9500 Results for: "Fmoc-D-Asp-odor"

Supplier: Bioss

DEAD-box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp, are putative RNA helicases implicated in several cellular processes involving modifications of RNA secondary structure and ribosome/spliceosome assembly. Based on their distribution patterns, some members of this family may be involved in embryogenesis, spermatogenesis, and cellular growth and division. DDX32 is a 743 amino acid nuclear protein that localizes to the mitochondria and is a member of the DEAD box helicase family. Expressed in various tissues, DDX32 is up-regulated by ionomycin in T lymphocytes and down-regulated in acute lymphoblastic leukemia. Considered a novel RNA helicase, DDX32 may play an important role in the development of colorectal cancer and may be involved in regulating T-cell response to certain apoptotic stimuli.

Supplier: Bachem Americas

c(RGDfV) is a potent inhibitor of cell adhesion. It inhibited tumor cell adhesion to laminin and vitronectin substrates. In vivo investigations in rats provided the first evidence of its utility in the amelioration of ischemic acute renal failure. c(RGDfV) inhibited tubular obstruction by preventing cell-cell adhesion. Hammes et al. showed that the cyclopeptide can also be used to prevent retinal neovascularization. c(RGDfV) binds to αvβ3 receptors.

Supplier: Bioss

Binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction. Promotes Arg-Gly-Asp-dependent cell attachment.

Supplier: Bachem Americas

Substrates often used for characterizing newly isolated PPIases, subtilisins or other enzymes. Bachem offers Suc-Ala-Ala-Pro-Xaa (Suc-AAPX) substrates containing Ala, Leu, Met, Nle, and Nva (the pancreatic elastase substrates L-1775, L-1390, L-1395, and L-1780), Arg, Asp, Glu, Ile, Lys, Orn, Phe (the PPIase substrates I-1465, L-1400, and M-2305), and Val (the neutrophil elastase substrates I-1490 and L-1770) as Xaa.

Supplier: Prosci

DDX23 encodes a member of the DEAD box protein family. DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are implicated in a number of cellular processes involving alteration of RNA secondary structure, such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Based on their distribution patterns, some members of this family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. The protein encoded by this gene is a component of the U5 snRNP complex; it may facilitate conformational changes in the spliceosome during nuclear pre-mRNA splicing. An alternatively spliced transcript variant has been found for this gene, but its biological validity has not been determined.

Supplier: Bioss

DEAD-box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp, are putative RNA helicases implicated in several cellular processes involving modifications of RNA secondary structure and ribosome/spliceosome assembly. Based on their distribution patterns, some members of this family may be involved in embryogenesis, spermatogenesis, and cellular growth and division. DDX32 is a 743 amino acid nuclear protein that localizes to the mitochondria and is a member of the DEAD box helicase family. Expressed in various tissues, DDX32 is up-regulated by ionomycin in T lymphocytes and down-regulated in acute lymphoblastic leukemia. Considered a novel RNA helicase, DDX32 may play an important role in the development of colorectal cancer and may be involved in regulating T-cell response to certain apoptotic stimuli.

Supplier: Bioss

DEAD-box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp, are putative RNA helicases implicated in several cellular processes involving modifications of RNA secondary structure and ribosome/spliceosome assembly. Based on their distribution patterns, some members of this family may be involved in embryogenesis, spermatogenesis, and cellular growth and division. DDX32 is a 743 amino acid nuclear protein that localizes to the mitochondria and is a member of the DEAD box helicase family. Expressed in various tissues, DDX32 is up-regulated by ionomycin in T lymphocytes and down-regulated in acute lymphoblastic leukemia. Considered a novel RNA helicase, DDX32 may play an important role in the development of colorectal cancer and may be involved in regulating T-cell response to certain apoptotic stimuli.

Supplier: Bioss

Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10. May participate in the GZMB apoptotic pathways. Cleaves ADPRT. Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-|-AMC. Likely target for the cowpox virus CRMA death inhibitory protein. Isoform 5, isoform 6, isoform 7 and isoform 8 lack the catalytic site and may interfere with the pro-apoptotic activity of the complex.

Supplier: MilliporeSigma

A potent, cell-permeable, and irreversible inhibitor of caspase-1 (ICE) and caspase-4.

Supplier: Bioss

Binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction. Promotes Arg-Gly-Asp-dependent cell attachment.

