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Trafficking Protein Particle Complex 2 (TRAPPC2) is assumed to be part of a large multi-subunit complex involved in the targeting and fusion of endoplasmic reticulum-to-Golgi transport vesicles with their acceptor compartment. Moreover, the TRAPPC2 protein can bind c-myc promoter-binding protein 1 and block its transcriptional repression capability. TRAPPC2 gene mutations are a cause of spondyloepiphyseal dysplasia tarda (SEDT).

Trafficking protein particle complex 4 (TRAPPC4) is part of the multisubunit TRAPP (transport protein particle) complex and interacts with SDC2. TRAPPC4 has a role in vesicular transport from endoplasmic reticulum to Golgi.

Trafficking Protein Particle Complex 2-Like (TRAPPC2L) takes part in vesicular transport from endoplasmic reticulum to Golgi. TRAPPC2L is a part of the TRAPP small subunits family and is expressed in various organs like testis, liver, bladder, lung, spleen and brain.

TRAPPC3 is a part of the TRAPP complex that takes part in connection of transport vesicles to the cis-Golgi membrane. Additionally, TRAPPC3 is involved in vesicular transport from endoplasmic reticulum to Golgi.

Vesicle-trafficking protein SEC22b precursor (SEC22B) is a member of the synaptobrevin family. SEC22B forms a complex with SNARE and it is believed to have a role in the ER-Golgi protein trafficking. SEC22B has a strong similarity to the mouse and Chinese hamster proteins.

TRAF Family Member-Associated NFKB Activator (TANK) is located in the cytoplasm and binds Either TRAF1, TRAF2 or TRAF3. TANK is an inhibitor of TRAF function which regulates TRAF protein activity via sequestering TRAFs in a dormant position in the cytoplasm. Overexpression of TANK, inhibits TRAF2-mediated NF-Kappa-B activation signaled by CD40 and both TNF receptors and also inhibits LMP1-mediated NFkappa-B activation by blocking the connection of TRAF2 with LMP1.

BAT3 complex is a multiprotein complex which takes part in the post-translational delivery of tail-anchored (TA) membrane proteins to the endoplasmic reticulum membrane. Golgi To ER Traffic Protein 4 (GET4) is a part of the BAT3 complex. The complex functions by helping TA proteins (which contain a single C-terminal transmembrane region) which are captured by ASNA1/TRC40. BAT3 complex synthesizes membrane proteins, interacts with the transmembrane area of recently released TA proteins, and transfers them to ASNA1/TRC40 for targeting.

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.

SRP54 is a 54-kDa subunit of the signal recognition particle (SRP), a cytoplasmic ribonucleoprotein complex which leads the translocation of newly synthesized secretory proteins from the polysome to the endoplasmic reticulum. SRP is composed of six polypeptides and a tRNA-like molecule known as 7SL RNA. SRP54 is a GTP-binding protein that directly binds the signal sequences of nascent secretory and membrane proteins. Anti-SRP autoantibodies take place in patients with an autoimmune chronic muscle inflammation called polymyositis. These auto-antibodies predominantly recognize the SRP54 subunit and in addition are able to immunoprecipitate several of the SRP subunits and the RNA component. Nearly 5% of myositis patients are positive for anti-SRP autoantibodies, increasing to 18% in the subgroup of Jo-1 autoantibody-negative patients. The classic 'anti-SRP syndrome' is a severe form of polymyositis in which the myositic inflammation is acute and aggressive onset, with common myalgias and cardiac involvement. Normally there is a poor reaction to therapy with a 5-year survival rate of about 25%.

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.

Vacuolar protein sorting-associated protein 26A (VPS26A) is a vital element of the retromer complex, which is required to recover lysosomal enzyme receptors (IGF2R and M6PR) from endosomes to the trans-Golgi network. Furthermore, VPS26A is essential in the regulation of transcytosis of the polymeric immunoglobulin receptor (pIgR-pIgA). Expression analysis in yeast and mammalian cells reveal that VPS26A interacts directly with VPS35 that functions as the core of the retromer complex.

