You Searched For: Boc-D-Asp-OBzl

Catalog Number: (10397-068)

Supplier: Bioss

Description: The three dimensional structure of many extracellular proteins is stabilized by the formation of disulphide bonds. Studies suggest that a microsomal enzyme known as Protein Disulphide Isomerase (PDI) is involved in disulphide-bond formation and isomerization, as well as the reduction of disulphide bonds in proteins. PDI, which catalyses disulphide interchange between thiols and protein dilsulphides, has also been referred to as thiol:protein-disulphide oxidoreductase and as glutathione:insulin transhydrogenase because of its role in reduction of disulphide bonds. The highly conserved sequence Lys-Asp-Glu-Leu (KDEL) is present at the carboxy-terminus of PDI and other soluble endoplasmic reticulum (ER) resident proteins including the 78 and 94 kDa glucose regulated proteins (GRP78 and GRP94 respectively). The presence of carboxy-terminal KDEL appears to be necessary for ER retention and appears to be sufficient to reduce the secretion of proteins from the ER. This retention is reported to be mediated by a KDEL receptor.

Supplier: Bachem Americas

Description: Fluorogenic (FRET) substrate for pro-memapsin-2 containing the β-secretase site EVNLDAEF of the Swedish mutation of APP. The kinetic parameters at pH 4.5 are Km = 5.4 µM and kcat = 0.24 min⁻¹.

Catalog Number: (10083-252)

Supplier: Proteintech

Description: ATG5, also named as APG5L and ASP, belongs to the ATG5 family. It is required for autophagy. It plays an important role in the apoptotic process, possibly within the modified cytoskeleton. Its expression is a relatively late event in the apoptotic process, occurring downstream of caspase activity. Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents. Formation of the autophagosome involves a ubiquitin-like conjugation system in which Atg12 is covalently bound to Atg5 and targeted to autophagosome vesicles. It mediates autophagosome-independent host protection. This antibody is raised against 28-275 amino acids of human ATG5. It can recognize the ATG5-ATG12 complex (55 kDa) and free ATG5 (32 kDa).

Catalog Number: (102997-140)

Supplier: Anaspec Inc

Description: HLA-A*0201 restricted epitope from influenza virus RNA polymerase subunit, PA (46-54).
Sequence: FMYSDFHFI
MW: 1206.4 Da
% Peak area by HPLC: 95
Storage condition: -20°C

Catalog Number: (CAPIPA5-18568)

Supplier: Thermo Scientific

Description: This antibody is predicted to react with canine, mouse and rat based on sequence homology. The protein encoded by this gene is a secreted, extracellular matrix protein containing an Arg-Gly-Asp motif and calcium-binding EGF-like domains. It promotes adhesion of endothelial cells through interaction of integrins and the RGD motif. It is prominently expressed in developing arteries but less so in adult vessels. However, its expression is reinduced in balloon-injured vessels and atherosclerotic lesions, notably in intimal vascular smooth muscle cells and endothelial cells. Therefore, the protein encoded by this gene may play a role in vascular development and remodeling. Defects in this gene are a cause of autosomal dominant cutis laxa, autosomal recessive cutis laxa type I , and age-related macular degeneration type 3 .

Catalog Number: (M-2485.0001BA)

Supplier: Bachem Americas

Description: Fluorogenic (FRET) substrate for pro-memapsin-2 containing the β-secretase site of the Swedish mutation of APP. The kinetic parameters of Mca-SEVNLDAEFK(Dnp) amide at pH 4.5 are Km = 4.5 µM and kcat = 0.25 min⁻¹.

Catalog Number: (76078-418)

Supplier: Bioss

Description: The three dimensional structure of many extracellular proteins is stabilized by the formation of disulphide bonds. Studies suggest that a microsomal enzyme known as Protein Disulphide Isomerase (PDI) is involved in disulphide-bond formation and isomerization, as well as the reduction of disulphide bonds in proteins. PDI, which catalyses disulphide interchange between thiols and protein dilsulphides, has also been referred to as thiol:protein-disulphide oxidoreductase and as glutathione:insulin transhydrogenase because of its role in reduction of disulphide bonds. The highly conserved sequence Lys-Asp-Glu-Leu (KDEL) is present at the carboxy-terminus of PDI and other soluble endoplasmic reticulum (ER) resident proteins including the 78 and 94 kDa glucose regulated proteins (GRP78 and GRP94 respectively). The presence of carboxy-terminal KDEL appears to be necessary for ER retention and appears to be sufficient to reduce the secretion of proteins from the ER. This retention is reported to be mediated by a KDEL receptor.

