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Référence Produit: (BOSSBS-9491R-FITC)
Fournisseur: Bioss
Description: The SOSS (Sensor of single-strand DNA) complex consists of multiple proteins that promote DNA repair and G2/M checkpoint downstream of the MRN (Mre11, Rad50 and Nbs1) complex. The complex is composed of SSBP1, INTS3 and C9orf80. Specifically, the SOSS complex binds to ssDNA at DNA lesions that influences diverse endpoints in the cellular DNA damage response. The complex is required for efficient homologous recombination-dependent repair of double-stranded breaks and ATM-dependent signaling pathways. C9orf80, also known as SOSS complex subunit C and Single-stranded DNA-binding protein-interacting protein 1 (SSBIP1), is a 104 amino acid nuclear protein that is a component of the SOSS complex. Upon DNA damage, C9orf80 along with other components of the SOSS complex migrate to the nucleus. There are two isoforms of C9orf80 that are produced as a result of alternative splicing events.
UOM: 1 * 100 µl


Référence Produit: (BOSSBS-9491R-A647)
Fournisseur: Bioss
Description: The SOSS (Sensor of single-strand DNA) complex consists of multiple proteins that promote DNA repair and G2/M checkpoint downstream of the MRN (Mre11, Rad50 and Nbs1) complex. The complex is composed of SSBP1, INTS3 and C9orf80. Specifically, the SOSS complex binds to ssDNA at DNA lesions that influences diverse endpoints in the cellular DNA damage response. The complex is required for efficient homologous recombination-dependent repair of double-stranded breaks and ATM-dependent signaling pathways. C9orf80, also known as SOSS complex subunit C and Single-stranded DNA-binding protein-interacting protein 1 (SSBIP1), is a 104 amino acid nuclear protein that is a component of the SOSS complex. Upon DNA damage, C9orf80 along with other components of the SOSS complex migrate to the nucleus. There are two isoforms of C9orf80 that are produced as a result of alternative splicing events.
UOM: 1 * 100 µl


Référence Produit: (BOSSBS-9491R-HRP)
Fournisseur: Bioss
Description: The SOSS (Sensor of single-strand DNA) complex consists of multiple proteins that promote DNA repair and G2/M checkpoint downstream of the MRN (Mre11, Rad50 and Nbs1) complex. The complex is composed of SSBP1, INTS3 and C9orf80. Specifically, the SOSS complex binds to ssDNA at DNA lesions that influences diverse endpoints in the cellular DNA damage response. The complex is required for efficient homologous recombination-dependent repair of double-stranded breaks and ATM-dependent signaling pathways. C9orf80, also known as SOSS complex subunit C and Single-stranded DNA-binding protein-interacting protein 1 (SSBIP1), is a 104 amino acid nuclear protein that is a component of the SOSS complex. Upon DNA damage, C9orf80 along with other components of the SOSS complex migrate to the nucleus. There are two isoforms of C9orf80 that are produced as a result of alternative splicing events.
UOM: 1 * 100 µl


Référence Produit: (BOSSBS-9491R-A750)
Fournisseur: Bioss
Description: The SOSS (Sensor of single-strand DNA) complex consists of multiple proteins that promote DNA repair and G2/M checkpoint downstream of the MRN (Mre11, Rad50 and Nbs1) complex. The complex is composed of SSBP1, INTS3 and C9orf80. Specifically, the SOSS complex binds to ssDNA at DNA lesions that influences diverse endpoints in the cellular DNA damage response. The complex is required for efficient homologous recombination-dependent repair of double-stranded breaks and ATM-dependent Signalling pathways. C9orf80, also known as SOSS complex subunit C and Single-stranded DNA-binding protein-interacting protein 1 (SSBIP1), is a 104 amino acid nuclear protein that is a component of the SOSS complex. Upon DNA damage, C9orf80 along with other components of the SOSS complex migrate to the nucleus. There are two isoforms of C9orf80 that are produced as a result of alternative splicing events.
UOM: 1 * 100 µl


Fournisseur: Bohlender
Description: Le b.safe Mini-display est la solution de base optimale pour le contrôle local d'unités HPLC individuelles.

Référence Produit: (BOSSBS-9491R-CY5)
Fournisseur: Bioss
Description: The SOSS (Sensor of single-strand DNA) complex consists of multiple proteins that promote DNA repair and G2/M checkpoint downstream of the MRN (Mre11, Rad50 and Nbs1) complex. The complex is composed of SSBP1, INTS3 and C9orf80. Specifically, the SOSS complex binds to ssDNA at DNA lesions that influences diverse endpoints in the cellular DNA damage response. The complex is required for efficient homologous recombination-dependent repair of double-stranded breaks and ATM-dependent signaling pathways. C9orf80, also known as SOSS complex subunit C and Single-stranded DNA-binding protein-interacting protein 1 (SSBIP1), is a 104 amino acid nuclear protein that is a component of the SOSS complex. Upon DNA damage, C9orf80 along with other components of the SOSS complex migrate to the nucleus. There are two isoforms of C9orf80 that are produced as a result of alternative splicing events.
UOM: 1 * 100 µl


Référence Produit: (BOSSBS-9491R)
Fournisseur: Bioss
Description: The SOSS (Sensor of single-strand DNA) complex consists of multiple proteins that promote DNA repair and G2/M checkpoint downstream of the MRN (Mre11, Rad50 and Nbs1) complex. The complex is composed of SSBP1, INTS3 and C9orf80. Specifically, the SOSS complex binds to ssDNA at DNA lesions that influences diverse endpoints in the cellular DNA damage response. The complex is required for efficient homologous recombination-dependent repair of double-stranded breaks and ATM-dependent signaling pathways. C9orf80, also known as SOSS complex subunit C and Single-stranded DNA-binding protein-interacting protein 1 (SSBIP1), is a 104 amino acid nuclear protein that is a component of the SOSS complex. Upon DNA damage, C9orf80 along with other components of the SOSS complex migrate to the nucleus. There are two isoforms of C9orf80 that are produced as a result of alternative splicing events.
UOM: 1 * 100 µl


Fournisseur: HORIBA
Description: Ces appareils de mesure étanches permettent de mesurer et d'afficher jusqu'à 11 paramètres simultanément avec une seule sonde. Grâce à leur conception robuste et leurs capteurs remplaçables sur site, ils sont idéaux pour une utilisation extérieure, par exemple lors du test des eaux souterraines ou de surface. Leur format compact et la dragonne permettent une utilisation d'une seule main.

