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Gentamicin sulphate 10 mg/ml, Reagent Grade

Supplier: MP Biomedicals
Description: Gentamicin is an aminoglycoside antibiotic complex produced by fermentation of <i>Micromonospora purpurea</i> or <i>M. echinospora</i>. It inhibits the growth of a wide variety of Gram-positive and Gram-negative microorganisms.

Image Unavailable-BOSSBS-9430R-CY7

Anti-HSPB7 Rabbit Polyclonal Antibody (Cy7®)

Catalog Number: (BOSSBS-9430R-CY7)
Supplier: Bioss
Description: The heat shock proteins (HSPs) comprise a group of highly conserved, abundantly expressed proteins with diverse functions, including the assembly and sequestering of multiprotein complexes, transportation of nascent polypeptide chains across cellular membranes and regulation of protein folding. Heat shock proteins (also known as molecular chaperones) fall into six general families: HSP 90, HSP 70, HSP 60, the small HSPs, the immunophilins and the HSP 110 family. HSPB7 (heat shock 27kDa protein family, member 7), also known as cvHSP (cardiovascular heat shock protein) or Heat shock protein beta-7, is a member of the small HSP (sHSP) family expressed in heart and skeletal muscle. Members of the sHSP family contain a conserved C-terminal ?crystallin domain and typically function in homo- or heteromeric complexes. The sHSPs bind to denatured proteins and are responsible for preventing the aggregation of these proteins. In response to muscle fiber transformation and in muscular dystrophy, the expression levels of HSPB7 are drastically increased, suggesting that HSPB7 may be a useful target in therapeutic strategies for preventing age-related muscle wasting.
UOM: 1 * 100 µl

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Product Image-BOSSBS-9430R

Anti-HSPB7 Rabbit Polyclonal Antibody

Catalog Number: (BOSSBS-9430R)
Supplier: Bioss
Description: The heat shock proteins (HSPs) comprise a group of highly conserved, abundantly expressed proteins with diverse functions, including the assembly and sequestering of multiprotein complexes, transportation of nascent polypeptide chains across cellular membranes and regulation of protein folding. Heat shock proteins (also known as molecular chaperones) fall into six general families: HSP 90, HSP 70, HSP 60, the small HSPs, the immunophilins and the HSP 110 family. HSPB7 (heat shock 27kDa protein family, member 7), also known as cvHSP (cardiovascular heat shock protein) or Heat shock protein beta-7, is a member of the small HSP (sHSP) family expressed in heart and skeletal muscle. Members of the sHSP family contain a conserved C-terminal ?crystallin domain and typically function in homo- or heteromeric complexes. The sHSPs bind to denatured proteins and are responsible for preventing the aggregation of these proteins. In response to muscle fiber transformation and in muscular dystrophy, the expression levels of HSPB7 are drastically increased, suggesting that HSPB7 may be a useful target in therapeutic strategies for preventing age-related muscle wasting.
UOM: 1 * 100 µl
Image Unavailable-BNC470225-100

Anti-MVP Mouse Monoclonal Antibody (CF647) [clone: 1032]

Supplier: Biotium
Description: Recognizes a protein of 104 kDa-110 kDa, characterized as major vault protein (MVP). Vaults are large ribonucleoprotein particles (RNPs) present in all eukaryotic cells. They have a complex morphology, including several small molecules of RNA, but a single protein species. The MVP accounts for >70% of their mass. Their shape is reminiscent of the nucleopore central plug. Treatment of cells with estradiol increases the amount of MVP in nuclear extract. The hormone-dependent interaction of vaults with ER is prevented in vitro by sodium molybdate. Antibodies to estrogen, progesterone and glucocorticoid receptors are able to co-immunoprecipitate the MVP. MVP is overexpressed in many neoplastic tissues and cell lines. Expression of MVP predicts a poor response to chemotherapy.

Image Unavailable-BNUB0225-500

Anti-MVP Mouse Monoclonal Antibody (Purified) [clone: 1032]

Supplier: Biotium
Description: Recognizes a protein of 104 kDa-110 kDa, characterized as major vault protein (MVP). Vaults are large ribonucleoprotein particles (RNPs) present in all eukaryotic cells. They have a complex morphology, including several small molecules of RNA, but a single protein species. The MVP accounts for >70% of their mass. Their shape is reminiscent of the nucleopore central plug. Treatment of cells with estradiol increases the amount of MVP in nuclear extract. The hormone-dependent interaction of vaults with ER is prevented in vitro by sodium molybdate. Antibodies to estrogen, progesterone and glucocorticoid receptors are able to co-immunoprecipitate the MVP. MVP is overexpressed in many neoplastic tissues and cell lines. Expression of MVP predicts a poor response to chemotherapy.