Supplier: Bioss

DPP6 is a Type-II serine proteinase of the clan SC. The clan SC proteinases have a catalytic triad of Ser-Asp-His, and like other Serine proteinases, the active site serine is in a Gly-Xaa-Ser-Xaa -Gly orientation. DPP6 has an Asp instead of Ser in the catalytic site. DPP6 is a member of a broader family of dipeptidyl peptidases including DPP4, FAP/Seprase, DPP2, DPP8, DPP9, DPP10, which have differing substrate specificity and tissue localizations. The surface-bound DPP6 is a homodimer, and cleavage of in the stalk region releases a shed form of DPP6. The shed is the form found in serum. DPP6 has been found in highest abundance in the brain, but also in the kidney, liver and lung.

Supplier: Bioss

DPP6 is a Type-II serine proteinase of the clan SC. The clan SC proteinases have a catalytic triad of Ser-Asp-His, and like other Serine proteinases, the active site serine is in a Gly-Xaa-Ser-Xaa -Gly orientation. DPP6 has an Asp instead of Ser in the catalytic site. DPP6 is a member of a broader family of dipeptidyl peptidases including DPP4, FAP/Seprase, DPP2, DPP8, DPP9, DPP10, which have differing substrate specificity and tissue localizations. The surface-bound DPP6 is a homodimer, and cleavage of in the stalk region releases a shed form of DPP6. The shed is the form found in serum. DPP6 has been found in highest abundance in the brain, but also in the kidney, liver and lung.

Supplier: Bachem Americas

Substrates often used for characterizing newly isolated PPIases, subtilisins or other enzymes. Bachem offers Suc-Ala-Ala-Pro-Xaa (Suc-AAPX) substrates containing Ala, Leu, Met, Nle, and Nva (the pancreatic elastase substrates L-1775, L-1390, L-1395, and L-1780), Arg, Asp, Glu, Ile, Lys, Orn, Phe (the PPIase substrates I-1465, L-1400, and M-2305), and Val (the neutrophil elastase substrates I-1490 and L-1770) as Xaa.

Supplier: Bioss

DPP6 is a Type-II serine proteinase of the clan SC. The clan SC proteinases have a catalytic triad of Ser-Asp-His, and like other Serine proteinases, the active site serine is in a Gly-Xaa-Ser-Xaa -Gly orientation. DPP6 has an Asp instead of Ser in the catalytic site. DPP6 is a member of a broader family of dipeptidyl peptidases including DPP4, FAP/Seprase, DPP2, DPP8, DPP9, DPP10, which have differing substrate specificity and tissue localizations. The surface-bound DPP6 is a homodimer, and cleavage of in the stalk region releases a shed form of DPP6. The shed is the form found in serum. DPP6 has been found in highest abundance in the brain, but also in the kidney, liver and lung.

Supplier: Bachem Americas

This dipeptide has a sweetening power which is 180 to 200 times that of sucrose.

Supplier: Bioss

Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10. May participate in the GZMB apoptotic pathways. Cleaves ADPRT. Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-|-AMC. Likely target for the cowpox virus CRMA death inhibitory protein. Isoform 5, isoform 6, isoform 7 and isoform 8 lack the catalytic site and may interfere with the pro-apoptotic activity of the complex.

Supplier: Bachem Americas

Ac-ED(edans)KPILFFRLGK(dabcyl)E-amide, a sensitive fluorescent (FRET) peptide substrate for cathepsin D. This enzyme can degrade extracellular matrix components and may facilitate the spread of tumor cells. High levels of active cathepsin D were found within senile plaques in brains of Alzheimer's patients.

Supplier: Bachem Americas

The Italian mutation of β-amyloid 1-40 (E22K) aggregates more rapidly than the wild-type sequence 1-40. It showed increased neurotoxicity, which (according to a solid-phase NMR-study of Masuda et al.) may be due to the salt bridge formed between Lys²² and Asp²³ in the minor conformer. As the Arctic, Flemish, and Dutch mutants, the Italian mutant is degraded considerably more slowly than wild-type Aβ by neprilysin.

Supplier: Prosci

WDR12 is a member of the WD repeat protein family. WD repeats are minimally conserved regions of approximately 40 amino acids typically bracketed by gly-his and trp-asp (GH-WD), which may facilitate formation of heterotrimeric or multiprotein complexes. Members of this family are involved in a variety of cellular processes, including cell cycle progression, signal transduction, apoptosis, and gene regulation. The function of this protein is not known.This gene encodes a member of the WD repeat protein family. WD repeats are minimally conserved regions of approximately 40 amino acids typically bracketed by gly-his and trp-asp (GH-WD), which may facilitate formation of heterotrimeric or multiprotein complexes. Members of this family are involved in a variety of cellular processes, including cell cycle progression, signal transduction, apoptosis, and gene regulation. This protein is highly similar to the mouse WD repeat domain 12 protein at the amino acid level. The function of this protein is not known.