Référence Produit: (BOSSBS-9491R-CY5.5)
Fournisseur: Bioss
Description: The SOSS (Sensor of single-strand DNA) complex consists of multiple proteins that promote DNA repair and G2/M checkpoint downstream of the MRN (Mre11, Rad50 and Nbs1) complex. The complex is composed of SSBP1, INTS3 and C9orf80. Specifically, the SOSS complex binds to ssDNA at DNA lesions that influences diverse endpoints in the cellular DNA damage response. The complex is required for efficient homologous recombination-dependent repair of double-stranded breaks and ATM-dependent signaling pathways. C9orf80, also known as SOSS complex subunit C and Single-stranded DNA-binding protein-interacting protein 1 (SSBIP1), is a 104 amino acid nuclear protein that is a component of the SOSS complex. Upon DNA damage, C9orf80 along with other components of the SOSS complex migrate to the nucleus. There are two isoforms of C9orf80 that are produced as a result of alternative splicing events.
UOM: 1 * 100 µl


Référence Produit: (BOSSBS-9491R-A555)
Fournisseur: Bioss
Description: The SOSS (Sensor of single-strand DNA) complex consists of multiple proteins that promote DNA repair and G2/M checkpoint downstream of the MRN (Mre11, Rad50 and Nbs1) complex. The complex is composed of SSBP1, INTS3 and C9orf80. Specifically, the SOSS complex binds to ssDNA at DNA lesions that influences diverse endpoints in the cellular DNA damage response. The complex is required for efficient homologous recombination-dependent repair of double-stranded breaks and ATM-dependent signaling pathways. C9orf80, also known as SOSS complex subunit C and Single-stranded DNA-binding protein-interacting protein 1 (SSBIP1), is a 104 amino acid nuclear protein that is a component of the SOSS complex. Upon DNA damage, C9orf80 along with other components of the SOSS complex migrate to the nucleus. There are two isoforms of C9orf80 that are produced as a result of alternative splicing events.
UOM: 1 * 100 µl


Référence Produit: (BOSSBS-9491R-A488)
Fournisseur: Bioss
Description: The SOSS (Sensor of single-strand DNA) complex consists of multiple proteins that promote DNA repair and G2/M checkpoint downstream of the MRN (Mre11, Rad50 and Nbs1) complex. The complex is composed of SSBP1, INTS3 and C9orf80. Specifically, the SOSS complex binds to ssDNA at DNA lesions that influences diverse endpoints in the cellular DNA damage response. The complex is required for efficient homologous recombination-dependent repair of double-stranded breaks and ATM-dependent signaling pathways. C9orf80, also known as SOSS complex subunit C and Single-stranded DNA-binding protein-interacting protein 1 (SSBIP1), is a 104 amino acid nuclear protein that is a component of the SOSS complex. Upon DNA damage, C9orf80 along with other components of the SOSS complex migrate to the nucleus. There are two isoforms of C9orf80 that are produced as a result of alternative splicing events.
UOM: 1 * 100 µl


Référence Produit: (BOSSBS-6634R-A750)
Fournisseur: Bioss
Description: Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex. Has only a low DNA repair activity by itself which is stimulated by RAD23B and RAD23A. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides. This feature is proposed to be related to a dynamic sensor function: XPC can rapidly screen duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA-binding activity. The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognises a wide spectrum of damaged DNA characterised by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognise and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. <i>in vitro</i>, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts.
UOM: 1 * 100 µl


Référence Produit: (BOSSBS-6634R-A488)
Fournisseur: Bioss
Description: Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex. Has only a low DNA repair activity by itself which is stimulated by RAD23B and RAD23A. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides. This feature is proposed to be related to a dynamic sensor function: XPC can rapidly screen duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA-binding activity. The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts.
UOM: 1 * 100 µl


Référence Produit: (BOSSBS-6634R-CY7)
Fournisseur: Bioss
Description: Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex. Has only a low DNA repair activity by itself which is stimulated by RAD23B and RAD23A. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides. This feature is proposed to be related to a dynamic sensor function: XPC can rapidly screen duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA-binding activity. The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts.
UOM: 1 * 100 µl


Référence Produit: (BOSSBS-6634R-FITC)
Fournisseur: Bioss
Description: Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex. Has only a low DNA repair activity by itself which is stimulated by RAD23B and RAD23A. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides. This feature is proposed to be related to a dynamic sensor function: XPC can rapidly screen duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA-binding activity. The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts.
UOM: 1 * 100 µl


Référence Produit: (BOSSBS-6634R-CY3)
Fournisseur: Bioss
Description: Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex. Has only a low DNA repair activity by itself which is stimulated by RAD23B and RAD23A. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides. This feature is proposed to be related to a dynamic sensor function: XPC can rapidly screen duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA-binding activity. The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts.
UOM: 1 * 100 µl


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