You Searched For: N-Acetyl-S-trityl-L-cysteine

Catalog Number: (10109-770)

Supplier: Prosci

Description: CHIC2 is a member of the CHIC family of proteins. This protein contains a cysteine-rich hydrophobic (CHIC) motif, and is localized to vesicular structures and the plasma membrane. CHIC2 gene is associated with some cases of acute myeloid leukemia.This gene encodes a member of the CHIC family of proteins. The encoded protein contains a cysteine-rich hydrophobic (CHIC) motif, and is localized to vesicular structures and the plasma membrane. This gene is associated with some cases of acute myeloid leukemia.

Catalog Number: (10072-964)

Supplier: Prosci

Description: CXCL16 is a member of the CXC chemokine family and signals through the CXCR6 receptor. CXCL16 may play a role in attracting lymphocyte subsets during inflammation and may facilitate certain immune responses. The chemokine domain of CXCL16 contains six cysteine residues including the four highly conserved cysteine residues characteristic of CXC chemokines. The CXCL16 gene codes for a 273 amino acid polypeptide, which includes a 29 amino acid cytoplasmic domain and transmembrane sequence containing approximately 20 amino acids. The extracellular portion of CXCL16 contains a chemokines domain and an extended C-terminal ?mucin-like stalk? sequence. The extracellular domain contains 89 amino acid residues (86 a.a. residues for the murine homolog). Recombinant murine CXCL16 is a 9.9 kDa protein containing 88 amino acid residues.

Catalog Number: (10349-408)

Supplier: Bioss

Description: Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide, cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. Isoform 3 seems to be inactive.

Catalog Number: (76083-154)

Supplier: Bioss

Description: Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide, cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. Isoform 3 seems to be inactive.

Catalog Number: (10483-340)

Supplier: Bioss

Description: Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes (UBE1s), ubiquitin-conjugating enzymes (UBE2s), and ubiquitin-protein ligases (UBE3s). When ubiquitin is activated by a UBE1, it is transferred to the cysteine residue on a UBE2. UBE2 then binds a UBE3, which transfers the ubiquitin from the UBE2 cysteine to a lysine residue on the target protein. Ubiquitin-conjugating enzyme E2 Q1 (UBE2Q1), also known as ubiquitin-protein ligase Q1 or ubiquitin carrier protein Q1, is an 422 amino acid protein belonging to the ubiquitin-conjugating enzyme (UBE2) family. Two named isoforms of UBE2Q1 exist as a result of alternative splicing events.

Catalog Number: (10408-764)

Supplier: Bioss

Description: The cystatin superfamily encompasses proteins that contain multiple cystatin-like sequences. Some of the members are active cysteine protease inhibitors, while others have lost or perhaps never acquired this inhibitory activity. There are three inhibitory families in the superfamily, including the type 1 cystatins (stefins), type 2 cystatins, and kininogens. This gene encodes a stefin that functions as a cysteine protease inhibitor, forming tight complexes with papain and the cathepsins B, H, and L. The protein is one of the precursor proteins of cornified cell envelope in keratinocytes and plays a role in epidermal development and maintenance. Stefins have been proposed as prognostic and diagnostic tools for cancer. [provided by RefSeq, Jul 2008]

Supplier: AFG Bioscience

Description: 2-Acetamido-3,4,6-tri-O-acetyl-2-deoxy-β-D-glucopyranosyl azide 97%

Catalog Number: (10751-500)

Supplier: Prosci

Description: SIVA Antibody: SIVA plays an important role in the apoptotic pathway induced by the CD27 antigen, a member of the tumor necrosis factor receptor (TFNR) superfamily. SIVA is a small cysteine-rich protein with a unique N-terminal amphipathic helical region, a death domain homology region (DDHR) and a C-terminal cysteine-rich B-box-like or zinc-finger-like structure. The DDHR domain binds to CD27 and induces apoptosis in T cells through a caspase-dependent mitochondrial pathway. SIVA inhibits BCL2L1 isoform Bcl-xL anti-apoptotic activity and inhibits activation of NFkappa -B and promotes T-cell receptor-mediated apoptosis. SIVA represents a potential therapeutic target for the treatment of neuronal cell death diseases.

Catalog Number: (103006-424)

Supplier: Anaspec Inc

Description: This peptide corresponds to the protein transduction domain of the TAT protein and is synthesized with an activated cysteine residue C(Npys), wherein Npys is 3-Nitro-2-pyridinesulfenyl group and is used for activating S of cysteine and for rapid reaction when a thiol group is introduced. This is synthesized with C(Npys) at the N-terminus for applications requiring specific conjugation reactions and has a fluorophore labeled with FAM having Abs/Em=494/518 nm. This kind of modification has been used to render this peptide as a cell penetrating and carrier peptide applicable in conjugation studies.
Sequence: C(Npys)YGRKKRRQRRR-K(FAM)-NH2
MW: 2302.7 Da
% Peak area by HPLC: 95
Storage condition: -20°C

Catalog Number: (RL600-403-B07)

Supplier: Rockland Immunochemical

Description: 100ug. Polyclonal. Immunogen: synthetic peptide corresponding to a region near the carboxy terminal end of human NAG-1 protein. A residue of cysteine was added to facilitate coupling to KLH. Reactivity: human, mouse

Supplier: AFG Bioscience

Description: 1,3,4-tri-O-Acetyl-2-azido-2,6-dideoxy-L-talose ≥95%

Catalog Number: (76083-152)

Supplier: Bioss

Description: Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide, cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. Isoform 3 seems to be inactive.

Catalog Number: (10349-402)

Supplier: Bioss

Description: Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide, cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. Isoform 3 seems to be inactive.

Catalog Number: (10408-758)

Supplier: Bioss

Description: The cystatin superfamily encompasses proteins that contain multiple cystatin-like sequences. Some of the members are active cysteine protease inhibitors, while others have lost or perhaps never acquired this inhibitory activity. There are three inhibitory families in the superfamily, including the type 1 cystatins (stefins), type 2 cystatins, and kininogens. This gene encodes a stefin that functions as a cysteine protease inhibitor, forming tight complexes with papain and the cathepsins B, H, and L. The protein is one of the precursor proteins of cornified cell envelope in keratinocytes and plays a role in epidermal development and maintenance. Stefins have been proposed as prognostic and diagnostic tools for cancer. [provided by RefSeq, Jul 2008]

Catalog Number: (TCA1526-005G)

Supplier: TCI America

Description: CAS Number: 2832-10-2
MDL Number: MFCD00009211
Molecular Formula: C10H16O4
Molecular Weight: 200.23
Purity/Analysis Method: >96.0% (GC)
Form: Clear Liquid
Boiling point (°C): 182
Flash Point (°C): 110
Specific Gravity (20/20): 1.07

SDS

Catalog Number: (CA95057-556)

Supplier: G-Biosciences

Description: Trypsin is a serine endopeptidase that specifically cleaves peptide bonds on the carboxy side of s-aminoethyl cysteine, arginine and lysine residues

SDS Certificates