Image Unavailable-BNCB0224-100

Anti-MVP Mouse Monoclonal Antibody (Biotin) [clone: 1014]

Supplier: Biotium
Description: Recognizes a protein of 104 kDa-110 kDa, characterized as major vault protein (MVP). Vaults are large ribonucleoprotein particles (RNPs) present in all eukaryotic cells. They have a complex morphology, including several small molecules of RNA, but a single protein species. The MVP accounts for >70% of their mass. Their shape is reminiscent of the nucleopore central plug. Treatment of cells with estradiol increases the amount of MVP in nuclear extract. The hormone-dependent interaction of vaults with ER is prevented in vitro by sodium molybdate. Antibodies to estrogen, progesterone and glucocorticoid receptors are able to co-immunoprecipitate the MVP. MVP is overexpressed in many neoplastic tissues and cell lines. Expression of MVP predicts a poor response to chemotherapy.

Image Unavailable-BNC680225-500

Anti-MVP Mouse Monoclonal Antibody (CF568) [clone: 1032]

Supplier: Biotium
Description: Recognizes a protein of 104 kDa-110 kDa, characterized as major vault protein (MVP). Vaults are large ribonucleoprotein particles (RNPs) present in all eukaryotic cells. They have a complex morphology, including several small molecules of RNA, but a single protein species. The MVP accounts for >70% of their mass. Their shape is reminiscent of the nucleopore central plug. Treatment of cells with estradiol increases the amount of MVP in nuclear extract. The hormone-dependent interaction of vaults with ER is prevented in vitro by sodium molybdate. Antibodies to estrogen, progesterone and glucocorticoid receptors are able to co-immunoprecipitate the MVP. MVP is overexpressed in many neoplastic tissues and cell lines. Expression of MVP predicts a poor response to chemotherapy.

Image Unavailable-BNC940225-100

Anti-MVP Mouse Monoclonal Antibody (CF594) [clone: 1032]

Supplier: Biotium
Description: Recognizes a protein of 104 kDa-110 kDa, characterized as major vault protein (MVP). Vaults are large ribonucleoprotein particles (RNPs) present in all eukaryotic cells. They have a complex morphology, including several small molecules of RNA, but a single protein species. The MVP accounts for >70% of their mass. Their shape is reminiscent of the nucleopore central plug. Treatment of cells with estradiol increases the amount of MVP in nuclear extract. The hormone-dependent interaction of vaults with ER is prevented in vitro by sodium molybdate. Antibodies to estrogen, progesterone and glucocorticoid receptors are able to co-immunoprecipitate the MVP. MVP is overexpressed in many neoplastic tissues and cell lines. Expression of MVP predicts a poor response to chemotherapy.

Image Unavailable-BNC400224-100

Anti-MVP Mouse Monoclonal Antibody (CF640R) [clone: 1014]

Supplier: Biotium
Description: Recognizes a protein of 104 kDa-110 kDa, characterized as major vault protein (MVP). Vaults are large ribonucleoprotein particles (RNPs) present in all eukaryotic cells. They have a complex morphology, including several small molecules of RNA, but a single protein species. The MVP accounts for >70% of their mass. Their shape is reminiscent of the nucleopore central plug. Treatment of cells with estradiol increases the amount of MVP in nuclear extract. The hormone-dependent interaction of vaults with ER is prevented in vitro by sodium molybdate. Antibodies to estrogen, progesterone and glucocorticoid receptors are able to co-immunoprecipitate the MVP. MVP is overexpressed in many neoplastic tissues and cell lines. Expression of MVP predicts a poor response to chemotherapy.

