You Searched For: S-Trityl-D-cysteine

Catalog Number: (BOSSBS-11277R-A750)

Supplier: Bioss

Description: DnaJ-like proteins interact with HSP 70 molecular chaperones and function to facilitate protein folding and mitochondrial protein import. HSP 40-4, also known as HDJ2, is the human DnaJ homolog that functions as a co-chaperone with a cysteine-rich zinc finger domain. The cellular redox enzyme thioredoxin interacts with HSP 40-4, and oxidation and reduction reversibly regulate HSP 40-4 function in response to the changing redox states of the cell. The zinc finger domain of HSP 40-4 may act as a redox sensor of chaperone-mediated protein-folding machinery, since HSP 40-4 inactivation leads to the oxidation of cysteine thiols and a simultaneous release of coordinated zinc. Loss of the HSP 40-4 protein may be linked to severe defects in spermatogenesis that involve aberrant androgen Signalling.

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Catalog Number: (BOSSBS-11175R-HRP)

Supplier: Bioss

Description: Lubricin, also designated proteoglycan-4 or megakaryocyte stimulating factor, is important for boundary lubrication within articulating joints. It is a disulfide-linked homodimer (between Cysteine 1146 and Cysteine 1403) that is essential for protein cleavage. Lubricin inhibits synovial cell adhesion to the cartilage surface, but also prevents the deposition of proteins from synovial fluid onto cartilage. Lubricin is highly expressed in cartilage, liver and synovial tissue. Defects in the gene encoding for lubricin can cause Jakobs syndrome, also designated camptodactyly-arthropathy-coxa vara-pericarditis syndrome (CACP). CACP is an autosomal recessive disorder characterized by joint failure associated with noninflammatory synoviocyte hyperplasia and subinitimal fibrosis of the synovial capsule. Lubricin undergoes different levels of glycosylation and may be detected at varying molecular weights.

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Catalog Number: (BOSSBS-3873R-CY5)

Supplier: Bioss

Description: ATG4A is a cysteine protease required for autophagy, which cleaves the C-terminal part of either MAP1LC3, GABARAPL2 or GABARAP, allowing the liberation of form I. A subpopulation of form I is subsequently converted to a smaller form (form II). Form II, with a revealed C-terminal glycine, is considered to be the phosphatidylethanolamine (PE)-conjugated form, and has the capacity for the binding to autophagosomes.

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Catalog Number: (BOSSBS-3873R-CY5.5)

Supplier: Bioss

Description: ATG4A is a cysteine protease required for autophagy, which cleaves the C-terminal part of either MAP1LC3, GABARAPL2 or GABARAP, allowing the liberation of form I. A subpopulation of form I is subsequently converted to a smaller form (form II). Form II, with a revealed C-terminal glycine, is considered to be the phosphatidylethanolamine (PE)-conjugated form, and has the capacity for the binding to autophagosomes.

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Catalog Number: (BOSSBS-3873R-CY3)

Supplier: Bioss

Description: ATG4A is a cysteine protease required for autophagy, which cleaves the C-terminal part of either MAP1LC3, GABARAPL2 or GABARAP, allowing the liberation of form I. A subpopulation of form I is subsequently converted to a smaller form (form II). Form II, with a revealed C-terminal glycine, is considered to be the phosphatidylethanolamine (PE)-conjugated form, and has the capacity for the binding to autophagosomes.

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Catalog Number: (BOSSBS-5720R)

Supplier: Bioss

Description: GDF10, or growth differentiation factor 10, bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. GDF10 is expressed in femur, brain, lung, skeletal muscle, pancreas and testis.

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Catalog Number: (BOSSBS-12947R)

Supplier: Bioss

Description: CRP2BP is a 782 amino acid protein encoded by the human gene CSRP2BP. CRP2BP specifically interacts with the double LIM domain protein CRP2. The LIM domain is a conserved cysteine and histidine-containing structural module of two tandemly arranged zinc fingers. It has been identified in single or multiple copies in a variety of regulatory proteins, either in combination with defined functional domains, like homeodomains, or alone, like in the CRP family of LIM proteins. Members of the cysteine- and glycine-rich protein family (CRP1, CRP2 and CRP3) contain two zinc-binding LIM domains, LIM1 (amino-terminal) and LIM2 (carboxyl-terminal), and are implicated in diverse cellular processes linked to differentiation, growth control and pathogenesis. Although present in cytoplasm, CRP2BP is mainly a ubiquitously expressed nuclear protein, with highest expression in skeletal muscle and heart.

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Catalog Number: (BOSSBS-12947R-A680)

Supplier: Bioss

Description: CRP2BP is a 782 amino acid protein encoded by the human gene CSRP2BP. CRP2BP specifically interacts with the double LIM domain protein CRP2. The LIM domain is a conserved cysteine and histidine-containing structural module of two tandemly arranged zinc fingers. It has been identified in single or multiple copies in a variety of regulatory proteins, either in combination with defined functional domains, like homeodomains, or alone, like in the CRP family of LIM proteins. Members of the cysteine- and glycine-rich protein family (CRP1, CRP2 and CRP3) contain two zinc-binding LIM domains, LIM1 (amino-terminal) and LIM2 (carboxyl-terminal), and are implicated in diverse cellular processes linked to differentiation, growth control and pathogenesis. Although present in cytoplasm, CRP2BP is mainly a ubiquitously expressed nuclear protein, with highest expression in skeletal muscle and heart.