Supplier: Genetex

Goat Polyclonal antibody to DHX58

Supplier: Prosci

WDR33 is a member of the WD repeat protein family. WD repeats are minimally conserved regions of approximately 40 amino acids typically bracketed by gly-his and trp-asp (GH-WD), which may facilitate formation of heterotrimeric or multiprotein complexes. Members of this family are involved in a variety of cellular processes, including cell cycle progression, signal transduction, apoptosis, and gene regulation. This gene is highly expressed in testis and the protein is localized to the nucleus. This gene may play important roles in the mechanisms of cytodifferentiation and/or DNA recombination.This gene encodes a member of the WD repeat protein family. WD repeats are minimally conserved regions of approximately 40 amino acids typically bracketed by gly-his and trp-asp (GH-WD), which may facilitate formation of heterotrimeric or multiprotein complexes. Members of this family are involved in a variety of cellular processes, including cell cycle progression, signal transduction, apoptosis, and gene regulation. This gene is highly expressed in testis and the protein is localized to the nucleus. This gene may play important roles in the mechanisms of cytodifferentiation and/or DNA recombination. Multiple alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.

Supplier: Prosci

DDX3 Antibody: DDX3 contains all of the motifs of the DEAD-box family of RNA helicases, including the Asp-Glu-Ala-Asp sequence that gives the protein family its name and distinguishes it from other RNA helicases. DDX3 is localized to the X chromosome and has a highly conserved functional homolog (DBY) on the Y chromosome. DDX3 is thought to be involved in RNA splicing, RNA transport, and translation initiation. It has also been shown to be involved in cell growth control and is deregulated in hepatitis virus-associated hepatocellular carcinoma. Recent experiments suppressing DDX3 expression blocked HIV-1 RNA export from the nucleus, suggesting that DDX3 functions as a shuttling protein that transports the HIV-1 protein Rev and its cofactor CRM1 from the nucleus to the cytoplasm.

Supplier: Bioss

Binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction. Promotes Arg-Gly-Asp-dependent cell attachment.

Supplier: Bioss

DCTN6 belongs to the pointed end complex of the dynactin shoulder complex tpgether with the DCTN4, DCTN5 and DCTN6 subunits and ACTR10. DCTN6 contains an RGD (Arg-Gly-Asp) motif in the N terminal region, which confers adhesive properties to macromolecular proteins like fibronectin. The exact function of this gene is not known.

Supplier: Bioss

Binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction. Promotes Arg-Gly-Asp-dependent cell attachment.

Supplier: Bachem Americas

Also known as dioxopiperazines, piperazine-2,5-diones or DKPs. Diketopiperazines may occur as by-products during peptide synthesis or during the degradation of peptides. These cyclic dipeptides have been detected as taste-modulating compounds in food, they often show biological activity. DKPs are valuable chiral synthons, employed e.g. in Schöllkopf's versatile bislactim ether approach. They also have found use as catalysts for enantioselective synthesis, e.g. in the asymmetric Strecker reaction. See also the TRH metabolite cyclo(-His-Pro), G-1745, and cyclo(-Asp-Phe), G-1695, the major degradation product of aspartame.

Supplier: Bioss

Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP1. May participate in the GZMB apoptotic pathways. Cleaves ADPRT. Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-|-AMC. Likely target for the cowpox virus CRMA death inhibitory protein.

Supplier: Bioss

Endoplasmic reticulum Marker. The sequence Lys-Asp-Glu-Leu (KDEL) or a closely related sequence, is present at the carboxy-terminus of soluble endoplasmic reticulum (ER) resident proteins and some membrane proteins. 78 and 94 kDa glucose regulated proteins (GRP 78) and GRP 94 respectively and protein disulfide isomerase (PDI) all share the C-terminal KDEL sequence. 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

The bioactive tetrapeptide goralatide which corresponds to the N-terminus of Thymosin β₄, is a physiological regulator of hematopoiesis and inhibits the entry into the S-phase of murine and human hematopoietic stem cells. Ac-SDKP has been shown to reduce the damage to specific compartments in the bone marrow resulting from treatment with chemotherapeutic agents, ionizing radiations, hyperthermy, or phototherapy. It protects from doxorubicin-induced toxicity. Ac-SDKP is a physiological substrate of angiotensin I- converting enzyme (ACE).

Supplier: Genetex

Rabbit polyclonal antibody to DHX35 (N-terminal)