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GABARAP is a ligand-gated chloride channel that mediates inhibitory neurotransmission. GABARAP is highly positively charged in its N-terminus and shares sequence similarity with light chain-3 of microtubule-associated proteins 1A and 1B. GABARAP clusters neurotransmitter receptors by mediating interaction with the cytoskeleton.

GABARAPL1 [Gamma-aminobutyric acid (GABA) receptor-associated protein-like 1] is a member of the MAP1 LC3 family. GABARAPL1 increases cell surface expression of kappa type opioid receptor through facilitating anterograde intracellular trafficking of the receptor.

GABARAPL2 takes part in intra Golgi traffic and modulates intra Golgi transport by coupling between NSF activity and SNAREs activation. GABARAPL2 first stimulates the ATPase activity of NSF which in turn stimulates the association with GOSR1.

RGS19 is a member of RGS (regulator of G protein signaling) family and negatively regulates G protein coupled receptor signaling. RGS19 protein specifically cooperates with heterotrimeric GTP-binding protein G alpha i3 (GAI3).

The recombinant Protein A/G is a genetically engineered protein comprised of 7 IgG-binding domains EDABC-C1C3, corresponding to the Protein A and G domains which are included in the recombinant sequence. The Protein A part is from Staphylococcus aureus segments E, D, A, B and C. The Protein G part is from Streptococcus segments C1 and C3. The recombinant Protein A/G has a broader binding capacity than either Protein A or Protein G alone. The recombinant Protein A/G is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G binds to various human, mouse and rat IgG subclasses such as the human IgG1, IgG2, IgG3, IgG4; mouse IgG2a, IgG2b, IgG3 and rat IgG2a, IgG2c. In addition, Protein A/G binds to total IgG from cow, goat, sheep, horse, rabbit, guinea pig, pig, dog and cat.

Protein A is a cell wall protein deriving from Staphylococcus aureus which exhibits unique binding properties for IgG from a variety of mammalian species and for some IgM and IgA as well. It binds with the Fc region of immunoglobulins through interaction with the heavy chain. It couples to a wide variety of reporter molecules including fluorescent dyes, enzyme markers, biotin, colloidal gold and radioactive iodine without affecting the antibody binding site. Recombinant Protein A was developed to increase the specificity of the molecule for IgG and is widely used both in research and bioprocessing. The recombinant protein A is produced by expressing a modified protein A gene in E.coli. A specific purification process with strict quality control was taken to get the recombinant protein A with the purity of more than 98% , no human IgG affinity step is used during validated fermentation and purification and devoid of bacterial contaminant found normally in native Protein A. (Free of Staphylococcus endotoxins and hemolysin).

GADD45GIP1 is a nuclear protein which takes part in apoptosis control. GADD45GIP1 is expressed in several tissues, such as heart, thyroid, trachea, kidney, ovary, pancreas, testis and stomach and acts as a negative regulator of G1 to S phase cell cycle production by collaborating with GADD45 proteins to inhibit the activity of cyclin-dependent kinases.

Recombinant Protein A/G fusion protein joins IgG binding domains of both Protein A and Protein G.
Protein A/G includes four Fc binding domains from Protein A and two from Protein G, yielding a final mass of 50.4 kDa. The binding dependency to pH of Protein A/G lower than Protein A, but has the additive properties of Protein A and G together. Protein A/G binds to all subclasses of human IgG, making it helpful for purifying polyclonal or monoclonal IgG antibodies whose subclasses have not been identifieed. Protein A/G binds to IgA, IgE, IgM and IgD. Protein A/G binds to all subclasses of mouse IgG excluding mouse IgA, IgM or serum albumin. This permits Protein A/G to be used in purification and detection of mouse monoclonal IgG antibodies, with no interference from IgA, IgM and serum albumin. Mouse monoclonal antibodies normally have a stronger affinity to the chimeric Protein A/G than to either Protein A or Protein G. Protein A/G also has been used for purification of macaque IgG.