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Catalog Number: (BOSSBS-12947R-A750)

Supplier: Bioss

Description: CRP2BP is a 782 amino acid protein encoded by the human gene CSRP2BP. CRP2BP specifically interacts with the double LIM domain protein CRP2. The LIM domain is a conserved cysteine and histidine-containing structural module of two tandemly arranged zinc fingers. It has been identified in single or multiple copies in a variety of regulatory proteins, either in combination with defined functional domains, like homeodomains, or alone, like in the CRP family of LIM proteins. Members of the cysteine- and glycine-rich protein family (CRP1, CRP2 and CRP3) contain two zinc-binding LIM domains, LIM1 (amino-terminal) and LIM2 (carboxyl-terminal), and are implicated in diverse cellular processes linked to differentiation, growth control and pathogenesis. Although present in cytoplasm, CRP2BP is mainly a ubiquitously expressed nuclear protein, with highest expression in skeletal muscle and heart.

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Catalog Number: (BOSSBS-12945R-CY7)

Supplier: Bioss

Description: Cysteine string proteins (CSPs) are synaptic vesicle-associated, secretory vesicle proteins that are involved in Ca2+-regulated exocytosis of synaptic vesicles and modulation of presynaptic transmembrane calcium fluxes in neuroendocrine and endocrine cell types. CSP contains a J-domain that binds HSP 70/HSC 70 chaperone ATPases and a membrane-targeting, palmitoylated cysteine-rich string region. CSPs may act as molecular chaperones in synapses, and mediate conformational folding of components of the vesicular exocytotic machinery. CSP is involved in the fine tuning of neurotransmission through its interaction with receptor-coupled trimeric GTP binding proteins (G proteins) and N-type Ca2+ channels. Two variants of CSP have been described: CSP1; and the 31 amino acid, C-terminally truncated isoform, CSP2. Subcellular fractionation of insulinoma cells shows CSP1 in granular fractions, while the membrane and cytosol fractions contain predominantly CSP2. The fractions also contain additional proteins, presumably CSP dimers. Furthermore, in various mammalian cell lines (including rat brain) CSP1 expression predominates CSP2 expression.

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Catalog Number: (BOSSBS-6236R-CY5)

Supplier: Bioss

Description: This gene encodes one of several deubiquitylating enzymes. Ubiquitin modification of proteins is needed for their stability and function; to reverse the process, deubiquityling enzymes remove ubiquitin. This protein contains an OTU domain and binds Ubal (ubiquitin aldehyde); an active cysteine protease site is present in the OTU domain.

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Catalog Number: (BOSSBS-1351R-CY5.5)

Supplier: Bioss

Description: This enzyme is necessary for target cell lysis in cell-mediated immune responses. It cleaves after Asp. Seems to be linked to an activation cascade of caspases (aspartate-specific cysteine proteases) responsible for apoptosis execution. Cleaves caspase-3, -7, -9 and 10 to give rise to active enzymes mediating apoptosis.

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Catalog Number: (BOSSBS-8329R-A680)

Supplier: Bioss

Description: Contributes to oxidative stress resistance by reducing cysteine-sulfinic acid formed under exposure to oxidants in the peroxiredoxins PRDX1, PRDX2, PRDX3 and PRDX4. Does not act on PRDX5 or PRDX6. May catalyze the reduction in a multi-step process by acting both as a specific phosphotransferase and a thioltransferase.

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Catalog Number: (BOSSBS-8329R-A647)

Supplier: Bioss

Description: Contributes to oxidative stress resistance by reducing cysteine-sulfinic acid formed under exposure to oxidants in the peroxiredoxins PRDX1, PRDX2, PRDX3 and PRDX4. Does not act on PRDX5 or PRDX6. May catalyze the reduction in a multi-step process by acting both as a specific phosphotransferase and a thioltransferase.

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Catalog Number: (BOSSBS-8329R-A488)

Supplier: Bioss

Description: Contributes to oxidative stress resistance by reducing cysteine-sulfinic acid formed under exposure to oxidants in the peroxiredoxins PRDX1, PRDX2, PRDX3 and PRDX4. Does not act on PRDX5 or PRDX6. May catalyze the reduction in a multi-step process by acting both as a specific phosphotransferase and a thioltransferase.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-6236R-A680)

Supplier: Bioss

Description: This gene encodes one of several deubiquitylating enzymes. Ubiquitin modification of proteins is needed for their stability and function; to reverse the process, deubiquityling enzymes remove ubiquitin. This protein contains an OTU domain and binds Ubal (ubiquitin aldehyde); an active cysteine protease site is present in the OTU domain.

UOM: 1 * 100 µl

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