Imprimer

Votre recherche pour: 1,2,4-Trim\\u00E9thoxybenz\\u00E8ne


4 388  les résultats ont été trouvés

SearchResultCount:"4388"

Sort Results

Vue liste Vue simple

Évaluez le résultat de cette recherche

Numéro de catalogue: (BOSSBS-9174R-A555)
Fournisseur: Bioss
Description: Tripartite motif-containing protein 3 (TRIM3), also known as RING finger protein 22 (RNF22), RING finger protein 97 (RNF97) or brain-expressed RING finger protein (BERP), is a 744 amino acid member of the TRIM family, also known as the RING-B-box coiled-coil (RBCC) family. Members of the RBCC family have an N-terminal RING finger, followed by one or two zinc-binding domains (B-box domains), a leucine coiled-coil region and a variable C-terminal domain. Localized to cytoplasmic filaments, TRIM3 has been shown to interact with å-actinin-4 and myosin V, two proteins associated with the actin cytoskeleton. Specifically, å-actinin-4 interacts with the RBCC domain of TRIM3, and the C-terminal tail of Myosin V interacts with with the unique C-terminal ∫-propeller domain of TRIM3. These associations suggest that TRIM3 may play a role in cell motility and cargo transport. Three named isoforms of TRIM3 exist as a result of alternative splicing events.
UOM: 1 * 100 µl


Numéro de catalogue: (BOSSBS-9174R-A647)
Fournisseur: Bioss
Description: Tripartite motif-containing protein 3 (TRIM3), also known as RING finger protein 22 (RNF22), RING finger protein 97 (RNF97) or brain-expressed RING finger protein (BERP), is a 744 amino acid member of the TRIM family, also known as the RING-B-box coiled-coil (RBCC) family. Members of the RBCC family have an N-terminal RING finger, followed by one or two zinc-binding domains (B-box domains), a leucine coiled-coil region and a variable C-terminal domain. Localized to cytoplasmic filaments, TRIM3 has been shown to interact with å-actinin-4 and myosin V, two proteins associated with the actin cytoskeleton. Specifically, å-actinin-4 interacts with the RBCC domain of TRIM3, and the C-terminal tail of Myosin V interacts with with the unique C-terminal ∫-propeller domain of TRIM3. These associations suggest that TRIM3 may play a role in cell motility and cargo transport. Three named isoforms of TRIM3 exist as a result of alternative splicing events.
UOM: 1 * 100 µl


Numéro de catalogue: (BOSSBS-9174R-A350)
Fournisseur: Bioss
Description: Tripartite motif-containing protein 3 (TRIM3), also known as RING finger protein 22 (RNF22), RING finger protein 97 (RNF97) or brain-expressed RING finger protein (BERP), is a 744 amino acid member of the TRIM family, also known as the RING-B-box coiled-coil (RBCC) family. Members of the RBCC family have an N-terminal RING finger, followed by one or two zinc-binding domains (B-box domains), a leucine coiled-coil region and a variable C-terminal domain. Localized to cytoplasmic filaments, TRIM3 has been shown to interact with å-actinin-4 and myosin V, two proteins associated with the actin cytoskeleton. Specifically, å-actinin-4 interacts with the RBCC domain of TRIM3, and the C-terminal tail of Myosin V interacts with with the unique C-terminal ∫-propeller domain of TRIM3. These associations suggest that TRIM3 may play a role in cell motility and cargo transport. Three named isoforms of TRIM3 exist as a result of alternative splicing events.
UOM: 1 * 100 µl


Numéro de catalogue: (BOSSBS-9174R)
Fournisseur: Bioss
Description: Tripartite motif-containing protein 3 (TRIM3), also known as RING finger protein 22 (RNF22), RING finger protein 97 (RNF97) or brain-expressed RING finger protein (BERP), is a 744 amino acid member of the TRIM family, also known as the RING-B-box coiled-coil (RBCC) family. Members of the RBCC family have an N-terminal RING finger, followed by one or two zinc-binding domains (B-box domains), a leucine coiled-coil region and a variable C-terminal domain. Localized to cytoplasmic filaments, TRIM3 has been shown to interact with å-actinin-4 and myosin V, two proteins associated with the actin cytoskeleton. Specifically, å-actinin-4 interacts with the RBCC domain of TRIM3, and the C-terminal tail of Myosin V interacts with with the unique C-terminal ∫-propeller domain of TRIM3. These associations suggest that TRIM3 may play a role in cell motility and cargo transport. Three named isoforms of TRIM3 exist as a result of alternative splicing events.
UOM: 1 * 100 µl


Numéro de catalogue: (PRSI28-155)
Fournisseur: ProSci Inc.
Description: TRIM15 is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The protein localizes to the cytoplasm. Its function has not been identified.
UOM: 1 * 1 EA


Fournisseur: PFM Medical GmbH
Description: These trimming blades in conjunction with the handle F-1326P allow fast and easy blade change thus providing users with increased safety and comfort in their daily laboratory work. With back metal, blade can be attached/detached without touching blade directly.

