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Description: The cassette trimming system CTS 500 is used to remove excess paraffin from the outside edges of the cassettes after processing and embedding. This simplifies and speeds up the preparation of tissue blocks in the histology laboratory.
Numéro de catalogue: 632-0061
UOM: 1 * 1 ST
Fournisseur: PFM Medical GmbH


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.
Numéro de catalogue: BOSSBS-13389R-CY5
UOM: 1 * 100 µl
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.
Numéro de catalogue: BOSSBS-13389R-A647
UOM: 1 * 100 µl
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. Localizing 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 fertilization. In addition, TRIM36 is overexpressed in prostate cancer, suggesting a possible role for TRIM36 in prostate tumorigenesis.
Numéro de catalogue: BOSSBS-9155R
UOM: 1 * 100 µl
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.
Numéro de catalogue: BOSSBS-13389R-CY7
UOM: 1 * 100 µl
Fournisseur: Bioss


Description: Midline-2 is a 715 amino acid protein encoded by the human gene MID2. Midline-2 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-2 is a cytoplasmic protein found as a homodimer or heterodimer with Midline-1. It also interacts with IGBP1 (Lymphocyte signaling protein A4). Dimerization is mediated by the tripartite motif (RBCC; RING- and B box-type zinc fingers and coiled coil domains) and microtubule association is dependent on the C-terminal B30.2 domain. Midline-2 is expressed at low levels in fetal kidney and lung, and in adult prostate, ovary and small intestine.
Numéro de catalogue: BOSSBS-11029R-CY3
UOM: 1 * 100 µl
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.
Numéro de catalogue: BOSSBS-9244R-A750
UOM: 1 * 100 µl
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. Localizing 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 fertilization. In addition, TRIM36 is overexpressed in prostate cancer, suggesting a possible role for TRIM36 in prostate tumorigenesis.
Numéro de catalogue: BOSSBS-9155R-CY3
UOM: 1 * 100 µl
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.
Numéro de catalogue: BOSSBS-13389R-A488
UOM: 1 * 100 µl
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.
Numéro de catalogue: BOSSBS-13389R-HRP
UOM: 1 * 100 µl
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.
Numéro de catalogue: BOSSBS-13389R-A680
UOM: 1 * 100 µl
Fournisseur: Bioss


Description: Midline-2 is a 715 amino acid protein encoded by the human gene MID2. Midline-2 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-2 is a cytoplasmic protein found as a homodimer or heterodimer with Midline-1. It also interacts with IGBP1 (Lymphocyte signaling protein A4). Dimerization is mediated by the tripartite motif (RBCC; RING- and B box-type zinc fingers and coiled coil domains) and microtubule association is dependent on the C-terminal B30.2 domain. Midline-2 is expressed at low levels in fetal kidney and lung, and in adult prostate, ovary and small intestine.
Numéro de catalogue: BOSSBS-11029R-FITC
UOM: 1 * 100 µl
Fournisseur: Bioss


Description: Anti-TRIM Mouse Monoclonal Antibody [clone: TRIM-04]
Numéro de catalogue: ANTIA86682-100
UOM: 1 * 1 EA
Fournisseur: ANTIBODIES.COM

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Description: Midline-2 is a 715 amino acid protein encoded by the human gene MID2. Midline-2 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-2 is a cytoplasmic protein found as a homodimer or heterodimer with Midline-1. It also interacts with IGBP1 (Lymphocyte signaling protein A4). Dimerization is mediated by the tripartite motif (RBCC; RING- and B box-type zinc fingers and coiled coil domains) and microtubule association is dependent on the C-terminal B30.2 domain. Midline-2 is expressed at low levels in fetal kidney and lung, and in adult prostate, ovary and small intestine.
Numéro de catalogue: BOSSBS-11029R-A488
UOM: 1 * 100 µl
Fournisseur: Bioss


Description: Midline-2 is a 715 amino acid protein encoded by the human gene MID2. Midline-2 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-2 is a cytoplasmic protein found as a homodimer or heterodimer with Midline-1. It also interacts with IGBP1 (Lymphocyte signaling protein A4). Dimerization is mediated by the tripartite motif (RBCC; RING- and B box-type zinc fingers and coiled coil domains) and microtubule association is dependent on the C-terminal B30.2 domain. Midline-2 is expressed at low levels in fetal kidney and lung, and in adult prostate, ovary and small intestine.
Numéro de catalogue: BOSSBS-11029R-A555
UOM: 1 * 100 µl
Fournisseur: Bioss


Description: Midline-2 is a 715 amino acid protein encoded by the human gene MID2. Midline-2 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-2 is a cytoplasmic protein found as a homodimer or heterodimer with Midline-1. It also interacts with IGBP1 (Lymphocyte signaling protein A4). Dimerization is mediated by the tripartite motif (RBCC; RING- and B box-type zinc fingers and coiled coil domains) and microtubule association is dependent on the C-terminal B30.2 domain. Midline-2 is expressed at low levels in fetal kidney and lung, and in adult prostate, ovary and small intestine.
Numéro de catalogue: BOSSBS-11029R-CY7
UOM: 1 * 100 µl
Fournisseur: Bioss


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