BAIAP2 is a ubiquitous regulator of the actin cytoskeleton. Controled by the Rho-family GTPases BAIAP2 facilitates filopodia development. BAIAP2 is expressed in the cytoplasm and binds small membrane-bound G-proteins to cytoplasmic effector proteins. BAIAP2 was identified as interacting with the dentatorubral-pallidoluysian atrophy gene, which is related to an autosomal dominant neurodegenerative disease.

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.

Ganglioside GM2 activator (GM2A) is a small glycolipid transport protein which functions as a substrate specific co-factor for the lysosomal enzyme beta-hexosaminidase A. GM2A participates in lipid metabolism. GM2A protein is localized in lysosomes. The GM2A protein forms a large binding pocket for a number of single chain phospholipids and fatty acids. GM2A demonstrates calcium-independent phospholipase activity. GM2A stimulates ganglioside GM2 degradation by presenting GM2 to beta-hexosaminidase A. The Beta-hexosaminidase A, along with GM2A, catalyzes the degradation of the ganglioside GM2, and other molecules containing terminal N-acetyl hexosamines. GM2A gene mutations result in GM2-gangliosidosis type AB or the AB variant of Tay-Sachs disease.

Adaptor-related protein complex 1 associated regulatory protein (AP1AR) is essential for AP-1 dependent transport between the trans-Golgi network and endosomes. AP1AR regulates the membrane association of AP1G1/Gamma1-adaptin which is one of the subunits of the AP-1 adapter complex. AP1AR plays a role as effector of AP-1 in calcium-induced endo-lysosome secretion. The interaction with AP1G1/Gamma1-adaptin attenuates the release of the AP-1 complex from membranes.

GPN-loop GTPase 1 (GPN1) is a member of the GPN-loop GTPase family. GPN1 is a guanosine triphosphatase enzyme which has a role in DNA repair and may function in activation of transcription. Small GTPases, which share a biochemical mechanism, act as binary molecular switches and function in the cell is nucleocytoplasmic transport of both proteins and RNA. In addition, GPN1 establishs an interface between the RNA polymerase II enzyme and chaperone/scaffolding protein, proposing that it is essential to connect RNA polymerase II to regulators of protein complex formation. GPN1 may also be involved in nuclear localization of XPA.

Golgi SNAP receptor complex member 2 isoform A (GOSR2) is a part of the SNARE Protein family which consists of important trafficking proteins between the endoplasmic reticulum and the Golgi and between Golgi subcompartments. GOSR2 is located near a locus implicated in familial essential hypertension, indicating that it is a potential candidate gene for this disease. GOSR2 exists as cytoplasmically oriented integral membrane proteins.

Glypican 4, also known as GPC4, is part of a family of glycosylphosphatidylinositol (GPI)-anchored heparan sulphate proteoglycans (HSPGs) which take part in the control of cell division and growth regulation. GPC4 is broadly expressed in human tissues, including lung, kidney, heart, placenta, skeletal muscle, and pancreas. In addition, GPC4 has been shown to be present in astrocytes, haematopoietic-progenitor and bone-marrow-stromal cells.

The signal sequence receptor (SSR) is a glycosylated endoplasmic reticulum membrane receptor related with protein translocation across the ER membrane. The SSR consists of 2 subunits, a 34-kD glycoprotein (alpha-SSR or SSR1) and a 22-kD glycoprotein (beta-SSR or SSR2). The human beta-signal sequence receptor gene (SSR2) maps to chromosome bands 1q21-q23. Diseases correlated with SSR2 include calcaneonavicular coalition, and osteosarcoma, and among its related super-pathways are Viral mRNA Translation and Generic Transcription Pathway.

GCSAM is a protein which functions in signal transduction pathways and whose expression raises in germinal cell lymphomas. GCSAM contains a putative PDZ-interacting domain, an immunoreceptor tyrosine-based activation motif (ITAM), and two putative SH2 binding sites. In B cells, GCSAM expression is particularly induced by interleukin-4.

