Votre recherche pour: 1,2,3-Trim\u00E9thoxybenz\u00E8ne

Numéro de catalogue: (BOSSBS-9380R-CY3)

Fournisseur: Bioss

Description: Midline-1 (Tripartite motif-containing protein 18, Putative transcription factor XPRF, RING finger protein 59) is a 667 amino acid protein encoded by the human gene MID1. Midline-1 belongs to the TRIM/RBCC family and contains two B box-type zinc fingers, one B30.2/SPRY domain, one COS domain, one fibronectin type-III domain and one RING-type zinc finger. Midline-1 is believed to have E3 ubiquitin ligase activity which targets the catalytic subunit of protein phosphatase 2 for degradation. It is a cytoplasmic protein found as a homodimer or heterodimer with Midline-2. It also interacts with IGBP1 (Lymphocyte signaling protein A4). Defects in MID1 are the cause of Opitz syndrome type I (OS-I). OS-I is an X-linked recessive disorder characterized by hypertelorism, genital-urinary defects such as hypospadias in males and splayed labia in females, lip-palate-laryngotracheal clefts, imperforate anus, developmental delay and congenital heart defects. OS-I mutations produce proteins with a decreased affinity for microtubules.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-9380R-A488)

Fournisseur: Bioss

Description: Midline-1 (Tripartite motif-containing protein 18, Putative transcription factor XPRF, RING finger protein 59) is a 667 amino acid protein encoded by the human gene MID1. Midline-1 belongs to the TRIM/RBCC family and contains two B box-type zinc fingers, one B30.2/SPRY domain, one COS domain, one fibronectin type-III domain and one RING-type zinc finger. Midline-1 is believed to have E3 ubiquitin ligase activity which targets the catalytic subunit of protein phosphatase 2 for degradation. It is a cytoplasmic protein found as a homodimer or heterodimer with Midline-2. It also interacts with IGBP1 (Lymphocyte signaling protein A4). Defects in MID1 are the cause of Opitz syndrome type I (OS-I). OS-I is an X-linked recessive disorder characterized by hypertelorism, genital-urinary defects such as hypospadias in males and splayed labia in females, lip-palate-laryngotracheal clefts, imperforate anus, developmental delay and congenital heart defects. OS-I mutations produce proteins with a decreased affinity for microtubules.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-9238R-HRP)

Fournisseur: Bioss

Description: The RING-type zinc finger motif is present in a number of viral and eukaryotic proteins and is made of a conserved cysteine-rich domain that is able to bind two zinc atoms. Proteins that contain this conserved domain are generally involved in the ubiquitination pathway of protein degradation. RNF23 (RING finger protein 23), also known as tripartite motif-containing protein 39 (TRIM39) or testis-abundant finger protein, is a 518 amino acid protein belonging to the TRIM/RBCC family that is known to interact with MOAP1. Ubiquitously expressed and existing as two alternatively spliced isoforms, RNF23 is found at highest levels in spleen, testis, brain, kidney, liver, heart and skeletal muscle. RNF23 typically localizes to cytosol but shifts to mitochondria upon co-localization with MOAP1, a short-lived, pro-apoptotic protein which RNF23 prevents from becoming poly-ubiquitinated and degraded, thereby facilitating apoptosis. RNF23 contains one B box-type zinc finger, a B30.2/SPRY domain and a single RING-type zinc finger.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-9380R-CY5.5)

Fournisseur: Bioss

Description: Midline-1 (Tripartite motif-containing protein 18, Putative transcription factor XPRF, RING finger protein 59) is a 667 amino acid protein encoded by the human gene MID1. Midline-1 belongs to the TRIM/RBCC family and contains two B box-type zinc fingers, one B30.2/SPRY domain, one COS domain, one fibronectin type-III domain and one RING-type zinc finger. Midline-1 is believed to have E3 ubiquitin ligase activity which targets the catalytic subunit of protein phosphatase 2 for degradation. It is a cytoplasmic protein found as a homodimer or heterodimer with Midline-2. It also interacts with IGBP1 (Lymphocyte signaling protein A4). Defects in MID1 are the cause of Opitz syndrome type I (OS-I). OS-I is an X-linked recessive disorder characterized by hypertelorism, genital-urinary defects such as hypospadias in males and splayed labia in females, lip-palate-laryngotracheal clefts, imperforate anus, developmental delay and congenital heart defects. OS-I mutations produce proteins with a decreased affinity for microtubules.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-9380R-A750)

