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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
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-CY7
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-A647
UOM: 1 * 100 µl
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.
Numéro de catalogue: BOSSBS-9174R-CY5.5
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-A680
UOM: 1 * 100 µl
Fournisseur: Bioss


Description: Disposable cartilage knife with Sheffield stainless steel double honed blade and molded handle with finger guard.
Numéro de catalogue: 720-0015
UOM: 1 * 10 ST
Fournisseur: CELLPATH


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-A555
UOM: 1 * 100 µl
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.
Numéro de catalogue: BOSSBS-9174R-CY3
UOM: 1 * 100 µl
Fournisseur: Bioss


Description: TRIM35 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. TRIM35 may play a role as a tumor suppressor, and is implicated in the cell death mechanism. 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. The function of this protein has not been identified.
Numéro de catalogue: PRSI25-205
UOM: 1 * 50 µG
Fournisseur: ProSci Inc.


Description: TRIM38 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 function of this protein has not been identified.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. The function of this protein has not been identified.
Numéro de catalogue: PRSI28-943
UOM: 1 * 1 EA
Fournisseur: ProSci Inc.


Description: The carbon steel trimming blades are special blades for cutting tissue samples without causing deformations. The trimming blade handles are made from heat-resistant plastic and due to their ergonomic design, they are particularly easy to grip.
Numéro de catalogue: FEAT205500001
UOM: 1 * 50 ST
Fournisseur: PFM Medical GmbH


Description: TRIM8 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 nuclear bodies. Its structure is similar to some tumor suppressor proteins and its gene maps to a locus thought to contain tumor suppressor genes.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 nuclear bodies. Its structure is similar to some tumor suppressor proteins and its gene maps to a locus thought to contain tumor suppressor genes.
Numéro de catalogue: PRSI25-540
UOM: 1 * 50 µG
Fournisseur: ProSci Inc.


Description: TRIM31 encodes for 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 both the cytoplasm and the nucleus. 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. The protein localizes to both the cytoplasm and the nucleus. Its function has not been identified.
Numéro de catalogue: PRSI27-116
UOM: 1 * 50 µG
Fournisseur: ProSci Inc.


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-FITC
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-A488
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-A555
UOM: 1 * 100 µl
Fournisseur: Bioss


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