Catalog Number: (75789-482)

Supplier: Prosci

Description: CD99 is a type I transmembrane glycoprotein and the founding member of the CD99 family of molecules. The extracellular domain of CD99 contains no identifiable motifs, its cytoplasmic region, although short, does have signal transduction capability. Cells known to express CD99 include fibroblasts, neutrophils, T cells, double positive thymocytes, CD34+ stem cells, monocytes and endothelial cells. Two types of CD99 isoforms have been classified. Native human CD99 is referred to as the long, or type I isoform. The best studied type II isoform shows an Asp-Gly substitution for the C terminal 27 amino acids. The type I and II isoforms have distinctive signal transduction pathways (FAKsrc for type I PI3K plus srcERK1/2 for type II), and mediate clearly different biological outcomes. Homophilic interaction between CD99 on the neutrophil and CD99 on the endothelial cell regulates the transendothelial migration of neutrophils during inflammation. Human CD99 has 48% aa sequence identity to mouse CD99.

Supplier: Bachem Americas

Description: Heavy isotope-labeled human pTH (1-34) (Teriparatide) useful for pharmacokinetic/pharmacodynamic studies in combination with Bachem product H-4835 pTH (1-34) (human) or the corresponding generic API.

Catalog Number: (10397-052)

Supplier: Bioss

Description: The three dimensional structure of many extracellular proteins is stabilized by the formation of disulphide bonds. Studies suggest that a microsomal enzyme known as Protein Disulphide Isomerase (PDI) is involved in disulphide-bond formation and isomerization, as well as the reduction of disulphide bonds in proteins. PDI, which catalyses disulphide interchange between thiols and protein dilsulphides, has also been referred to as thiol:protein-disulphide oxidoreductase and as glutathione:insulin transhydrogenase because of its role in reduction of disulphide bonds. The highly conserved sequence Lys-Asp-Glu-Leu (KDEL) is present at the carboxy-terminus of PDI and other soluble endoplasmic reticulum (ER) resident proteins including the 78 and 94 kDa glucose regulated proteins (GRP78 and GRP94 respectively). The presence of carboxy-terminal KDEL appears to be necessary for ER retention and appears to be sufficient to reduce the secretion of proteins from the ER. This retention is reported to be mediated by a KDEL receptor.

Catalog Number: (75790-404)

Supplier: Prosci

Description: CD99 is a type I transmembrane glycoprotein and the founding member of the CD99 family of molecules. The extracellular domain of CD99 contains no identifiable motifs, its cytoplasmic region, although short, does have signal transduction capability. Cells known to express CD99 include fibroblasts, neutrophils, T cells, double positive thymocytes, CD34+ stem cells, monocytes and endothelial cells. Two types of CD99 isoforms have been classified. Native human CD99 is referred to as the long, or type I isoform. The best studied type II isoform shows an Asp-Gly substitution for the C terminal 27 amino acids. The type I and II isoforms have distinctive signal transduction pathways (FAKsrc for type I PI3K plus srcERK1/2 for type II), and mediate clearly different biological outcomes. Homophilic interaction between CD99 on the neutrophil and CD99 on the endothelial cell regulates the transendothelial migration of neutrophils during inflammation. Human CD99 has 48% aa sequence identity to mouse CD99.