Guanine nucleotide-binding protein G(z) subunit alpha (GNAZ) belongs to the G protein subfamily which mediates signal transduction in pertussis toxin-insensitive systems. GNAZ has a role in maintaining the ionic balance of perilymphatic and endolymphatic cochlear fluids. G proteins are involved as modulators or transducers in a variety of transmembrane signaling systems.

Synaptic vesicle membrane docking and fusion is mediated by SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) located on the vesicle membrane (v-SNAREs) and the target membrane (t-SNAREs). The assembled v-SNARE/t-SNARE complex consists of a bundle of four helices, one of which is supplied by v-SNARE and the other three by t-SNARE. For t-SNAREs on the plasma membrane, the protein syntaxin supplies one helix and the protein encoded by this gene contributes the other two. Therefore, SNAP25 product is a presynaptic plasma membrane protein involved in the regulation of neurotransmitter release. The synaptosomal-associated protein (SNAP-25) is an essential component of the core complex that mediates presynaptic vesicle trafficking. Thus, SNAP-25 is directly involved in the release of neurotransmitters.

Ras-related GTP binding C (RRAGC) is a monomeric guanine nucleotide-binding protein, or G protein. As a result of binding GTP or GDP, small G proteins act as molecular regulators in various cell processes and signaling pathways. RRAGC regulates the organization of the actin cytoskeleton and has an intrinsic GTPase activity. RRAGC is possibly necessary for the amino acid-induced relocalization of mTORC1 to the lysosomes and its succeeding activation by the GTPase RHEB, which is key step in the activation of the TOR signaling cascade by amino acids.

CB1 cannabinoid receptor-interacting protein 1 (CNRIP1) is a 164 amino acid protein and G-protein coupled receptor which is a member of the CNRIP family. The CNRIP1 interacts with the C-terminal tail of cannabinoid receptor 1. CNRIP1 is expressed in the brain tissue and, at low levels, in the testis. CNRIP1 is involved in appetite, synaptic plasticity, neuroprotection and analgesia.

Amino-terminal enhancer of split (AES) is a member of the groucho/TLE family of proteins. AES can function as a homooligomer or as a heteroologimer with other family members in order to forcefully repress the expression of other family member genes. Furthermore, AES can repress NFkB-regulated gene expression and is believed to have a significant role in initiating and maintaining cell differentiation events. AES is similar in sequence to the amino terminus of Drosophila enhancer of split groucho, a protein which is involved in neurogenesis during embryonic development. The AES protein is expressed predominately in the fetal brain, liver, lung, heart and kidney and also in the adult muscle.

MAPT is a neuronal microtubule associated protein localized mostly on axons.
MAPT promotes tubulin polymerisation and stabilizes microtubules, however it also serves to connect certain signalling pathways to the cytoskeleton. MAPT, in its hyperphosphorylated form, is the main part of paired helical filaments (PHF) and neurofibrillary lesions in Alzheimer''s disease (AD) brain.

Retinoic acid receptor alpha (RAR) belongs to the large family of ligand responsive gene regulatory proteins that includes receptors for steroid and thyroid hormones. These proteins contain two highly conserved domains that are involved in determining their DNA and ligand-binding activities. There are three isotypes of RAR proteins: alpha, beta, and gamma. The RAR proteins are encoded by distinct genetic loci and possess distinct transcriptional properties. Typically, RAR-alpha represses target gene transcription in the absence of hormone, whereas RAR-beta and gamma fail to repress under these conditions. RARA is a receptor for retinoic acid that has profound effects on vertebrate development. Retinoic acid is a morphogen and is a powerful teratogen. RARA controls cell function by directly regulating gene expression.
Chromosomal aberrations involving RARA cause acute promyelocytic leukemia (APL).