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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: (PRSI56-968)

Fournisseur: ProSci Inc.

Description: The protein encoded by this gene 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. This protein localizes to the nucleus and the cytoplasm. Its function has not been identified. [provided by RefSeq].

UOM: 1 * 400 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-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-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

Promotion

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: (PRSI28-206)

Fournisseur: ProSci Inc.

Description: The protein encoded by TRIM9 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 cytoplasmic bodies. Its function has not been identified.

UOM: 1 * 50 µG

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Numéro de catalogue: (PRSI28-121)

Fournisseur: ProSci Inc.

Description: TRIM17 encodes a protein that 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 cytoplasmic bodies. The protein is expressed at high levels in the testis, but its function is unknown.

UOM: 1 * 50 µG

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Numéro de catalogue: (PRSI7383)

Fournisseur: ProSci Inc.

Description: TRIM24 Antibody: TRIM24 (TIF1), a member of the tripartite motif (TRIM) family, plays a role in the regulation of cell proliferation and apoptosis. TRIM24 localizes to nuclear bodies and is thought to associate with chromatin and heterochromatin-associated factors. The TRIM motif includes three zinc-binding domains (RING, B-box type 1 and B-box type 2) and a coiled-coil region. TIF1 mediates transcriptional events by interactions with the AF2 region of several nuclear receptors, such as the estrogen, retinoic acid and vitamin D3 receptors. Defects in TRIM24 are a cause of thyroid papillary carcinoma (TPC).

UOM: 1 * 1 EA

Promotion

Numéro de catalogue: (PRSI28-179)

Fournisseur: ProSci Inc.

Description: The protein encoded byTRIM14 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 cytoplasmic bodies and its function has not been determined. Four alternatively spliced transcript variants for this gene have been described.

UOM: 1 * 50 µG

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Numéro de catalogue: (PRSI92-074)

Fournisseur: ProSci Inc.

Description: T-Cell Receptor-Associated Transmembrane Adapter 1 (TRAT1) is a single-pass type III membrane protein. TRAT1 exists as a disulfide-linked homodimer and is strongly expressed in the thymus, and to a lesser extent in the spleen, lymph node, and peripheral blood lymphocytes. TRAT1 is phosphorylated on tyrosines by LCK or FYN upon TCR activation. Its function is to stabilizes the TCR (T-cell antigen receptor)/CD3 complex at the surface of T-cells.

UOM: 1 * 50 µG

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

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

Promotion

Numéro de catalogue: (PRSI31-262)

Fournisseur: ProSci Inc.

Description: TRIM23 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. This protein is also a member of the ADP ribosylation factor family of guanine nucleotide-binding family of proteins. Its carboxy terminus contains an ADP-ribosylation factor domain and a guanine nucleotide binding site, while the amino terminus contains a GTPase activating protein domain which acts on the guanine nucleotide binding site. The protein localizes to lysosomes and the Golgi apparatus. It plays a role in the formation of intracellular transport vesicles, their movement from one compartment to another, and phopholipase D activation. Three alternatively spliced transcript variants for this gene have been described. The protein encoded by this gene 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. This protein is also a member of the ADP ribosylation factor family of guanine nucleotide-binding family of proteins. Its carboxy terminus contains an ADP-ribosylation factor domain and a guanine nucleotide binding site, while the amino terminus contains a GTPase activating protein domain which acts on the guanine nucleotide binding site. The protein localizes to lysosomes and the Golgi apparatus. It plays a role in the formation of intracellular transport vesicles, their movement from one compartment to another, and phopholipase D activation. Three alternatively spliced transcript variants for this gene have been described.

UOM: 1 * 50 µG

Promotion

Numéro de catalogue: (PRSI56-155)

Fournisseur: ProSci Inc.

Description: The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1, a B-box type 2, and a coiled-coil region. The protein localizes to both the nucleus and the cytoplasm, and may represent a participant in the initiation of glycogen synthesis. Multiple transcript variants have been found for this gene, and some of them encode the same isoform. [provided by RefSeq].

UOM: 1 * 400 µl

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