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Streptavidin is a tetrameric protein secreted by Streptomyces avidinii which binds firmly to biotin. Streptavidin is widely used in molecular biology through its unique high affinity for the vitamin biotin. The dissociation constant (Kd) of the biotin-streptavidin complex is about ~10-15 mol/L. The strong affinity recognition of biotin and biotinylated molecules has made streptavidin one of the most important components in diagnostics and laboratory kits. The streptavidin/biotin system has one of the biggest free energies of association of yet observed for noncovalent binding of a protein and small ligand in aqueous solution (K_assoc = 10**14). The complexes are also extremely stable over a wide range of temperature and pH.

TAGLN3 holds a putative Actin-binding domain, two potential phosphorylation sites, two EF-hand motifs and a calponin-homology (CH) domain. TAGLN3 is homologic to transgelin and calponin, two cytoskeleton-interacting proteins. TAGLN3 is a member of the calponin family, and is co-localized with Actin and tubulin, which indicates that TAGLN3 has a part in neuronal plasticity or as a signaling protein. As a result of a wide-ranging expression pattern, TAGLN3 is able to take different roles in the developing and adult brain.

IL2-Ra is one of the three constituent subunits of the IL2 receptor.
IL-2Ra is released into the serum after increased cellular expression such as increased activation of B and T cells. Clinical manifestations of IL2-Ra elevation include autoimmune conditions and some leukemias and lymphomas.

Lipopolysaccharide-induced TNF-alpha factor (LITAF) is a small integral membrane protein of lysosome/late endosome. The expression of inflammatory cytokines such as TNF-alpha in Lipopolysaccharide-induced processes is mediated by LITAF. LITAF connects to STAT6B, which belongs to the STAT6 family forming a complex on the TNF-alpha promoter that modifies TNF activity. High levels of expression of LITAF mRNA are observed mostly in the placenta, peripheral blood leukocytes, lymph nodes and spleen.

The bone morphogenetic protein (BMP) receptors are a family of transmembrane serine/threonine kinases that include the type I receptors BMPR1A and BMPR1B and the type II receptor BMPR2. These receptors are also closely related to the receptors, ACVR1 and ACVR2. The ligands of these receptors are members of the TGF-beta superfamily. TGF-betas transduce their signals through the formation of heteromeric complexes with 2 different types of serine (threonine) kinase receptors: type I receptors of about 50-55 kD and type II receptors of about 70-80 kD. Type II receptors bind ligands in the absence of type I receptors, but they require their respective type I receptors for signaling, whereas type I receptors require their respective type II receptors for ligand binding.

SNRPB is one of several nuclear proteins which are found in common among U1, U2, U4/U6, and U5 small ribonucleoprotein particles (snRNPs). These snRNPs are involved in pre-mRNA splicing, and the SNRPB protein may also have a role in pre-mRNA splicing or snRNP structure. SNRPB binds to the downstream cleavage product (DCP) of histone pre-mRNA in a U7 snRNP dependent manner. SNRPB functions in the U7 snRNP complex which is involved in histone 3'-end processing.

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

Dystroglycan 1 (DAG1) is a laminin binding component of the dystrophin-glycoprotein complex which provides a connection between the subsarcolemmal cytoskeleton and the extracellular matrix. The N-terminal domain of alpha-dystroglycan is secreted into the cerebrospinal fluid. The effect of DAG1 on the nervous system remains vague. The complete dystroglycan complex is expressed in a various tissues and has a role in processes such as laminin and basement membrane assembly, sarcolemmal stability, cell survival, peripheral nerve myelination, nodal structure, cell migration, and epithelial polarization. DAG1 is a candidate gene for the site of the mutation in autosomal recessive muscular dystrophies. The dramatic decrease of DAG1 in Duchenne muscular dystrophy leads to a loss of linkage between the sarcolemma and extracellular matrix, making muscle fibers more susceptible to necrosis.

PI3 is an elastase-specific protease inhibitor, which contains a WAP-type four-disulfide core (WFDC) domain, and is thus a member of the WFDC domain family. Most WFDC gene members are localized to chromosome 20q12-q13 in two clusters: centromeric and telomeric. PI3 belongs to the centromeric cluster.

Hemagglutinin-Influenza A Virus H7N9 Anhui 2013 (Anhui H7N9) is a part of the influenza viruses hemagglutinin family. H7N9 Anhui is anantigenic glycoprotein which is responsible for binding the virus to the infected cell. An H7N9 virus was firstreported to have infected humans in March 2013, in China. Although the risk is low, The H7N9 virus has thegreatest potential compared with other influenza A viruses to cause a pandemicbecause like other type A viruses, it is not easily transmitted between people in its current form.

CALN1 is highly similar to the calcium-binding proteins of the calmodulin family. The CALN1 protein contains two EF-hand domains and potential calcium-binding sites. Also, CALN1 negatively regulates Golgi-to-plasma membrane trafficking by interacting with PI4KB and inhibiting its activity. CALN1 has a role in the physiology of neurons and is potentially significant in memory and learning.