Fournisseur: Bioss

Description: Midline-1 (Tripartite motif-containing protein 18, Putative transcription factor XPRF, RING finger protein 59) is a 667 amino acid protein encoded by the human gene MID1. Midline-1 belongs to the TRIM/RBCC family and contains two B box-type zinc fingers, one B30.2/SPRY domain, one COS domain, one fibronectin type-III domain and one RING-type zinc finger. Midline-1 is believed to have E3 ubiquitin ligase activity which targets the catalytic subunit of protein phosphatase 2 for degradation. It is a cytoplasmic protein found as a homodimer or heterodimer with Midline-2. It also interacts with IGBP1 (Lymphocyte signaling protein A4). Defects in MID1 are the cause of Opitz syndrome type I (OS-I). OS-I is an X-linked recessive disorder characterised by hypertelorism, genital-urinary defects such as hypospadias in males and splayed labia in females, lip-palate-laryngotracheal clefts, imperforate anus, developmental delay and congenital heart defects. OS-I mutations produce proteins with a decreased affinity for microtubules.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-9238R-A555)

Fournisseur: Bioss

Description: The RING-type zinc finger motif is present in a number of viral and eukaryotic proteins and is made of a conserved cysteine-rich domain that is able to bind two zinc atoms. Proteins that contain this conserved domain are generally involved in the ubiquitination pathway of protein degradation. RNF23 (RING finger protein 23), also known as tripartite motif-containing protein 39 (TRIM39) or testis-abundant finger protein, is a 518 amino acid protein belonging to the TRIM/RBCC family that is known to interact with MOAP1. Ubiquitously expressed and existing as two alternatively spliced isoforms, RNF23 is found at highest levels in spleen, testis, brain, kidney, liver, heart and skeletal muscle. RNF23 typically localizes to cytosol but shifts to mitochondria upon co-localization with MOAP1, a short-lived, pro-apoptotic protein which RNF23 prevents from becoming poly-ubiquitinated and degraded, thereby facilitating apoptosis. RNF23 contains one B box-type zinc finger, a B30.2/SPRY domain and a single RING-type zinc finger.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-9238R-CY7)

Fournisseur: Bioss

Description: The RING-type zinc finger motif is present in a number of viral and eukaryotic proteins and is made of a conserved cysteine-rich domain that is able to bind two zinc atoms. Proteins that contain this conserved domain are generally involved in the ubiquitination pathway of protein degradation. RNF23 (RING finger protein 23), also known as tripartite motif-containing protein 39 (TRIM39) or testis-abundant finger protein, is a 518 amino acid protein belonging to the TRIM/RBCC family that is known to interact with MOAP1. Ubiquitously expressed and existing as two alternatively spliced isoforms, RNF23 is found at highest levels in spleen, testis, brain, kidney, liver, heart and skeletal muscle. RNF23 typically localizes to cytosol but shifts to mitochondria upon co-localization with MOAP1, a short-lived, pro-apoptotic protein which RNF23 prevents from becoming poly-ubiquitinated and degraded, thereby facilitating apoptosis. RNF23 contains one B box-type zinc finger, a B30.2/SPRY domain and a single RING-type zinc finger.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-9238R-A750)

Fournisseur: Bioss

Description: The RING-type zinc finger motif is present in a number of viral and eukaryotic proteins and is made of a conserved cysteine-rich domain that is able to bind two zinc atoms. Proteins that contain this conserved domain are generally involved in the ubiquitination pathway of protein degradation. RNF23 (RING finger protein 23), also known as tripartite motif-containing protein 39 (TRIM39) or testis-abundant finger protein, is a 518 amino acid protein belonging to the TRIM/RBCC family that is known to interact with MOAP1. Ubiquitously expressed and existing as two alternatively spliced isoforms, RNF23 is found at highest levels in spleen, testis, brain, kidney, liver, heart and skeletal muscle. RNF23 typically localises to cytosol but shifts to mitochondria upon co-localisation with MOAP1, a short-lived, pro-apoptotic protein which RNF23 prevents from becoming poly-ubiquitinated and degraded, thereby facilitating apoptosis. RNF23 contains one B box-type zinc finger, a B30.2/SPRY domain and a single RING-type zinc finger.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-9238R)

