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Artikel-Nr: (BOSSBS-3051R-CY3)
Lieferant: Bioss
Beschreibung: Deubiquitinating enzyme that plays a key role in chromatin by mediating deubiquitination of histone H2A and HCFC1. Catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1). Does not deubiquitinate monoubiquitinated histone H2B. Acts as a regulator of cell growth by mediating deubiquitination of HCFC1 N-terminal and C-terminal chains, with some specificity toward 'Lys-48'-linked polyubiquitin chains compared to 'Lys-63'-linked polyubiquitin chains. Deubiquitination of HCFC1 does not lead to increase stability of HCFC1. Interferes with the BRCA1 and BARD1 heterodimer activity by inhibiting their ability to mediate ubiquitination and autoubiquitination. It however does not mediate deubiquitination of BRCA1 and BARD1. Able to mediate autodeubiquitination via intramolecular interactions to couteract monoubiquitination at the nuclear localization signal (NLS), thereby protecting it from cytoplasmic sequestration (PubMed:24703950). Acts as a tumor suppressor.
VE: 1 * 100 µl


Artikel-Nr: (BOSSBS-8411R-A647)
Lieferant: Bioss
Beschreibung: Cysteine-rich secretory proteins (CRISPs) represent a family of evolutionarily conserved proteins that may play a role in the innate immune system and are transcriptionally regulated by androgens in several tissues. GAPR-1 (Golgi-associated plant pathogenesis-related protein 1), also known as GLIPR2, is a 154 amino acid lipid anchor protein belonging to the CRISP family. GAPR-1 also shares similarity with the pathogenesis-related protein (PR) superfamily, and may play an important role in the immune system. Existing as a homodimer, GAPR-1 is highly expressed in lung and peripheral leukocytes with minor expression in liver and kidney. Containing a conserved sperm-coating protein (SCP) domain, GAPR-1 binds to negatively charged lipids and may be involved in the differentiation of epithelial cells into mesenchymal cells. Increased expression of GAPR-1 in kidney may contribute to the development of fibrosis.
VE: 1 * 100 µl


Artikel-Nr: (BOSSBS-8411R-A680)
Lieferant: Bioss
Beschreibung: Cysteine-rich secretory proteins (CRISPs) represent a family of evolutionarily conserved proteins that may play a role in the innate immune system and are transcriptionally regulated by androgens in several tissues. GAPR-1 (Golgi-associated plant pathogenesis-related protein 1), also known as GLIPR2, is a 154 amino acid lipid anchor protein belonging to the CRISP family. GAPR-1 also shares similarity with the pathogenesis-related protein (PR) superfamily, and may play an important role in the immune system. Existing as a homodimer, GAPR-1 is highly expressed in lung and peripheral leukocytes with minor expression in liver and kidney. Containing a conserved sperm-coating protein (SCP) domain, GAPR-1 binds to negatively charged lipids and may be involved in the differentiation of epithelial cells into mesenchymal cells. Increased expression of GAPR-1 in kidney may contribute to the development of fibrosis.
VE: 1 * 100 µl


Artikel-Nr: (BOSSBS-8411R-CY3)
Lieferant: Bioss
Beschreibung: Cysteine-rich secretory proteins (CRISPs) represent a family of evolutionarily conserved proteins that may play a role in the innate immune system and are transcriptionally regulated by androgens in several tissues. GAPR-1 (Golgi-associated plant pathogenesis-related protein 1), also known as GLIPR2, is a 154 amino acid lipid anchor protein belonging to the CRISP family. GAPR-1 also shares similarity with the pathogenesis-related protein (PR) superfamily, and may play an important role in the immune system. Existing as a homodimer, GAPR-1 is highly expressed in lung and peripheral leukocytes with minor expression in liver and kidney. Containing a conserved sperm-coating protein (SCP) domain, GAPR-1 binds to negatively charged lipids and may be involved in the differentiation of epithelial cells into mesenchymal cells. Increased expression of GAPR-1 in kidney may contribute to the development of fibrosis.
VE: 1 * 100 µl


Artikel-Nr: (BOSSBS-8411R-CY5.5)
Lieferant: Bioss
Beschreibung: Cysteine-rich secretory proteins (CRISPs) represent a family of evolutionarily conserved proteins that may play a role in the innate immune system and are transcriptionally regulated by androgens in several tissues. GAPR-1 (Golgi-associated plant pathogenesis-related protein 1), also known as GLIPR2, is a 154 amino acid lipid anchor protein belonging to the CRISP family. GAPR-1 also shares similarity with the pathogenesis-related protein (PR) superfamily, and may play an important role in the immune system. Existing as a homodimer, GAPR-1 is highly expressed in lung and peripheral leukocytes with minor expression in liver and kidney. Containing a conserved sperm-coating protein (SCP) domain, GAPR-1 binds to negatively charged lipids and may be involved in the differentiation of epithelial cells into mesenchymal cells. Increased expression of GAPR-1 in kidney may contribute to the development of fibrosis.
VE: 1 * 100 µl


