acts as an autoantigen in systemic lupus erythematosus and Sjogren's syndrome patients. La is involved in various aspects of RNA metabolism, including binding and protecting 3-prime UUU(OH) elements of newly RNA polymerase III - transcribed RNA, processing 5-prime and 3-prime ends of pre-tRNA precursors, acting as an RNA chaperone, and binding viral RNAs linked to hepatitis C virus. It occurs in both the nucleus and the cytoplasm, where it assumes different roles. In the nucleus, La protein facilitates the production of tRNAs, acting as an RNA polymerase III (RNAP III) transcription factor by attaching to the U-rich 3'UTR of nascent transcripts, aiding in their folding and maturation. In the cytoplasm, La protein facilitates the translation of specific mRNAs, acting as a translation factor. As an RNA binding protein (RBP), La protein associates with subsets of mRNAs which contain a 5'-terminal oligopyrimidine (5'TOP) motif known to direct protein synthesis. The binding of La protein to particular classes of RNA molecules regulates their downstream processing, guards them from endonuclease digestion, and organizes their export from the nucleus. La/SS-B appears to be readily disposed to proteolysis, which results in many smaller (42kD, 320, and 270) nevertheless still immunoreactive polypeptides. La/SS-B antigen is strongly conserved across species. Anti-La/SS-B autoantibodies were originally found as precipitating autoantibodies in sera of Sjogren's Syndrome patients and referred to as SjT. Anti-La/SS-B precipitins are most frequently found in Sjogren's Syndrome, Systemic Lupus Erythematosus (SLE) and Subacute Cutaneous Lupus. Also, there seems to be a correlation between anti-La/SS-B and the absence of nephritis in SLE patients.

Syntaxin-binding protein 6 (STXBP6) binds components of the SNARE complex and takes part in regulating SNARE complex configuration. STXBP6 forms non-fusogenic complexes with SNAP25 and STX1A and modulates the formation of SNARE complexes and exocytosis.

Fibrinogen silencer-binding protein (FSBP), interacts with X11alpha. The X11alpha/FSBP complex send signals to the nucleus in order to repress glycogen synthase kinase-3beta promoter activity. X11alpha is a neuronal adaptor protein that interacts with the amyloid precursor protein (APP) via a centrally located phosphotyrosine binding domain to inhibit the production of Abeta peptide that is deposited in Alzheimer's diseased brains.

Serine peptidase inhibitor Kazal type 7 (SPINK7) which includes one Kazal-like domain is most likely serine protease inhibitor. Diseases linked with SPINK7 include esophageal cancer, and oral squamous cell carcinoma

SAR1B is a small GTPase that functions as a homodimer. GTP-Binding Protein SAR1B (SAR1b) is involved in transport from the endoplasmic reticulum to the Golgi apparatus and also in the selection of the protein cargo and the assembly of the COPII coat complex. The SAR1B protein is activated by the guanine nucleotide exchange factor PREB. SAR1B gene defects are a cause of chylomicron retention disease (CMRD), also known as Anderson disease (ANDD).

Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. This I-domain containing alpha integrin combines with the beta 2 chain (ITGB2) to form a leukocyte-specific integrin referred to as macrophage receptor 1 ('Mac-1'), or inactivated-C3b (iC3b) receptor 3 ('CR3'). The alpha M beta 2 integrin is important in the adherence of neutrophils and monocytes to stimulated endothelium, and also in the phagocytosis of complement coated particles. Integrin alpha-m/beta-2 is implicated in various adhesive interactions of monocytes, macrophages and granulocytes as well as in mediating the uptake of complement-coated particles. CD-11b is identical with cr-3, the receptor for the ic3b fragment of the third complement component. CD-11b probably recognizes the r-g-d peptide in c3b. Integrin alpha-m/beta-2 is also a receptor for fibrinogen, factor x and icam1. it recognizes p1 and p2 peptides of fibrinogen gamma chain.

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.

RANKL binds to tnfrsf11b/opg and to tnfrsf11a/rank. Osteoclast differentiation and activation factor. Augments the ability of dendritic cells to stimulate naive t-cell proliferation. May be an important regulator of interactions between t-cells and dendritic cells and may play a role in the regulation of the t-cell-dependent immune response. sRANKL may also play an important role in enhanced bone-resorption in humoral hypercalcemia of malignancy.