DPM1 blocking peptide Reference: GTX88562-PEP Dolichol-phosphate mannose (Dol-P-Man) serves as a donor of mannosyl residues on the lumenal side of the endoplasmic reticulum (ER). Lack of Dol-P-Man results in defective surface expression of GPI-anchored proteins. Dol-P-Man is synthesized from GDP-mannose and dolichol-phosphate on the cytosolic side of the ER by the enzyme dolichyl-phosphate mannosyltransferase. Human DPM1 lacks a carboxy-terminal transmembrane domain and signal sequence and is regulated by DPM2. [provided by RefSeq, Jul 28]
Recombinant Human IL-27 / EBI-3 Reference: GFH162-5 Epstein-Barr virus induced gene-3 (EBI-3), is a secreted glycoprotein belonging to the hematopoietin receptor family related to the p40 subunit of interleukin-12 (IL-12). EBI-3 expression is induced in B-lymphocytes in response to Epstein-Barr virus infection. EBI-3 forms heterodimers with p28 to form interleukin-27 (IL-27), and with p35 to form interleukin-35 (IL-35). Both IL-27 and IL-35 have anti-inflammatory and regulatory activity.
COG7 blocking peptide Reference: GTX88563-PEP The protein encoded by this gene resides in the golgi, and constitutes one of the 8 subunits of the conserved oligomeric Golgi (COG) complex, which is required for normal golgi morphology and localization. Mutations in this gene are associated with the congenital disorder of glycosylation type IIe.[provided by RefSeq, May 21]
Recombinant Human IL-27 / EBI-3 Reference: GFH162-20 Epstein-Barr virus induced gene-3 (EBI-3), is a secreted glycoprotein belonging to the hematopoietin receptor family related to the p40 subunit of interleukin-12 (IL-12). EBI-3 expression is induced in B-lymphocytes in response to Epstein-Barr virus infection. EBI-3 forms heterodimers with p28 to form interleukin-27 (IL-27), and with p35 to form interleukin-35 (IL-35). Both IL-27 and IL-35 have anti-inflammatory and regulatory activity.
Lactoferrin blocking peptide Reference: GTX88565-PEP This gene is a member of the transferrin family of genes and its protein product is found in the secondary granules of neutrophils. The protein is a major iron-binding protein in milk and body secretions with an antimicrobial activity, making it an important component of the non-specific immune system. The protein demonstrates a broad spectrum of properties, including regulation of iron homeostasis, host defense against a broad range of microbial infections, anti-inflammatory activity, regulation of cellular growth and differentiation and protection against cancer development and metastasis. Antimicrobial, antiviral, antifungal and antiparasitic activity has been found for this protein and its peptides. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Sep 214]
Recombinant Human IL-27 / EBI-3 Reference: GFH162-100 Epstein-Barr virus induced gene-3 (EBI-3), is a secreted glycoprotein belonging to the hematopoietin receptor family related to the p40 subunit of interleukin-12 (IL-12). EBI-3 expression is induced in B-lymphocytes in response to Epstein-Barr virus infection. EBI-3 forms heterodimers with p28 to form interleukin-27 (IL-27), and with p35 to form interleukin-35 (IL-35). Both IL-27 and IL-35 have anti-inflammatory and regulatory activity.
IDS blocking peptide Reference: GTX88566-PEP The protein encoded by this gene belongs to the sulfatase family, is localized to the lysosome, and is involved in lysosomal degradation of heparan sulfate and dermatan sulfate. Mutations in this gene are associated with the X-linked lysosomal storage disease, mucopolysaccharidosis type II, also known as Hunter syndrome. Alternatively spliced transcript variants have been described for this gene. [provided by RefSeq, Aug 213]
Recombinant Human IL-27 / EBI-3 Reference: GFH162-1000 Epstein-Barr virus induced gene-3 (EBI-3), is a secreted glycoprotein belonging to the hematopoietin receptor family related to the p40 subunit of interleukin-12 (IL-12). EBI-3 expression is induced in B-lymphocytes in response to Epstein-Barr virus infection. EBI-3 forms heterodimers with p28 to form interleukin-27 (IL-27), and with p35 to form interleukin-35 (IL-35). Both IL-27 and IL-35 have anti-inflammatory and regulatory activity.
ERP29 blocking peptide Reference: GTX88567-PEP This gene encodes a reticuloplasmin, a protein which resides in the lumen of the endoplasmic reticulum (ER). The protein shows sequence similarity to the protein disulfide isomerase family. However, it lacks the thioredoxin motif characteristic of this family, suggesting that this protein does not function as a disulfide isomerase. The protein dimerizes and is thought to play a role in the processing of secretory proteins within the ER. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jul 28]
Recombinant Human IL-27 / EBI-3 (Animal-Free) Reference: GFH162AF-5 Epstein-Barr virus induced gene-3 (EBI-3), is a secreted glycoprotein belonging to the hematopoietin receptor family related to the p40 subunit of interleukin-12 (IL-12). EBI-3 expression is induced in B-lymphocytes in response to Epstein-Barr virus infection. EBI-3 forms heterodimers with p28 to form interleukin-27 (IL-27), and with p35 to form interleukin-35 (IL-35). Both IL-27 and IL-35 have anti-inflammatory and regulatory activity.
Endothelial Lipase / LIPG blocking peptide Reference: GTX88568-PEP The protein encoded by this gene has substantial phospholipase activity and may be involved in lipoprotein metabolism and vascular biology. This protein is designated a member of the TG lipase family by its sequence and characteristic lid region which provides substrate specificity for enzymes of the TG lipase family. [provided by RefSeq, Jul 28]
Recombinant Human IL-27 / EBI-3 (Animal-Free) Reference: GFH162AF-20 Epstein-Barr virus induced gene-3 (EBI-3), is a secreted glycoprotein belonging to the hematopoietin receptor family related to the p40 subunit of interleukin-12 (IL-12). EBI-3 expression is induced in B-lymphocytes in response to Epstein-Barr virus infection. EBI-3 forms heterodimers with p28 to form interleukin-27 (IL-27), and with p35 to form interleukin-35 (IL-35). Both IL-27 and IL-35 have anti-inflammatory and regulatory activity.