Artikel-Nr: (SIAL558249-10G)
Lieferant: Merck
Beschreibung: Dipraseodymtrioxid, Sigma-Aldrich®
VE: 1 * 10 g


Artikel-Nr: (BOSSBS-8411R-HRP)
Lieferant: Bioss
Beschreibung: Cysteine-rich secretory proteins (CRISPs) represent a family of evolutionarily conserved proteins that may play a role in the innate immune system and are transcriptionally regulated by androgens in several tissues. GAPR-1 (Golgi-associated plant pathogenesis-related protein 1), also known as GLIPR2, is a 154 amino acid lipid anchor protein belonging to the CRISP family. GAPR-1 also shares similarity with the pathogenesis-related protein (PR) superfamily, and may play an important role in the immune system. Existing as a homodimer, GAPR-1 is highly expressed in lung and peripheral leukocytes with minor expression in liver and kidney. Containing a conserved sperm-coating protein (SCP) domain, GAPR-1 binds to negatively charged lipids and may be involved in the differentiation of epithelial cells into mesenchymal cells. Increased expression of GAPR-1 in kidney may contribute to the development of fibrosis.
VE: 1 * 100 µl


Artikel-Nr: (BOSSBS-8411R-FITC)
Lieferant: Bioss
Beschreibung: Cysteine-rich secretory proteins (CRISPs) represent a family of evolutionarily conserved proteins that may play a role in the innate immune system and are transcriptionally regulated by androgens in several tissues. GAPR-1 (Golgi-associated plant pathogenesis-related protein 1), also known as GLIPR2, is a 154 amino acid lipid anchor protein belonging to the CRISP family. GAPR-1 also shares similarity with the pathogenesis-related protein (PR) superfamily, and may play an important role in the immune system. Existing as a homodimer, GAPR-1 is highly expressed in lung and peripheral leukocytes with minor expression in liver and kidney. Containing a conserved sperm-coating protein (SCP) domain, GAPR-1 binds to negatively charged lipids and may be involved in the differentiation of epithelial cells into mesenchymal cells. Increased expression of GAPR-1 in kidney may contribute to the development of fibrosis.
VE: 1 * 100 µl


Artikel-Nr: (BOSSBS-3051R-CY5.5)
Lieferant: Bioss
Beschreibung: Deubiquitinating enzyme that plays a key role in chromatin by mediating deubiquitination of histone H2A and HCFC1. Catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1). Does not deubiquitinate monoubiquitinated histone H2B. Acts as a regulator of cell growth by mediating deubiquitination of HCFC1 N-terminal and C-terminal chains, with some specificity toward 'Lys-48'-linked polyubiquitin chains compared to 'Lys-63'-linked polyubiquitin chains. Deubiquitination of HCFC1 does not lead to increase stability of HCFC1. Interferes with the BRCA1 and BARD1 heterodimer activity by inhibiting their ability to mediate ubiquitination and autoubiquitination. It however does not mediate deubiquitination of BRCA1 and BARD1. Able to mediate autodeubiquitination via intramolecular interactions to couteract monoubiquitination at the nuclear localization signal (NLS), thereby protecting it from cytoplasmic sequestration (PubMed:24703950). Acts as a tumor suppressor.
VE: 1 * 100 µl


Lieferant: Merck
Beschreibung: Praseodym(III,IV)oxid, Sigma-Aldrich®

Artikel-Nr: (BOSSBS-3051R-A647)
Lieferant: Bioss
Beschreibung: Deubiquitinating enzyme that plays a key role in chromatin by mediating deubiquitination of histone H2A and HCFC1. Catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1). Does not deubiquitinate monoubiquitinated histone H2B. Acts as a regulator of cell growth by mediating deubiquitination of HCFC1 N-terminal and C-terminal chains, with some specificity toward 'Lys-48'-linked polyubiquitin chains compared to 'Lys-63'-linked polyubiquitin chains. Deubiquitination of HCFC1 does not lead to increase stability of HCFC1. Interferes with the BRCA1 and BARD1 heterodimer activity by inhibiting their ability to mediate ubiquitination and autoubiquitination. It however does not mediate deubiquitination of BRCA1 and BARD1. Able to mediate autodeubiquitination via intramolecular interactions to couteract monoubiquitination at the nuclear localization signal (NLS), thereby protecting it from cytoplasmic sequestration (PubMed:24703950). Acts as a tumor suppressor.
VE: 1 * 100 µl


Artikel-Nr: (BOSSBS-3051R-A555)
Lieferant: Bioss
Beschreibung: Deubiquitinating enzyme that plays a key role in chromatin by mediating deubiquitination of histone H2A and HCFC1. Catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1). Does not deubiquitinate monoubiquitinated histone H2B. Acts as a regulator of cell growth by mediating deubiquitination of HCFC1 N-terminal and C-terminal chains, with some specificity toward 'Lys-48'-linked polyubiquitin chains compared to 'Lys-63'-linked polyubiquitin chains. Deubiquitination of HCFC1 does not lead to increase stability of HCFC1. Interferes with the BRCA1 and BARD1 heterodimer activity by inhibiting their ability to mediate ubiquitination and autoubiquitination. It however does not mediate deubiquitination of BRCA1 and BARD1. Able to mediate autodeubiquitination via intramolecular interactions to couteract monoubiquitination at the nuclear localization signal (NLS), thereby protecting it from cytoplasmic sequestration (PubMed:24703950). Acts as a tumor suppressor.
VE: 1 * 100 µl


