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RAET1L plays a role as a stress-induced ligand for NKG2D receptor. Retinoic Acid Early Transcript 1L (RAET1L) is linked to the cell membrane by the GPI anchor. HCMV infection triggers RAET1L’sexpression but HCMV alters its function. HCMV-encoded UL16 glycoprotein retains RAET1L/ULBP6 inside the cells, preventing it from reaching the cell surface and being exposed to cells of the immune system. RAET1L has a more restricted expression profile in cell lines and primary human tissues than other NKG2D ligands.

SNRPD1 Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 16kDa.
SNRPD1 is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.

BID accession number NP_001187 is a pro-apoptotic Bcl-2 protein having only the BH3 domain. In reaction to apoptotic signaling, BID interacts with another Bcl-2 family of cell death regulators, called Bax, they form a heterodimer resulting to the insertion of Bax into the outer mitochondrial membrane. Bax induces the opening of the mitochondrial voltage-dependent anion channel which lead to the release of cytochrome c and other pro-apoptotic factors from the mitochondria resulting in activation of caspases. BID is a mediator of mitochondrial damage induced by caspase-8 (CASP8). CASP8 cleaves BID, and the COOH-terminal part translocates to mitochondria where it triggers cytochrome c release. The major proteolytic product p15 BID releasea cytochrome c. Isoform 1, Isoform 2 and Isoform 4 induce ice-like proteases and apoptosis while Isoform 3 does not induce apoptosis.

STAM Binding Protein Like 1 (STAMBPL1) is a zinc metalloprotease which specifically cleaves 'Lys-63'-linked polyubiquitin chains, however, it doesn’t cleave 'Lys-48'-linked polyubiquitin chains. STAMBPL1 binds 2 zinc ions per subunit. The JAMM motif is vital for the protease activity. STAMBPL1 is a member of the peptidase M67C family. STAMBPL1 contains 1 MPN (JAB/Mov34) domain.

Small VCP/p97-interacting protein (SVIP) is involved in various cellular processes, including membrane fusion and ubiquitin-dependent protein degradation. SVIP functions as an inhibitor of the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway. On the other hand, SVIP overexpression increased the levels of p62 protein and enhanced starvation-activated autophagy as well as stimulated sequestration of polyubiquitinated proteins and p62 in autophagosomes.

PDXP is the active form of vitamin B6 that functions as a coenzyme in preserving biochemical homeostasis. The desired degradation route from PLP to 4-pyridoxic acid involves the dephosphorylation of PLP by PDXP. PDXP shows activity to pyridoxal 5''-phosphate (PLP), pyridoxine 5''-phosphate (PMP) and Pyridoxine 5''-phosphate (PNP), with a highest activity with PLP followed by PNP.

Phospholipid scramblase (PLSCR1) is a member of the phospholipid scramblase family. PLSCR1 has a significant part in the antiviral reaction of IFN by intensifying and improving the IFN reaction via increasing expression of select subset of potent antiviral genes. PLSCR1 promotes cytokine-regulated cell proliferation and differentiation.

Gem-Associated Protein 6 (GEMIN6) is a member of a large macromolecular complex, localized to both the cytoplasm and the nucleus, which takes part in the cytoplasmic assembly of small nuclear ribonucleoproteins (snRNPs). SMN, GEMIN2, GEMIN3, GEMIN4, and GEMIN5 are additional members of this complex.

Mannose-6-Phosphate Receptor (M6PR) belongs to the P-type lectin family. P-type lectins play a vital role in lysosome function through the specific transport of mannose-6-phosphate-containing acid hydrolases from the Golgi complex to lysosomes. The M6PR protein functions as a homodimer and needs divalent cations for ligand binding. Lysosomal enzymes carrying phosphomannosyl residues bind specifically to mannose-6-phosphate receptors in the Golgi apparatus and the ensuing receptor-ligand complex is transferred to an acidic prelyosomal compartment where the low pH mediates the dissociation of the complex.

CRH is a powerful stimulator of synthesis and secretion of preopiomelanocortin-derived peptides. CRH concentration in the human peripheral circulation is usually low. The concentration rises during pregnancy and fall back quickly after parturition. Maternal plasma CRH most likely originates from the placenta. Human plasma has a CRH-binding protein that inactivates CRH and can inhibit inappropriate pituitary-adrenal stimulation in pregnancy.

RPA-interacting protein isoform d (RPAIN) is a single-stranded-DNA binding protein which participates in various eukaryotic DNA processes such as replication, repair and recombination. RPAIN interacting protein has been indicated as an adapter protein that is involved in RPA nuclear import instead of the prototypical importin proteins that normally mediate nuclear import. RPAIN is mainly expressed in pancreas, kidney, muscle, liver, lung, placenta, brain, heart, leukocytes, colon, intestine, ovary, testis, prostate, thymus and spleen.