Numéro de catalogue: (PRSI29-868)
Fournisseur: ProSci Inc.
Description: TRIM42 is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, namely a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region.This gene encodes a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, namely a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region.
UOM: 1 * 50 µG


Numéro de catalogue: (PRSI28-827)
Fournisseur: ProSci Inc.
Description: TRIM21 is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. TRIM21 is part of the RoSSA ribonucleoprotein, which includes a single polypeptide and one of four small RNA molecules. The RoSSA particle localizes to both the cytoplasm and the nucleus. RoSSA interacts with autoantigens in patients with Sjogren syndrome and systemic lupus erythematosus.This gene encodes a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The encoded protein is part of the RoSSA ribonucleoprotein, which includes a single polypeptide and one of four small RNA molecules. The RoSSA particle localizes to both the cytoplasm and the nucleus. RoSSA interacts with autoantigens in patients with Sjogren syndrome and systemic lupus erythematosus. Alternatively spliced transcript variants for this gene have been described but the full-length nature of only one has been determined. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.
UOM: 1 * 1 EA


Numéro de catalogue: (PRSI4745)
Fournisseur: ProSci Inc.
Description: TRIM30 Antibody: TRIM30 belongs to a family of the tripartite motif (TRIM) proteins involved in the regulation of cell proliferation, differentiation, development, oncogenesis, apoptosis and antiviral responses. The TRIM protein family is an expanding family of RING ('really interesting new gene') proteins, also known as RBCC proteins as they contain an RBCC motif, which comprises a RING domain, one or two B-boxes and a predicted coiled-coil region. Studies have shown that some TRIM family members are critical to innate immunity; TRIM5, TRIM19 and TRIM25, for example, have been shown to restrict viral infection. A recent study shows that TRIM30 functions as a negative modulator of the TLR signaling pathway, by targeting TAB2 and TAB3, and contributes to the inhibition of TLR-mediated NF-kappa B activation. The importance of TRIM30 in the attenuation or termination of NF-kappa B activation suggests that targeting of TAB2 and TAB3 by TRIM30 alpha may be a mechanism for modulating many types of immune responses.
UOM: 1 * 1 EA


Numéro de catalogue: (BOSSBS-9244R-FITC)
Fournisseur: Bioss
Description: Tripartite motif-containing protein 34 (TRIM34), also known as RING finger protein 21 (RNF21) or interferon-responsive finger protein 1 (IFP1), is a 488 amino acid member of the TRIM family, also known as the RING-B-box coiled-coil (RBCC) family. Members of the RBCC family have an N-terminal RING finger, followed by one or two zinc-binding domains (B-box domains), a leucine coiled-coil region and a variable C-terminal domain. Three isoforms of TRIM34 exist as a result of alternative splicing events. Isoform 1, the most abundant isoform, is highly expressed in placenta, spleen, colon and peripheral blood leukocytes. Studies have shown that Interferon (IFN) stimulation leads to an upregulation of TRIM34. These findings suggest that TRIM34 maybe a downstream effector that mediates IFN activities.
UOM: 1 * 100 µl


Numéro de catalogue: (BOSSBS-9244R-A488)
Fournisseur: Bioss
Description: Tripartite motif-containing protein 34 (TRIM34), also known as RING finger protein 21 (RNF21) or interferon-responsive finger protein 1 (IFP1), is a 488 amino acid member of the TRIM family, also known as the RING-B-box coiled-coil (RBCC) family. Members of the RBCC family have an N-terminal RING finger, followed by one or two zinc-binding domains (B-box domains), a leucine coiled-coil region and a variable C-terminal domain. Three isoforms of TRIM34 exist as a result of alternative splicing events. Isoform 1, the most abundant isoform, is highly expressed in placenta, spleen, colon and peripheral blood leukocytes. Studies have shown that Interferon (IFN) stimulation leads to an upregulation of TRIM34. These findings suggest that TRIM34 maybe a downstream effector that mediates IFN activities.
UOM: 1 * 100 µl


Numéro de catalogue: (BOSSBS-9244R-A555)
Fournisseur: Bioss
Description: Tripartite motif-containing protein 34 (TRIM34), also known as RING finger protein 21 (RNF21) or interferon-responsive finger protein 1 (IFP1), is a 488 amino acid member of the TRIM family, also known as the RING-B-box coiled-coil (RBCC) family. Members of the RBCC family have an N-terminal RING finger, followed by one or two zinc-binding domains (B-box domains), a leucine coiled-coil region and a variable C-terminal domain. Three isoforms of TRIM34 exist as a result of alternative splicing events. Isoform 1, the most abundant isoform, is highly expressed in placenta, spleen, colon and peripheral blood leukocytes. Studies have shown that Interferon (IFN) stimulation leads to an upregulation of TRIM34. These findings suggest that TRIM34 maybe a downstream effector that mediates IFN activities.
UOM: 1 * 100 µl