Catalog Number: (10397-072)

Supplier: Bioss

Description: The three dimensional structure of many extracellular proteins is stabilized by the formation of disulphide bonds. Studies suggest that a microsomal enzyme known as Protein Disulphide Isomerase (PDI) is involved in disulphide-bond formation and isomerization, as well as the reduction of disulphide bonds in proteins. PDI, which catalyses disulphide interchange between thiols and protein dilsulphides, has also been referred to as thiol:protein-disulphide oxidoreductase and as glutathione:insulin transhydrogenase because of its role in reduction of disulphide bonds. The highly conserved sequence Lys-Asp-Glu-Leu (KDEL) is present at the carboxy-terminus of PDI and other soluble endoplasmic reticulum (ER) resident proteins including the 78 and 94 kDa glucose regulated proteins (GRP78 and GRP94 respectively). The presence of carboxy-terminal KDEL appears to be necessary for ER retention and appears to be sufficient to reduce the secretion of proteins from the ER. This retention is reported to be mediated by a KDEL receptor.

Catalog Number: (10397-066)

Supplier: Bioss

Description: The three dimensional structure of many extracellular proteins is stabilized by the formation of disulphide bonds. Studies suggest that a microsomal enzyme known as Protein Disulphide Isomerase (PDI) is involved in disulphide-bond formation and isomerization, as well as the reduction of disulphide bonds in proteins. PDI, which catalyses disulphide interchange between thiols and protein dilsulphides, has also been referred to as thiol:protein-disulphide oxidoreductase and as glutathione:insulin transhydrogenase because of its role in reduction of disulphide bonds. The highly conserved sequence Lys-Asp-Glu-Leu (KDEL) is present at the carboxy-terminus of PDI and other soluble endoplasmic reticulum (ER) resident proteins including the 78 and 94 kDa glucose regulated proteins (GRP78 and GRP94 respectively). The presence of carboxy-terminal KDEL appears to be necessary for ER retention and appears to be sufficient to reduce the secretion of proteins from the ER. This retention is reported to be mediated by a KDEL receptor.

Catalog Number: (10397-074)

Supplier: Bioss

Description: The three dimensional structure of many extracellular proteins is stabilized by the formation of disulphide bonds. Studies suggest that a microsomal enzyme known as Protein Disulphide Isomerase (PDI) is involved in disulphide-bond formation and isomerization, as well as the reduction of disulphide bonds in proteins. PDI, which catalyses disulphide interchange between thiols and protein dilsulphides, has also been referred to as thiol:protein-disulphide oxidoreductase and as glutathione:insulin transhydrogenase because of its role in reduction of disulphide bonds. The highly conserved sequence Lys-Asp-Glu-Leu (KDEL) is present at the carboxy-terminus of PDI and other soluble endoplasmic reticulum (ER) resident proteins including the 78 and 94 kDa glucose regulated proteins (GRP78 and GRP94 respectively). The presence of carboxy-terminal KDEL appears to be necessary for ER retention and appears to be sufficient to reduce the secretion of proteins from the ER. This retention is reported to be mediated by a KDEL receptor.

Catalog Number: (102981-166)

Supplier: Adipogen

Description: R-FSL-1 (R-Pam2CGDPKHPKSF) is a synthetic lipoprotein that represents the N-terminal part of the 44kDa lipoprotein LP44 of Mycoplasma salivarium. The naturally occurring R-stereoisomer is biologically more active than the S-stereoisomer. Stimulator of TLR2/TLR6. Inducer of TNF-alpha production in macrophages. Upregulates proinflammatory cytokines. Activator of the proinflammatory transcription factor NF-kappaB.

Catalog Number: (10397-064)

Supplier: Bioss

Description: The three dimensional structure of many extracellular proteins is stabilized by the formation of disulphide bonds. Studies suggest that a microsomal enzyme known as Protein Disulphide Isomerase (PDI) is involved in disulphide-bond formation and isomerization, as well as the reduction of disulphide bonds in proteins. PDI, which catalyses disulphide interchange between thiols and protein dilsulphides, has also been referred to as thiol:protein-disulphide oxidoreductase and as glutathione:insulin transhydrogenase because of its role in reduction of disulphide bonds. The highly conserved sequence Lys-Asp-Glu-Leu (KDEL) is present at the carboxy-terminus of PDI and other soluble endoplasmic reticulum (ER) resident proteins including the 78 and 94 kDa glucose regulated proteins (GRP78 and GRP94 respectively). The presence of carboxy-terminal KDEL appears to be necessary for ER retention and appears to be sufficient to reduce the secretion of proteins from the ER. This retention is reported to be mediated by a KDEL receptor.