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Procurou por: Nonidet®+P+40+Substitute+(NP-40)


16 090  resultados encontrados

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Fornecedor: Abcam
Descrição: Rabbit monoclonal [EPR28604-40] to Syntenin - BSA and Azide free.

Novo produto

Fornecedor: Abcam
Descrição: Rabbit monoclonal [EPR23200-40] to ZNFN1A2/HELIOS.

Novo produto

Fornecedor: Abcam
Descrição: Rabbit monoclonal [EPR23228-40] to EGR2 - BSA and Azide free.

Fornecedor: Abcam
Descrição: Rabbit monoclonal [EPR22509-40] to CD36 - BSA and Azide free.

Fornecedor: Abcam
Descrição: Rabbit monoclonal [EPR26465-40] to RIG-I/DDX58.

Novo produto

Fornecedor: Spectrum Chemical
Descrição: Polyoxyl 40 Stearate, Type II, NF is commonly used in pharmaceutical formulations as an emulsifier and a surfactant.

Código de Artigo: (BOSSBS-11277R-A750)
Fornecedor: Bioss
Descrição: DnaJ-like proteins interact with HSP 70 molecular chaperones and function to facilitate protein folding and mitochondrial protein import. HSP 40-4, also known as HDJ2, is the human DnaJ homolog that functions as a co-chaperone with a cysteine-rich zinc finger domain. The cellular redox enzyme thioredoxin interacts with HSP 40-4, and oxidation and reduction reversibly regulate HSP 40-4 function in response to the changing redox states of the cell. The zinc finger domain of HSP 40-4 may act as a redox sensor of chaperone-mediated protein-folding machinery, since HSP 40-4 inactivation leads to the oxidation of cysteine thiols and a simultaneous release of coordinated zinc. Loss of the HSP 40-4 protein may be linked to severe defects in spermatogenesis that involve aberrant androgen Signalling.
UOM: 1 * 100 µl


Código de Artigo: (BOSSBS-11277R-A555)
Fornecedor: Bioss
Descrição: DnaJ-like proteins interact with HSP 70 molecular chaperones and function to facilitate protein folding and mitochondrial protein import. HSP 40-4, also known as HDJ2, is the human DnaJ homolog that functions as a co-chaperone with a cysteine-rich zinc finger domain. The cellular redox enzyme thioredoxin interacts with HSP 40-4, and oxidation and reduction reversibly regulate HSP 40-4 function in response to the changing redox states of the cell. The zinc finger domain of HSP 40-4 may act as a redox sensor of chaperone-mediated protein-folding machinery, since HSP 40-4 inactivation leads to the oxidation of cysteine thiols and a simultaneous release of coordinated zinc. Loss of the HSP 40-4 protein may be linked to severe defects in spermatogenesis that involve aberrant androgen signaling.
UOM: 1 * 100 µl


Fornecedor: Abcam
Descrição: Rabbit monoclonal [EPR22403-40] to NCR1 - BSA and Azide free.

Código de Artigo: (BOSSBS-11277R-A647)
Fornecedor: Bioss
Descrição: DnaJ-like proteins interact with HSP 70 molecular chaperones and function to facilitate protein folding and mitochondrial protein import. HSP 40-4, also known as HDJ2, is the human DnaJ homolog that functions as a co-chaperone with a cysteine-rich zinc finger domain. The cellular redox enzyme thioredoxin interacts with HSP 40-4, and oxidation and reduction reversibly regulate HSP 40-4 function in response to the changing redox states of the cell. The zinc finger domain of HSP 40-4 may act as a redox sensor of chaperone-mediated protein-folding machinery, since HSP 40-4 inactivation leads to the oxidation of cysteine thiols and a simultaneous release of coordinated zinc. Loss of the HSP 40-4 protein may be linked to severe defects in spermatogenesis that involve aberrant androgen signaling.
UOM: 1 * 100 µl