Image Unavailable-BNUM0224-50

Anti-MVP Mouse Monoclonal Antibody (Purified, BSA-free) [clone: 1014]

Catalog Number: (BNUM0224-50)
Supplier: Biotium
Description: Recognizes a protein of 104 kDa-110 kDa, characterized as major vault protein (MVP). Vaults are large ribonucleoprotein particles (RNPs) present in all eukaryotic cells. They have a complex morphology, including several small molecules of RNA, but a single protein species. The MVP accounts for >70% of their mass. Their shape is reminiscent of the nucleopore central plug. Treatment of cells with estradiol increases the amount of MVP in nuclear extract. The hormone-dependent interaction of vaults with ER is prevented in vitro by sodium molybdate. Antibodies to estrogen, progesterone and glucocorticoid receptors are able to co-immunoprecipitate the MVP. MVP is overexpressed in many neoplastic tissues and cell lines. Expression of MVP predicts a poor response to chemotherapy.
UOM: 1 * 50 µl
Image Unavailable-BOSSBS-9430R-A750

Anti-HSPB7 Rabbit Polyclonal Antibody (Alexa Fluor® 750)

Catalog Number: (BOSSBS-9430R-A750)
Supplier: Bioss
Description: The heat shock proteins (HSPs) comprise a group of highly conserved, abundantly expressed proteins with diverse functions, including the assembly and sequestering of multiprotein complexes, transportation of nascent polypeptide chains across cellular membranes and regulation of protein folding. Heat shock proteins (also known as molecular chaperones) fall into six general families: HSP 90, HSP 70, HSP 60, the small HSPs, the immunophilins and the HSP 110 family. HSPB7 (heat shock 27kDa protein family, member 7), also known as cvHSP (cardiovascular heat shock protein) or Heat shock protein beta-7, is a member of the small HSP (sHSP) family expressed in heart and skeletal muscle. Members of the sHSP family contain a conserved C-terminal crystallin domain and typically function in homo- or heteromeric complexes. The sHSPs bind to denatured proteins and are responsible for preventing the aggregation of these proteins. In response to muscle fiber transformation and in muscular dystrophy, the expression levels of HSPB7 are drastically increased, suggesting that HSPB7 may be a useful target in therapeutic strategies for preventing age-related muscle wasting.
UOM: 1 * 100 µl
Image Unavailable-BOSSBS-9430R-A488

Anti-HSPB7 Rabbit Polyclonal Antibody (Alexa Fluor® 488)

Catalog Number: (BOSSBS-9430R-A488)
Supplier: Bioss
Description: The heat shock proteins (HSPs) comprise a group of highly conserved, abundantly expressed proteins with diverse functions, including the assembly and sequestering of multiprotein complexes, transportation of nascent polypeptide chains across cellular membranes and regulation of protein folding. Heat shock proteins (also known as molecular chaperones) fall into six general families: HSP 90, HSP 70, HSP 60, the small HSPs, the immunophilins and the HSP 110 family. HSPB7 (heat shock 27kDa protein family, member 7), also known as cvHSP (cardiovascular heat shock protein) or Heat shock protein beta-7, is a member of the small HSP (sHSP) family expressed in heart and skeletal muscle. Members of the sHSP family contain a conserved C-terminal ?crystallin domain and typically function in homo- or heteromeric complexes. The sHSPs bind to denatured proteins and are responsible for preventing the aggregation of these proteins. In response to muscle fiber transformation and in muscular dystrophy, the expression levels of HSPB7 are drastically increased, suggesting that HSPB7 may be a useful target in therapeutic strategies for preventing age-related muscle wasting.
UOM: 1 * 100 µl
Image Unavailable-BOSSBS-9430R-A350

Anti-HSPB7 Rabbit Polyclonal Antibody (Alexa Fluor® 350)

Catalog Number: (BOSSBS-9430R-A350)
Supplier: Bioss
Description: The heat shock proteins (HSPs) comprise a group of highly conserved, abundantly expressed proteins with diverse functions, including the assembly and sequestering of multiprotein complexes, transportation of nascent polypeptide chains across cellular membranes and regulation of protein folding. Heat shock proteins (also known as molecular chaperones) fall into six general families: HSP 90, HSP 70, HSP 60, the small HSPs, the immunophilins and the HSP 110 family. HSPB7 (heat shock 27kDa protein family, member 7), also known as cvHSP (cardiovascular heat shock protein) or Heat shock protein beta-7, is a member of the small HSP (sHSP) family expressed in heart and skeletal muscle. Members of the sHSP family contain a conserved C-terminal ?crystallin domain and typically function in homo- or heteromeric complexes. The sHSPs bind to denatured proteins and are responsible for preventing the aggregation of these proteins. In response to muscle fiber transformation and in muscular dystrophy, the expression levels of HSPB7 are drastically increased, suggesting that HSPB7 may be a useful target in therapeutic strategies for preventing age-related muscle wasting.
UOM: 1 * 100 µl
Image Unavailable-BOSSBS-9430R-CY5.5

