You Searched For: S-Benzyl-L-cysteine

Catalog Number: (BOSSBS-12947R-FITC)

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.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-6039R-A680)

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 the kininogens. The type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in a variety of human fluids and secretions. Expression of the protein has been observed in various human cancer cell lines established from malignant tumors.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-6039R-CY5.5)

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 the kininogens. The type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in a variety of human fluids and secretions. Expression of the protein has been observed in various human cancer cell lines established from malignant tumors.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-0156R-A350)

Supplier: Bioss

Description: Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In the brain and peripheral nervous system, NO displays many properties of a neurotransmitter. Probably has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such SRR.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-8329R-CY3)

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-9217R-HRP)

Supplier: Bioss

Description: The cystatin superfamily is a well-established family of cysteine protease inhibitors. All true cystatins inhibit cysteine peptidases of the papain family, such as cathepsins, while some also inhibit legumain family enzymes. The CRES (cystatin-related epididymal spermatogenic) protein defines a new subgroup in the family 2 cystatins of the cystatin superfamily. CRES proteins lack two of the three consensus sites necessary for the cystatin inhibition of C1 cysteine proteases. Due to their expression patterns, it is likely that CRES proteins may perform unique and tissue-specific functions in the reproductive and neuroendocrine systems. As a member of the CRES subfamily, Cystatin 9, also designated CLM, is a 159 amino acid protein that is expressed in heart, placenta, lung, liver, skeletal muscle and pancreas. Cystatin 9 is thought to play a role in hematopoietic differentiation or inflammation. It has also been shown to be upregulated by LPS in some cancer cell lines, such as promyelocytic leukemia (HL-60) and myelomonocytic leukemia.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11177R-HRP)

Supplier: Bioss

Description: Cysteine-rich secretory proteins (CRISPs) represent a family of evolutionarily conserved proteins which play a role in the innate immune system and are transcriptionally regulated by androgens in several tissues. CRISP-8 (Cysteine-rich secretory protein 8), also known as PI15 (Peptidase inhibitor 15), P25TI or SugarCrisp, is a 258 amino acid secreted protein that belongs to the CRISP family. Expressed at low levels in thyroid, prostate, salivary and mammary tissue, CRISP-8 functions as a serine protease inhibitor that exhibits weak inhibitory action against Trypsin, a serine protease found in the digestive system. In addition to its role as a protease inhibitor, CRISP-8 is secreted in neuroblastoma and glioblastoma cell lines, suggesting a role for CRISP-8 in tumor formation and metastasis within the central nervous system.

UOM: 1 * 100 µl

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Catalog Number: (ENZOADIAAM114E)

Supplier: ENZO LIFE SCIENCES

Description: The caspases are a family of cysteine proteases that cleave after certain aspartate residues, and are primarily recognized as mediators of apoptosis.

UOM: 1 * 100 µG

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Catalog Number: (786-793)

Supplier: G-Biosciences

Description: Ficin (or Ficain) is a cysteine protease enzyme (EC 3.4.22.3) isolated from fig latex is that has the endopeptidase activity to cleave Immunoglobulin G (IgG) molecules in the hinge region.

UOM: 1 * 5 mL

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Catalog Number: (BOSSBS-11277R-CY5)

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 signaling.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11277R-CY3)

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 signaling.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-6039R-A647)

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 the kininogens. The type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in a variety of human fluids and secretions. Expression of the protein has been observed in various human cancer cell lines established from malignant tumors.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-0156R-A750)

Supplier: Bioss

Description: Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In the brain and peripheral nervous system, NO displays many properties of a neurotransmitter. Probably has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such SRR.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-0156R-A647)

Supplier: Bioss

Description: Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In the brain and peripheral nervous system, NO displays many properties of a neurotransmitter. Probably has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such SRR.

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-8329R-CY7)

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-3595R-HRP)

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 the kininogens. The type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in a variety of human fluids and secretions, where they appear to provide protective functions. The cystatin locus on chromosome 20 contains the majority of the type 2 cystatin genes and pseudogenes. This gene is located in the cystatin locus and encodes the most abundant extracellular inhibitor of cysteine proteases, which is found in high concentrations in biological fluids and is expressed in virtually all organs of the body. A mutation in this gene has been associated with amyloid angiopathy. Expression of this protein in vascular wall smooth muscle cells is severely reduced in both atherosclerotic and aneurysmal aortic lesions, establishing its role in vascular disease. [provided by RefSeq].

UOM: 1 * 100 µl

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