You Searched For: 2-Benzyl-N-boc-L-proline

Catalog Number: (BOSSBS-6351R-A680)

Supplier: Bioss

Description: his gene encodes a basic, proline-rich, 15-kD protein. The protein acts as a positive mediator of programmed cell death that is induced by interferon-gamma.

UOM: 1 * 100 µl

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Supplier: Apollo Scientific

Description: (2S,4S)-Methyl-4-fluoropyrrolidine-2-carboxylate hydrochloride

Supplier: Sartorius

Description: High quality pipettes with new, innovative design and technology, combining safety, ergonomics, efficiency in pipetting, with easy calibration and maintenance. They include built-in replaceable tip cone filters, which prevent pipette contamination and damage.

Catalog Number: (BOSSBS-1873R-CY5.5)

Supplier: Bioss

Description: Cleaves C-terminal amino acids linked to proline in peptides such as angiotensin II, III and des-Arg9-bradykinin. This cleavage occurs at acidic pH, but enzymatic activity is retained with some substrates at neutral pH.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-1873R-CY5)

Supplier: Bioss

Description: Cleaves C-terminal amino acids linked to proline in peptides such as angiotensin II, III and des-Arg9-bradykinin. This cleavage occurs at acidic pH, but enzymatic activity is retained with some substrates at neutral pH.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-7619R)

Supplier: Bioss

Description: This gene encodes a proline rich protein. Studies of the related mouse gene suggest that this gene is regulated by p53 and may participate in p53 mediated growth suppression. Alternatively spliced transcript variants encoding different isoforms have been described.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-1873R-A647)

Supplier: Bioss

Description: Cleaves C-terminal amino acids linked to proline in peptides such as angiotensin II, III and des-Arg9-bradykinin. This cleavage occurs at acidic pH, but enzymatic activity is retained with some substrates at neutral pH.

UOM: 1 * 100 µl

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Supplier: Sartorius

Description: Ergonomic pipettes with fast, easy operation. Selected models offer changeable tip cone filters to prevent liquids and aerosols entering the pipette.

Catalog Number: (BOSSBS-7619R-A350)

Supplier: Bioss

Description: This gene encodes a proline rich protein. Studies of the related mouse gene suggest that this gene is regulated by p53 and may participate in p53 mediated growth suppression. Alternatively spliced transcript variants encoding different isoforms have been described.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-5912R-FITC)

Supplier: Bioss

Description: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

UOM: 1 * 100 µl

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Catalog Number: (ENZOALX210898R100)

Supplier: ENZO LIFE SCIENCES

Description: VASP (vasodilator stimulated phosphoprotein) is a proline-rich protein substrate of cAMP- and cGMP-dependent protein kinases. Phosphorylation of VASP at Ser-157 causes a mobility shift in SDS gel electrophoresis from 46 to 50 kDa, which has been used as a convenient marker to monitor cyclic nucleotide-dependent protein kinase activity. VASP is the founding member of the Ena-VASP protein family, comprising the Drosophila protein Enabled (Ena), its mouse homologue Mena (mammalian Enabled), and mouse EVL (Ena-VASP-like protein). With these proteins VASP shares a conserved overall domain organization:
a) the conserved N-terminal Ena-VASP homology domain 1 (EVH1), which mediates binding to a proline-rich motif
b) a more divergent proline-rich central domain (which is responsible for profilin binding)
c) a conserved C-terminal EVH2 domain.

VASP is expressed in a variety of mammalian cell types and tissues. In cultured cells, VASP is associated with focal adhesions, cell-cell contacts, microfilaments, and highly dynamic membrane regions. From in vitro binding data VASP has been suggested to link profilin to zyxin, vinculin, and the Listeria spp. surface protein ActA, respectively. Functional evidence indicates that VASP is a crucial factor involved in the enhancement of actin filament formation and the actin-dependent motility of intracellular bacterial pathogens.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-12676R-A555)

Supplier: Bioss

Description: Complete remission of acute promyelocytic leukemia can be achieved by treating patients with retinoic acid, and PML-RAR-a (promyelocytic leukemia-retinoic acid receptor alpha fusion protein) plays a major role in mediating retinoic acid effects in leukemia cells. The retinoic acid-induced gene, PRAM-1 (PML-RAR-a target gene encoding an adaptor molecule 1) encodes an adaptor protein which is expressed and modulated during normal human myelopoiesis. PRAM-1 expression is hindered by expression of PML-RAR-a. The 718 amino acid PRAM-1 protein contains eight N-terminal proline-rich repeats and several proline residues that are clustered as type I or type II SH3 recognition motifs. PRAM-1 demonstrates expression in hematopoietic tissues and lung.

UOM: 1 * 100 µl

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Catalog Number: (ENZOALX804177C050)

Supplier: ENZO LIFE SCIENCES

Description: VASP (vasodilator stimulated phosphoprotein) is a proline-rich protein substrate of cAMP- and cGMP-dependent protein kinases. Phosphorylation of VASP at Ser-157 causes a mobility shift in SDS gel electrophoresis from 46 to 50 kDa, which has been used as a convenient marker to monitor cyclic nucleotide-dependent protein kinase activity. VASP is the founding member of the Ena-VASP protein family, comprising the Drosophila protein Enabled (Ena), its mouse homologue Mena (mammalian Enabled), and mouse EVL (Ena-VASP-like protein). With these proteins VASP shares a conserved overall domain organization:
a) the conserved N-terminal Ena-VASP homology domain 1 (EVH1), which mediates binding to a proline-rich motif,
b) a more divergent proline-rich central domain (which is responsible for profilin binding), and
c) a conserved C-terminal EVH2 domain.

Particularly high VASP levels are present in platelets, although VASP is expressed in a wide variety of cell types and tissues. In cultured cells, VASP is associated with focal adhesions, cell-cell contacts, microfilaments, and highly dynamic membrane regions. From in vitro binding data VASP has been suggested to link profilin to zyxin, vinculin, and the Listeria spp. surface protein ActA, respectively. Functional evidence indicates that VASP is a crucial factor involved in the enhancement of actin filament formation and the actin-dependent motility of intracellular bacterial pathogens.

UOM: 1 * 50 µG

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Catalog Number: (BOSSBS-3620R)

Supplier: Bioss

Description: Focal adhesions are actin-rich structures that enable cells to adhere to the extracellular matrix and at which protein complexes involved in signal transduction assemble. Zyxin is a zinc-binding phosphoprotein that concentrates at focal adhesions and along the actin cytoskeleton. Zyxin has an N-terminal proline-rich domain and three LIM domains in its C-terminal half. The proline-rich domain may interact with SH3 domains of proteins involved in signal transduction pathways while the LIM domains are likely involved in protein-protein binding. Zyxin may function as a messenger in the signal transduction pathway that mediates adhesion-stimulated changes in gene expression and may modulate the cytoskeletal organization of actin bundles. Alternative splicing results in multiple transcript variants that encode the same isoform. [provided by RefSeq, Jul 2008].

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-7632R-FITC)

Supplier: Bioss

Description: This gene encodes a mitochondrial protein that is characterized by a poly-proline rich region. A chicken homolog of this protein promotes mitochondrial fission and the mouse homolog protects cells from oxidative stress. A related pseudogene of this gene is found on chromosome X.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-7619R-CY5.5)

Supplier: Bioss

Description: This gene encodes a proline rich protein. Studies of the related mouse gene suggest that this gene is regulated by p53 and may participate in p53 mediated growth suppression. Alternatively spliced transcript variants encoding different isoforms have been described.

UOM: 1 * 100 µl

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