C1s enzyme (a subunit of the C1 complex) is the activated form of C1s proenzyme which is the first complement component in the classical pathway of complement. C1s proenzyme is an inactive zymogen until C1 is activated. C1 is a non-covalent calcium-dependent complex containing1 C1q, 2 C1r and 2 C1s molecules.The binding of multiple arms to immune complexes causesthe production of 2 proteases that cleave and activate the 2 C1s protease zymogens in the complex by the C1r proteins. This activation of C1s proenzyme results in its cleavage into 2 C1s chains of 58,000 and 28,000 Dalton.

P-Selectin also called Platelet Alpha-Granule Membrane Protein, CD62, and Granulocyte Membrane Protein GRMP belongs to a family of divalent cation-dependent carbohydrate-binding glycoproteins or adhesion molecules. Pselectin is expressed transiently on the surface of activated platelets and endothelial cells. P-Selectin is a 140 kDa protein which is stored in the alpha-granules of platelets and Weibel-Palade bodies of endothelial cells. Secreted P-selectin is thought to play a key role in the adhesion of platelets to monocytes and neutrophils during an inflammatory response. P-Selectin is a calcium-dependent receptor that binds to sialylated forms of Lewis blood group carbohydrate antigens on neutrophils and monocytes. Levels of P-Selectin may be elevated in a number of pathological conditions.

STIP1 is an adaptor protein that mediates the functions of HSP70 & HSP90 in protein folding. STIP1 supports the transfer of proteins from HSP70 to HSP90 by binding together HSP90 and substrate-bound HSP70. STIP1 stimulates the ATPase activity of HSP70 and inhibits the ATPase activity of HSP90, suggesting that it regulates both the conformations and ATPase cycles of these chaperones. STIP1 genetic variations are involved in regulating corticosteroid response in asthmatic subjects with reduced lung function.

Batroxobin is a serin protease that reduces fibronogen levels and is originally extracted from snake venom of Bothrops Atrox. Batroxobin is used in defibrinogenation and thrombolysis and also has an effect on c-fos gene and growth factor.
Batroxobin can efficiently restrain proliferation of VSMCs, by blocking the release and uptake of Ca2+, thus influencing [Ca2+]i.
Batroxobin converts fibrinogen to fibrin through the restricted release of fibrinopeptide-A from fibrinogen to promote blood to clot. Unlike thrombin, it is not affected by heparin and hirudin.

KPNB1 is a member of the importin beta family. The KPNB1 protein is engaged in nuclear protein import, either by coupling itself with an adapter protein (e.g., importin-alpha subunit which binds to nuclear localization signals (NLS) in cargo substrates), or by functioning autonomously as a nuclear transport receptor (acts as NLS receptor, docking of the importin/substrate complex to the nuclear pore complex).

Calcyphosine (CAPS) is a calcium-binding protein containing four EF-hand domains. CAPS protein was originally identified as thyroid protein p24 which is found in a number of epithelium and in some cells of the central nervous system. CAPS may have a role in the regulation of ion transport. In the thyroid follicular cells, CAPS is synthesized and phosphorylated in response to stimulation by thyrotropin and cAMP agonists.

Ras-related protein Rap-2b (RAP2B) is a part of RAS-related genes family. RAP2B has a threonine residue at aa 61Unlike normal ras proteins which have a nontransforming glutamine residue at that position. The threonine residue makes the intrinsic GTPase activity for Rap2B lower, by this means allows RAP2B to exist in the activated state for a longer period of time than normal ras proteins. RAP2B is a platelet protein which is activated by thrombin and involved in platelet activation. RAP2B may be a candidate oncogene which takes part in carcinogenesis through activation of NF-kappaB pathway.

CETN3 comprises of 4 EF-hand calcium binding domains, and is a part of the centrin protein family. CETN3 protein is widely expressed cytoskeletal components that demonstrate increased expression during cell differentiation. CETN3 takes part in centrosome reproduction.

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.

Sarcoglycan Beta, also known as SGCB, is a part of the sarcoglycan family. SGCB belongs to the sarcoglycan complex which is a subcomplex of the dystrophin-glycoprotein complex that connects between the F-actin cytoskeleton and the extracellular matrix.

BRISC And BRCA1 A Complex Member 1, also known as BABAM1, is a part of the BRCA1-A complex. The BRCA1-A complex identifies 'Lys-63'- linked ubiquitinated histones H2A and H2AX at DNA lesions sites and also holds deubiquitinase activity which removes in particular 'Lys-63'-linked ubiquitin on histones H2A and H2AX. BABAM1 is necessary to preserve the stability of BRE/BRCC45 and help the 'Lys-63'-linked deubiquitinase activity mediated by BRCC3/BRCC36 component.

Myosin regulatory light chains, including MRCL3, MYLPF and MYL9, regulate contraction in smooth muscle and non-muscle cells via phosphorylation by MLCK (myosin light chain kinase). Phosphorylation of myosin regulatory light chains, catalyzed by MLCK in the presence of calcium and calmodulin, increases the actin-activated myosin ATPase activity, thus regulating the contractile activity. MYLPF is vital for fast and slow skeletal muscle development.

Sprouty-Related EVH1 Domain Containing 1, also known as SPRED1, is a part of the Sprouty family of proteins and is phosphorylated by tyrosine kinase. SPRED1 inhibits growth-factor-mediated activation of MAP kinase. SPRED1 plays a role as a homodimer or as a heterodimer with SPRED2 to regulate activation of the MAP kinase cascade. SPRED1 is a negative regulator of hematopoiesis of bone marrow.