S100A6 is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. S100 proteins are involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21. S100A6 function in stimulation of prolactin secretion and exocytosis. Chromosomal rearrangements and altered expression of the S100A6 gene are implicated in melanoma.

S100P is a Ca2+ binding protein that is part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are found in the cytoplasm and/or nucleus of a large range of cells, and participates in the regulation of a number of cellular function such as cell cycle progression and differentiation. S100P participates in numerous biological functions but the exact functions or mechanism of its action is still mostly unknown. Once S100P binds calcium ions it goes through a conformational change that results in an exposure of a hydrophobic surface which permits the interaction with specific target proteins.

Heterogeneous nuclear ribonucleoprotein A1 (HNRNPA1) is a member of the A/B subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). HNRNPA1 is involved in the packing of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and may control splice site selection. The HNRNPA1 protein may also have a role in HCV RNA replication. In addition, HNRNPA1 is believed to have a key role in the formation of specific myometrial protein species in parturition.
The hnRNP proteins have distinctive nucleic acid binding properties. HNRNPA1 has 2 repeats of quasi-RRM domains that bind to RNAs. HNRNPA1 is one of the most copious core proteins of hnRNP complexes and it is restricted to the nucleoplasm. The HNRNPA1 protein, along with other hnRNP proteins, is exported from the nucleus, most likely bound to mRNA, and is immediately re-imported. The M9 domain of HNRNPA1 functions as both a nuclear localization and nuclear export signal.

Secreted Frizzled-Related Protein 5, also known as SFRP5, belongs to the SFRP family which includes a cysteine-rich domain homologous to the putative Wnt-binding site of Frizzled proteins. SFRPs perform like soluble modulators of Wnt signaling. SFRP5 & SFRP1 are implicated in determining the polarity of photoreceptor cells in the retina. SFRP5 is highly expressed in the retinal pigment epithelium, as well as moderately expressed in the pancreas.

BATF is a nuclear basic leucine zipper protein which is a member of the AP-1/ATF superfamily of transcription factors. BATF is intensely expressed in mature T and B lymphocytes, and is up-regulated after transformation by human T-cell leukemia virus type I. BATF acts as a tissue-specific modulator of the AP-1 transcription complex in human cells. Furthermore, BATF connects with IFP35 which is a leucine zipper protein that translocates to the nucleus following IFN treatment.

TCEB1 (elongin C) is a subunit of elongin, which is a common transcription elongation factor that increases the RNA polymerase II transcription elongation past template encoded arresting sites. The SIII complex is comprised of elongins A/A2, B and C. The SIII complex activates elongation by RNA polymerase II by curbing transient pausing of the polymerase at numerous sites within transcription units. Elongin A acts as the transcriptionally active component of the SIII complex, while elongins B and C are regulatory subunits. Elongin A2 is specifically expressed in the testis, and able to forming a stable complex with elongins B and C. The VHL (von Hippel-Lindau) tumor suppressor protein binds to elongins B and C, and thus inhibits transcription elongation.

KLRB1 has an inhibitory role on natural killer (NK) cells cytotoxicity which are lymphocytes who facilitate cytotoxicity and secrete cytokines subsequent to immune stimulation. Some genes of the C-type lectin superfamily, like the rodent NKRP1 family of glycoproteins, are expressed by NK cells and take part in NK cell function regulation. KLRB1 holds an extracellular domain with a few characteristic motifs of C-type lectins, a transmembrane domain, and a cytoplasmic domain. Due to its external C terminus KLRB1 is considered to be a type II membrane protein.

LDHA catalyzes the conversion of L-lactate and NAD to pyruvate and NADH in the final step of anaerobic glycolysis. LDHA is localized primarily in muscle tissue and is part of the lactate dehydrogenase family. Mutations in LDHA have been linked to exertional myoglobinuria. LDH1 is decreased in essential thrombocythemia. LDHA is induced through a non-genomic pathway of estrogen action. Reduction in LDH-A activity results in stimulation of mitochondrial respiration and decrease of mitochondrial membrane potential.

The proteasome is a multicatalytic proteinase complex with an extremely organized ring-shaped 20S core structure. The core structure consists of 4 rings of 28 non-identical subunits; 2 rings consist of 7 alpha subunits and 2 rings consist of 7 beta subunits. Proteasomes are spread all over the eukaryotic cells in large quantities and cleave peptides in an ATP/ubiquitin-dependent procedure in a non-lysosomal pathway. A vital role of a modified proteasome, the immunoproteasome, is the handling of class I MHC peptides.