Numéro de catalogue: (BOSSBS-13389R-FITC)
Fournisseur: Bioss
Description: Trimming of glucoses from N-linked core glycans on newly synthesized glycoproteins occurs sequentially through the action of Glucosidases I and II in the endoplasmic reticulum (ER). Glucosidase II is an ER-localized enzyme that contains a and b subunits (Glucosidase IIa and Glucosidase IIb) which form a defined heterodimeric complex. Glucosidase IIa is the catalyitc core of the enzyme and can function independently of the b subunit. The sequence of Glucosidase IIb encodes protein rich in glutamic and aspartic acid with a putative ER retention signal (HDEL) at the C-terminus. The phosphorylated form of Glucosidase IIb is localized in the plasma membrane and is highly expressed in FGF-stimulated fibroblasts and epidermal carcinoma cells. Glucosidase IIb was first purified from a human carcinoma cell line as a potential substrate for protein kinase C. Through the HDEL signal at the C-terminus, Glucosidase IIb retains the complete complex in the ER.
UOM: 1 * 100 µl


Numéro de catalogue: (BOSSBS-13389R-A750)
Fournisseur: Bioss
Description: Trimming of glucoses from N-linked core glycans on newly synthesized glycoproteins occurs sequentially through the action of Glucosidases I and II in the endoplasmic reticulum (ER). Glucosidase II is an ER-localized enzyme that contains a and b subunits (Glucosidase IIa and Glucosidase IIb) which form a defined heterodimeric complex. Glucosidase IIa is the catalyitc core of the enzyme and can function independently of the b subunit. The sequence of Glucosidase IIb encodes protein rich in glutamic and aspartic acid with a putative ER retention signal (HDEL) at the C-terminus. The phosphorylated form of Glucosidase IIb is localized in the plasma membrane and is highly expressed in FGF-stimulated fibroblasts and epidermal carcinoma cells. Glucosidase IIb was first purified from a human carcinoma cell line as a potential substrate for protein kinase C. Through the HDEL signal at the C-terminus, Glucosidase IIb retains the complete complex in the ER.
UOM: 1 * 100 µl


Numéro de catalogue: (BOSSBS-9244R-CY3)
Fournisseur: Bioss
Description: Tripartite motif-containing protein 34 (TRIM34), also known as RING finger protein 21 (RNF21) or interferon-responsive finger protein 1 (IFP1), is a 488 amino acid member of the TRIM family, also known as the RING-B-box coiled-coil (RBCC) family. Members of the RBCC family have an N-terminal RING finger, followed by one or two zinc-binding domains (B-box domains), a leucine coiled-coil region and a variable C-terminal domain. Three isoforms of TRIM34 exist as a result of alternative splicing events. Isoform 1, the most abundant isoform, is highly expressed in placenta, spleen, colon and peripheral blood leukocytes. Studies have shown that Interferon (IFN) stimulation leads to an upregulation of TRIM34. These findings suggest that TRIM34 maybe a downstream effector that mediates IFN activities.
UOM: 1 * 100 µl


Numéro de catalogue: (BOSSBS-9244R-CY5.5)
Fournisseur: Bioss
Description: Tripartite motif-containing protein 34 (TRIM34), also known as RING finger protein 21 (RNF21) or interferon-responsive finger protein 1 (IFP1), is a 488 amino acid member of the TRIM family, also known as the RING-B-box coiled-coil (RBCC) family. Members of the RBCC family have an N-terminal RING finger, followed by one or two zinc-binding domains (B-box domains), a leucine coiled-coil region and a variable C-terminal domain. Three isoforms of TRIM34 exist as a result of alternative splicing events. Isoform 1, the most abundant isoform, is highly expressed in placenta, spleen, colon and peripheral blood leukocytes. Studies have shown that Interferon (IFN) stimulation leads to an upregulation of TRIM34. These findings suggest that TRIM34 maybe a downstream effector that mediates IFN activities.
UOM: 1 * 100 µl


Appel de prix
Le stock de cet article est limité mais peut être disponible dans un entrepôt proche de vous. Merci de vous assurer que vous êtes connecté sur le site afin que le stock disponible soit affiché. Si l'call est toujours affiché et vous avez besoin d'aide, s'il vous plaît appelez-nous au 016 385 011
Le stock de cet article est limité mais peut être disponible dans un entrepôt proche de vous. Merci de vous assurer que vous êtes connecté sur le site afin que le stock disponible soit affiché. Si l'call est toujours affiché et vous avez besoin d'aide, s'il vous plaît appelez-nous au 016 385 011
Ces articles ne peuvent être ajoutés au Panier. Veuillez contacter votre service client ou envoyer un e-mail à vwr.be@vwr.com
Une documentation supplémentaire peut être nécessaire pour l'achat de cet article. Un représentant de VWR vous contactera si nécessaire.
Ce produit a été bloqué par votre organisation. Contacter votre service d'achat pour plus d'informations.
Le produit original n'est plus disponible. Le remplacement représenté est disponible
Les produits marqués de ce symbole ne seront bientôt plus disponibles - vente jusqu'à épuisement de stock. Des alternatives peuvent être disponibles en recherchant le code article VWR indiqué ci-dessus. Si vous avez besoin d'une assistance supplémentaire, veuillez contacter notre Service Clientèle au 016 385 011.
305 - 320 of 4 388
no targeter for Bottom