Votre recherche pour: phusion

Référence Produit: (USBIR1600-02)

Fournisseur: US Biological

Description: Anti-Respiratory Syncytial Virus, Fusion Protein Mouse Monoclonal Antibody [clone: 5E414]

UOM: 1 * 1 mL

*Promo

Fournisseur: VWR Chemicals

Description: Agarose high resolution is optimised to give exceptional separation on agarose of nucleic acid fragments below 1000 base pairs, and differing by only a few base pairs. It retains the low gelling characteristics of the standard Agarose HR, and offers significantly increased gel strength at the expense of a higher melting temperature. This results in gels which are flexible and easy to handle. These properties make it the agarose of choice for analytical gel separations to check the quality and size of amplified fragments, and for use in restriction mapping involving small digestion fragments.

FDS (Fiche de données de sécurité) Certificats.

Référence Produit: (ABCAAB302788-100)

Fournisseur: Abcam

Description: Anti-N-ethylmaleimide-sensitive fusion protein Rabbit Monoclonal Antibody [clone: EPR25190-1]

UOM: 1 * 100 µl

*Promo

Fournisseur: Abcam

Description: Anti-N-ethylmaleimide-sensitive fusion protein Rabbit Monoclonal Antibody [clone: EPR25190-1]

New Product

Fournisseur: Abcam

Description: Anti-Metapneumovirus Fusion Protein Rabbit Monoclonal Antibody [clone: EPR29365-579]

New Product

Fournisseur: Abcam

Description: Anti-Metapneumovirus Fusion Protein Rabbit Monoclonal Antibody [clone: EPR29365-579]

New Product

Référence Produit: (1086006.)

Fournisseur: USP

Description: USP Reference Standards are specified for use in conducting official USP–NF tests and assays. To confirm accuracy and reproducibility, USP Reference Standards are rigorously tested and evaluated by multiple independent laboratories including USP, commercial, regulatory, and academic labs. USP also provide publicly available, official documentary standards for pharmaceutical ingredients in the USP–NF that link directly with our primary reference standards.

UOM: 1 * 1 g

Certificats. *Promo

Référence Produit: (BOSSBS-0886R-FITC)

Fournisseur: Bioss

Description: Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (F protein) probably interacts with H at the virion surface. Upon HN binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis (By similarity).

UOM: 1 * 100 µl

*Promo

Référence Produit: (BOSSBS-0886R-HRP)

Fournisseur: Bioss

Description: Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (F protein) probably interacts with H at the virion surface. Upon HN binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis (By similarity).

UOM: 1 * 100 µl

*Promo

Référence Produit: (USBIR1600-08-100)

Fournisseur: US Biological

Description: Anti-Respiratory Syncytial Virus, Bovine, Fusion Protein F1 Rabbit Polyclonal Antibody

UOM: 1 * 100 µG

*Promo

Référence Produit: (USBIR1595-36C)

Fournisseur: US Biological

Description: Anti-Respiratory Syncytial Virus, Fusion Protein A,B Mouse Monoclonal Antibody [clone: 10F367]

UOM: 1 * 100 µG

*Promo

Référence Produit: (USBIR1600-17J)

Fournisseur: US Biological

Description: Anti-Respiratory Syncytial Virus, Fusion Protein A,B Mouse Monoclonal Antibody [clone: 5E420]

UOM: 1 * 1 mL

*Promo

Référence Produit: (USBIR1600-17)

Fournisseur: US Biological

Description: Anti-Respiratory Syncytial Virus, A,B, Fusion Protein Mouse Monoclonal Antibody [clone: 5E418]

UOM: 1 * 1 mL

*Promo

Référence Produit: (USBIR1600-17E)

Fournisseur: US Biological

Description: Anti-Respiratory Syncytial Virus, Fusion Protein A,B Mouse Monoclonal Antibody [clone: 5E419]

UOM: 1 * 1 mL

*Promo

Référence Produit: (BOSSBS-0886R-A350)

Fournisseur: Bioss

Description: Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (F protein) probably interacts with H at the virion surface. Upon HN binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis (By similarity).

UOM: 1 * 100 µl

*Promo

Référence Produit: (BOSSBS-0886R-A647)

Fournisseur: Bioss

Description: Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (F protein) probably interacts with H at the virion surface. Upon HN binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis (By similarity).

UOM: 1 * 100 µl

*Promo