HOMER1 takes part in determining the apoptotic susceptibility to TRAIL.
HOMER1 is a member of the Homer family of proteins that regulate signal transduction through, and the trafficking of, glutamate receptors, plus maintain and regulate extracellular glutamate levels in corticolimbic brain regions. The HOMER1 is enriched at excitatory synapses and binds group 1 metabotropic glutamate receptors (mGluRs).

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.

IFIH1 is a DEAD box protein which is upregulated in response to treatment with beta-interferon and a protein kinase C-activating compound, mezerein. Irreversible reprogramming of melanomas can be attained by therapy with both these agents; treatment with either agent alone only achieves reversible differentiation. DEAD box proteins are implicated in several cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly.

VAPB Vesicle-associated membrane protein (VAMP)-associated protein B (aka VAPB) is a type IV transmembrane protein and belongs to the VAP family of proteins. VAPB may have a role in vesicle trafficking. VAPB is found in plasma and intracellular vesicle membranes as a homodimer and heterodimer with VAPA, and interacts with VAMP1 and VAMP2. VAPB defects are the basis for the amyotrophic lateral sclerosis type 8 and spinal muscular atrophy autosomal dominant Finkel type.

Muted homolog (MUTED) is a component of the BLOC-1 complex, a complex which is necessary for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. The BLOC-1 complex is needed to steer membrane protein cargos into vesicles assembled at cell bodies for release into neurites and nerve terminals. In addition, this complex, along with SNARE proteins, is suggested to be involved in neurite extension. MUTED also interacts with pallidin, dystrobrevin binding protein 1 and CNO/cappuccino. MUTED is ubiquitously expressed with higher levels in the brain, bone marrow, kidney, and liver and lower levels in the skeletal muscle.

AMRC10 is a protein which contains an armadillo repeat and transmembrane domain. Upregulation of the AMRC10 gene has a role in hepatocellular carcinoma. AMRC10 decreases the transcriptional activity of the tumor suppressor protein p53 through direct interaction with the DNA-binding domain of p53, moreover it might play a role in cell growth and survival.

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.

Syntaxin is membrane integrated Q-SNARE protein participating in exocytosis. Syntaxin is composed of an N-terminal regulatory domain (Habc), a SNARE domain (known as H3), and a single C-terminal transmembrane domain. The SNARE (H3) domain binds to both synaptobrevin and SNAP-25 forming the core SNARE complex. Synaptic vesicles store neurotransmitters that are released during calcium-regulated exocytosis. The specificity of neurotransmitter release requires the localization of both synaptic vesicles and calcium channels to the presynaptic active zone. Syntaxins function in this vesicle fusion process. Syntaxins also serve as a substrate for botulinum neurotoxin type C, a metalloprotease that blocks exocytosis and has high affinity for a molecular complex that includes the alpha-latrotoxin receptor which produces exocytosis.

BLOC1S2 is a member of the BLOC1S2 family. Biogenesis of lysosome-related organelles complex 1 or BLOC-1 is a universally expressed multisubunit protein complex which is essential for regular biogenesis of specialized organelles of the endosomal-lysosomal system, like melanosomes and platelet dense granules. BLOC1S2 takes part in cell proliferation.

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.

Aprotinin inhibits the activity of several proteolytic enzymes such as chymotrypsin, kallikrein, plasmin and trypsin. Aprotinin is present in blood and in most tissues, with a high concentration in lung. Aprotinin inhibits pro-inflammatory cytokine release and maintains glycoprotein homeostasis. In platelets, aprotinin reduces glycoprotein loss (e.g., GpIb, GpIIb/IIIa), while in granulocytes it prevents the expression of pro-inflammatory adhesive glycoproteins (e.g., CD11b).

VPS28 is a subunit of the ESCRT-I complex (endosomal complexes required for transport) involved in the sorting of ubiquitinated proteins. VPS28 is involved in endosomal sorting of cell surface receptors using a multivesicular body/late endosome pathway. VSP28 binding with the TSG101 may have significant roles in budding of Retroviruses, such as HIV-1 and Ebola virus.
VSP28 interacts with TSG101, VPS37B, VPS37C, FAM125A and FAM125B, and also with VPS36, this interaction mediates the association with the ESCRT-II complex. Furthermore it interacts with SNF8 and VPS25 and CEP55.

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).