Artikel-Nr: (BOSSBS-3051R-CY7)
Lieferant: Bioss
Beschreibung: Deubiquitinating enzyme that plays a key role in chromatin by mediating deubiquitination of histone H2A and HCFC1. Catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1). Does not deubiquitinate monoubiquitinated histone H2B. Acts as a regulator of cell growth by mediating deubiquitination of HCFC1 N-terminal and C-terminal chains, with some specificity toward 'Lys-48'-linked polyubiquitin chains compared to 'Lys-63'-linked polyubiquitin chains. Deubiquitination of HCFC1 does not lead to increase stability of HCFC1. Interferes with the BRCA1 and BARD1 heterodimer activity by inhibiting their ability to mediate ubiquitination and autoubiquitination. It however does not mediate deubiquitination of BRCA1 and BARD1. Able to mediate autodeubiquitination via intramolecular interactions to couteract monoubiquitination at the nuclear localization signal (NLS), thereby protecting it from cytoplasmic sequestration (PubMed:24703950). Acts as a tumor suppressor.
VE: 1 * 100 µl


Artikel-Nr: (BOSSBS-3051R-A350)
Lieferant: Bioss
Beschreibung: Deubiquitinating enzyme that plays a key role in chromatin by mediating deubiquitination of histone H2A and HCFC1. Catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1). Does not deubiquitinate monoubiquitinated histone H2B. Acts as a regulator of cell growth by mediating deubiquitination of HCFC1 N-terminal and C-terminal chains, with some specificity toward 'Lys-48'-linked polyubiquitin chains compared to 'Lys-63'-linked polyubiquitin chains. Deubiquitination of HCFC1 does not lead to increase stability of HCFC1. Interferes with the BRCA1 and BARD1 heterodimer activity by inhibiting their ability to mediate ubiquitination and autoubiquitination. It however does not mediate deubiquitination of BRCA1 and BARD1. Able to mediate autodeubiquitination via intramolecular interactions to couteract monoubiquitination at the nuclear localization signal (NLS), thereby protecting it from cytoplasmic sequestration (PubMed:24703950). Acts as a tumor suppressor.
VE: 1 * 100 µl


Artikel-Nr: (BOSSBS-3051R-FITC)
Lieferant: Bioss
Beschreibung: Deubiquitinating enzyme that plays a key role in chromatin by mediating deubiquitination of histone H2A and HCFC1. Catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1). Does not deubiquitinate monoubiquitinated histone H2B. Acts as a regulator of cell growth by mediating deubiquitination of HCFC1 N-terminal and C-terminal chains, with some specificity toward 'Lys-48'-linked polyubiquitin chains compared to 'Lys-63'-linked polyubiquitin chains. Deubiquitination of HCFC1 does not lead to increase stability of HCFC1. Interferes with the BRCA1 and BARD1 heterodimer activity by inhibiting their ability to mediate ubiquitination and autoubiquitination. It however does not mediate deubiquitination of BRCA1 and BARD1. Able to mediate autodeubiquitination via intramolecular interactions to couteract monoubiquitination at the nuclear localization signal (NLS), thereby protecting it from cytoplasmic sequestration (PubMed:24703950). Acts as a tumor suppressor.
VE: 1 * 100 µl


Artikel-Nr: (BOSSBS-3051R-A680)
Lieferant: Bioss
Beschreibung: Deubiquitinating enzyme that plays a key role in chromatin by mediating deubiquitination of histone H2A and HCFC1. Catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1). Does not deubiquitinate monoubiquitinated histone H2B. Acts as a regulator of cell growth by mediating deubiquitination of HCFC1 N-terminal and C-terminal chains, with some specificity toward 'Lys-48'-linked polyubiquitin chains compared to 'Lys-63'-linked polyubiquitin chains. Deubiquitination of HCFC1 does not lead to increase stability of HCFC1. Interferes with the BRCA1 and BARD1 heterodimer activity by inhibiting their ability to mediate ubiquitination and autoubiquitination. It however does not mediate deubiquitination of BRCA1 and BARD1. Able to mediate autodeubiquitination via intramolecular interactions to couteract monoubiquitination at the nuclear localization signal (NLS), thereby protecting it from cytoplasmic sequestration (PubMed:24703950). Acts as a tumor suppressor.
VE: 1 * 100 µl


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Lager für diesen Artikel ist begrenzt, kann aber in einem Lagerhaus in Ihrer Nähe zur Verfügung. Bitte stellen Sie sicher, dass Sie in sind angemeldet auf dieser Seite, so dass verfügbare Bestand angezeigt werden können. Wenn das call noch angezeigt wird und Sie Hilfe benötigen, rufen Sie uns an 1-800-932 - 5000.
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