Código de Artigo: (BOSSBS-11277R-FITC)
Fornecedor: Bioss
Descrição: DnaJ-like proteins interact with HSP 70 molecular chaperones and function to facilitate protein folding and mitochondrial protein import. HSP 40-4, also known as HDJ2, is the human DnaJ homolog that functions as a co-chaperone with a cysteine-rich zinc finger domain. The cellular redox enzyme thioredoxin interacts with HSP 40-4, and oxidation and reduction reversibly regulate HSP 40-4 function in response to the changing redox states of the cell. The zinc finger domain of HSP 40-4 may act as a redox sensor of chaperone-mediated protein-folding machinery, since HSP 40-4 inactivation leads to the oxidation of cysteine thiols and a simultaneous release of coordinated zinc. Loss of the HSP 40-4 protein may be linked to severe defects in spermatogenesis that involve aberrant androgen signaling.
UOM: 1 * 100 µl


Código de Artigo: (BOSSBS-11277R-A350)
Fornecedor: Bioss
Descrição: DnaJ-like proteins interact with HSP 70 molecular chaperones and function to facilitate protein folding and mitochondrial protein import. HSP 40-4, also known as HDJ2, is the human DnaJ homolog that functions as a co-chaperone with a cysteine-rich zinc finger domain. The cellular redox enzyme thioredoxin interacts with HSP 40-4, and oxidation and reduction reversibly regulate HSP 40-4 function in response to the changing redox states of the cell. The zinc finger domain of HSP 40-4 may act as a redox sensor of chaperone-mediated protein-folding machinery, since HSP 40-4 inactivation leads to the oxidation of cysteine thiols and a simultaneous release of coordinated zinc. Loss of the HSP 40-4 protein may be linked to severe defects in spermatogenesis that involve aberrant androgen signaling.
UOM: 1 * 100 µl


Fornecedor: Abcam
Descrição: Rabbit monoclonal [EPR27216-40] to NLRX1 - BSA and Azide free.

Código de Artigo: (BOSSBS-4976R)
Fornecedor: Bioss
Descrição: Anti-H1N1 NP Rabbit Polyclonal Antibody
UOM: 1 * 100 µl


Código de Artigo: (USBIN2176-32B)
Fornecedor: US Biological
Descrição: Anti-NPS Rabbit Polyclonal Antibody (Biotin)
UOM: 1 * 100 µl


Código de Artigo: (BOSSBS-11277R-A488)
Fornecedor: Bioss
Descrição: DnaJ-like proteins interact with HSP 70 molecular chaperones and function to facilitate protein folding and mitochondrial protein import. HSP 40-4, also known as HDJ2, is the human DnaJ homolog that functions as a co-chaperone with a cysteine-rich zinc finger domain. The cellular redox enzyme thioredoxin interacts with HSP 40-4, and oxidation and reduction reversibly regulate HSP 40-4 function in response to the changing redox states of the cell. The zinc finger domain of HSP 40-4 may act as a redox sensor of chaperone-mediated protein-folding machinery, since HSP 40-4 inactivation leads to the oxidation of cysteine thiols and a simultaneous release of coordinated zinc. Loss of the HSP 40-4 protein may be linked to severe defects in spermatogenesis that involve aberrant androgen signaling.
UOM: 1 * 100 µl


Preço sob consulta
O stock para este item é limitado. Por favor, certifique-se de que efetuou o seu login para visualizar o stock disponível. Se a call ainda é exibida e precisar de ajuda, por favor, ligue para 213 600 770
O stock para este item é limitado. Por favor, certifique-se de que efetuou o seu login para visualizar o stock disponível. Se a call está visível e precisar de ajuda, por favor, ligue para 213 600 770
Este produto é sujeito a regulamentação especifica.
Em caso de encomenda, será contactado a solicitar documentação complementar necessária e/ou obrigatória (licença, autorização ou declaração de uso final) para a continuidade do pedido. Agradecemos a vossa compreensão
Este produto é sujeito a regulamentação especifica.
Em caso de encomenda, será contactado a solicitar documentação complementar necessária e/ou obrigatória (licença, autorização ou declaração de uso final) para a continuidade do pedido. Agradecemos a vossa compreensão.
Este produto está bloqueado. Para obter mais informações, contacte a VWR através do número 213 600 770.
O produto pretendido já não se encontra disponível. O produto indicado é um substituto.
Este produto encontra-se em rutura de stock. Poderá encontrar alternativas pesquisando pelo código de artigo indicado acima. Se precisar de ajuda, por favor contacte a VWR através do 213 600 770.
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