You Searched For: S-Benzyl-L-cysteine


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Catalog Number: (BOSSBS-0156R-FITC)
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


Catalog Number: (BOSSBS-0156R-A488)
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


Catalog Number: (BOSSBS-6236R)
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


Catalog Number: (ENZOENZ60001C001)
Supplier: ENZO LIFE SCIENCES
Description: Wnt expression and signal transduction have been identified as critical components in regulating embryogenesis, cell proliferation, and bone, glucose and lipid metabolism. Wnt-3a signalling also plays a role in regulating the differentation of stem cells. Wnt-3a is a member of the highly conserved, structurally related cysteine-rich Wnt family glycoproteins important for normal developmental processes and oncogenesis.
UOM: 1 * 1 µG

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Catalog Number: (ENZOALX522027C050)
Supplier: ENZO LIFE SCIENCES
Description: Produced in HEK 293 cells. The cysteine-rich region of human CD30 (Ki-1) (aa 1-380) is fused to the Fc portion of human IgG1 .
UOM: 1 * 50 µG

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Catalog Number: (BOSSBS-11175R-A555)
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.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11277R-A647)
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


Catalog Number: (BOSSBS-11277R-FITC)
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


Catalog Number: (BOSSBS-11175R-A350)
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.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12947R-A350)
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


Catalog Number: (BOSSBS-12936R-FITC)
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. They are also preferentially expressed in postmeiotic germ cells, the proximal caput epididymidis, and anterior pituitary gonadotrophs. Therefore, CRES proteins may perform unique and tissue-specific functions in the reproductive and neuroendocrine systems. As a member of the CRES subfamily, Cystatin-like 1 (CSTL1) is a 145 amino acid protein and is expressed in testis.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-1328R-FITC)
Supplier: Bioss
Description: Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-9218R-A488)
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. 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 a type 2 salivary cysteine peptidase inhibitor. The protein is an S-type cystatin, based on its high level of expression in saliva, tears and seminal plasma. The specific role in these fluids is unclear but antibacterial and antiviral activity is present, consistent with a protective function. [provided by RefSeq, Jul2008].
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-9216R)
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. They are also preferentially expressed in postmeiotic germ cells, the proximal caput epididymidis, and anterior pituitary gonadotrophs. Therefore, CRES proteins may perform unique and tissue-specific functions in the reproductive and neuroendocrine systems. As a member of the CRES subfamily, Cystatin 8 is a 142 amino acid protein that is expressed in the proximal caput region of the epididymis, where it performs a specialized role during sperm development and maturation.
UOM: 1 * 100 µl


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


Catalog Number: (BOSSBS-6701R-CY5)
Supplier: Bioss
Description: Specific inhibition of calpain (calcium-dependent cysteine protease). Plays a key role in postmortem tenderization of meat and have been proposed to be involved in muscle protein degradation in living tissue.
UOM: 1 * 100 µl


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