Anti-HSPB7 Rabbit Polyclonal Antibody (Cy5.5®)

Catalog Number: (BOSSBS-9430R-CY5.5)
Supplier: Bioss
Description: The heat shock proteins (HSPs) comprise a group of highly conserved, abundantly expressed proteins with diverse functions, including the assembly and sequestering of multiprotein complexes, transportation of nascent polypeptide chains across cellular membranes and regulation of protein folding. Heat shock proteins (also known as molecular chaperones) fall into six general families: HSP 90, HSP 70, HSP 60, the small HSPs, the immunophilins and the HSP 110 family. HSPB7 (heat shock 27kDa protein family, member 7), also known as cvHSP (cardiovascular heat shock protein) or Heat shock protein beta-7, is a member of the small HSP (sHSP) family expressed in heart and skeletal muscle. Members of the sHSP family contain a conserved C-terminal ?crystallin domain and typically function in homo- or heteromeric complexes. The sHSPs bind to denatured proteins and are responsible for preventing the aggregation of these proteins. In response to muscle fiber transformation and in muscular dystrophy, the expression levels of HSPB7 are drastically increased, suggesting that HSPB7 may be a useful target in therapeutic strategies for preventing age-related muscle wasting.
UOM: 1 * 100 µl
Image Unavailable-BOSSBS-9430R-HRP

Anti-HSPB7 Rabbit Polyclonal Antibody (HRP (Horseradish Peroxidase))

Catalog Number: (BOSSBS-9430R-HRP)
Supplier: Bioss
Description: The heat shock proteins (HSPs) comprise a group of highly conserved, abundantly expressed proteins with diverse functions, including the assembly and sequestering of multiprotein complexes, transportation of nascent polypeptide chains across cellular membranes and regulation of protein folding. Heat shock proteins (also known as molecular chaperones) fall into six general families: HSP 90, HSP 70, HSP 60, the small HSPs, the immunophilins and the HSP 110 family. HSPB7 (heat shock 27kDa protein family, member 7), also known as cvHSP (cardiovascular heat shock protein) or Heat shock protein beta-7, is a member of the small HSP (sHSP) family expressed in heart and skeletal muscle. Members of the sHSP family contain a conserved C-terminal ?crystallin domain and typically function in homo- or heteromeric complexes. The sHSPs bind to denatured proteins and are responsible for preventing the aggregation of these proteins. In response to muscle fiber transformation and in muscular dystrophy, the expression levels of HSPB7 are drastically increased, suggesting that HSPB7 may be a useful target in therapeutic strategies for preventing age-related muscle wasting.
UOM: 1 * 100 µl
Image Unavailable-BNC880225-500

Anti-MVP Mouse Monoclonal Antibody (CF488A) [clone: 1032]

Supplier: Biotium
Description: Recognizes a protein of 104 kDa-110 kDa, characterized as major vault protein (MVP). Vaults are large ribonucleoprotein particles (RNPs) present in all eukaryotic cells. They have a complex morphology, including several small molecules of RNA, but a single protein species. The MVP accounts for >70% of their mass. Their shape is reminiscent of the nucleopore central plug. Treatment of cells with estradiol increases the amount of MVP in nuclear extract. The hormone-dependent interaction of vaults with ER is prevented in vitro by sodium molybdate. Antibodies to estrogen, progesterone and glucocorticoid receptors are able to co-immunoprecipitate the MVP. MVP is overexpressed in many neoplastic tissues and cell lines. Expression of MVP predicts a poor response to chemotherapy.

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Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the call is still displayed and you need assistance, please call us on +353 1 88 22222.
Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the call is still displayed and you need assistance, please call us on +353 1 88 22222.
This product is marked as restricted and can only be purchased by approved Shipping Accounts. If you need further assistance, email VWR Regulatory Department at eurega_services@eu.vwr.com
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This product has been blocked by your organisation. Please contact your purchasing department for more information.
The original product is no longer available. The replacement shown is available.
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