Fournisseur: Bioss

Description: The RING-type zinc finger motif is present in a number of viral and eukaryotic proteins and is made of a conserved cysteine-rich domain that is able to bind two zinc atoms. Proteins that contain this conserved domain are generally involved in the ubiquitination pathway of protein degradation. RNF23 (RING finger protein 23), also known as tripartite motif-containing protein 39 (TRIM39) or testis-abundant finger protein, is a 518 amino acid protein belonging to the TRIM/RBCC family that is known to interact with MOAP1. Ubiquitously expressed and existing as two alternatively spliced isoforms, RNF23 is found at highest levels in spleen, testis, brain, kidney, liver, heart and skeletal muscle. RNF23 typically localizes to cytosol but shifts to mitochondria upon co-localization with MOAP1, a short-lived, pro-apoptotic protein which RNF23 prevents from becoming poly-ubiquitinated and degraded, thereby facilitating apoptosis. RNF23 contains one B box-type zinc finger, a B30.2/SPRY domain and a single RING-type zinc finger.

UOM: 1 * 100 µl

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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

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Numéro de catalogue: (ABNOMAB4526)

Fournisseur: Abnova

Description: Mouse monoclonal antibody raised against partial recombinant TRAT1.

UOM: 1 * 1 EA

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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

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Numéro de catalogue: (BOSSBS-9155R-A750)

Fournisseur: Bioss

Description: TRIM36 (tripartite motif-containing 36), also known as RNF98 (RING finger protein 98), HAPRIN (haploid germ cell-specific RBCC protein) or RBCC728, is a 728 amino acid protein that belongs to the TRIM/RBCC (Ring finger, B box, coiled-coil) family. Predominantly expressed in prostate, testis and brain with weak expression in heart, kidney and lung, TRIM36 contains two B box-type zinc fingers, a SPRY domain, a coiled-coil domain, a fibronectin type-III domain and a RING-type zinc finger; a motif that has zinc-chelating activity and is involved in mediating protein-protein and protein-DNA interactions. Localising to the cytoplasm and the acrosomal region of germ cells and mature sperm, TRIM36 is believed to play a role in the acrosome reaction and fertilisation. In addition, TRIM36 is overexpressed in prostate cancer, suggesting a possible role for TRIM36 in prostate tumorigenesis.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-9174R-FITC)

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

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Numéro de catalogue: (BOSSBS-9380R-A647)

Fournisseur: Bioss

Description: Midline-1 (Tripartite motif-containing protein 18, Putative transcription factor XPRF, RING finger protein 59) is a 667 amino acid protein encoded by the human gene MID1. Midline-1 belongs to the TRIM/RBCC family and contains two B box-type zinc fingers, one B30.2/SPRY domain, one COS domain, one fibronectin type-III domain and one RING-type zinc finger. Midline-1 is believed to have E3 ubiquitin ligase activity which targets the catalytic subunit of protein phosphatase 2 for degradation. It is a cytoplasmic protein found as a homodimer or heterodimer with Midline-2. It also interacts with IGBP1 (Lymphocyte signaling protein A4). Defects in MID1 are the cause of Opitz syndrome type I (OS-I). OS-I is an X-linked recessive disorder characterized by hypertelorism, genital-urinary defects such as hypospadias in males and splayed labia in females, lip-palate-laryngotracheal clefts, imperforate anus, developmental delay and congenital heart defects. OS-I mutations produce proteins with a decreased affinity for microtubules.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-9238R-FITC)

Fournisseur: Bioss

Description: The RING-type zinc finger motif is present in a number of viral and eukaryotic proteins and is made of a conserved cysteine-rich domain that is able to bind two zinc atoms. Proteins that contain this conserved domain are generally involved in the ubiquitination pathway of protein degradation. RNF23 (RING finger protein 23), also known as tripartite motif-containing protein 39 (TRIM39) or testis-abundant finger protein, is a 518 amino acid protein belonging to the TRIM/RBCC family that is known to interact with MOAP1. Ubiquitously expressed and existing as two alternatively spliced isoforms, RNF23 is found at highest levels in spleen, testis, brain, kidney, liver, heart and skeletal muscle. RNF23 typically localizes to cytosol but shifts to mitochondria upon co-localization with MOAP1, a short-lived, pro-apoptotic protein which RNF23 prevents from becoming poly-ubiquitinated and degraded, thereby facilitating apoptosis. RNF23 contains one B box-type zinc finger, a B30.2/SPRY domain and a single RING-type zinc finger.

UOM: 1 * 100 µl

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