Votre recherche pour: FHP+VILEDA+SCS

Référence Produit: (8196-02)

Fournisseur: Avantor

Description: Ces colonnes ont recours aux résines polymères BAKERBOND® DVB issues de la technologie de microparticules polymériques ultra-clean. Ces particules de résine affichent une large surface, elles sont hautement rigides, stables sur une plage de pH allant de 1 à 14, mouillables à l’eau et non impactées par le séchage par absorbant. On recommande de recourir à ces colonnes lorsqu'on utilise des méthodes de détection avancées.

UOM: 1 * 1 Pce

*Promo

Référence Produit: (BOSSBS-9010R-FITC)

Fournisseur: Bioss

Description: DPP6 is a Type-II serine proteinase of the clan SC. The clan SC proteinases have a catalytic triad of Ser-Asp-His, and like other Serine proteinases, the active site serine is in a Gly-Xaa-Ser-Xaa -Gly orientation. DPP6 has an Asp instead of Ser in the catalytic site. DPP6 is a member of a broader family of dipeptidyl peptidases including DPP4, FAP/Seprase, DPP2, DPP8, DPP9, DPP10, which have differing substrate specificity and tissue localizations. The surface-bound DPP6 is a homodimer, and cleavage of in the stalk region releases a shed form of DPP6. The shed is the form found in serum. DPP6 has been found in highest abundance in the brain, but also in the kidney, liver and lung.

UOM: 1 * 100 µl

*Promo

Référence Produit: (BOSSBS-9010R-HRP)

Fournisseur: Bioss

Description: DPP6 is a Type-II serine proteinase of the clan SC. The clan SC proteinases have a catalytic triad of Ser-Asp-His, and like other Serine proteinases, the active site serine is in a Gly-Xaa-Ser-Xaa -Gly orientation. DPP6 has an Asp instead of Ser in the catalytic site. DPP6 is a member of a broader family of dipeptidyl peptidases including DPP4, FAP/Seprase, DPP2, DPP8, DPP9, DPP10, which have differing substrate specificity and tissue localizations. The surface-bound DPP6 is a homodimer, and cleavage of in the stalk region releases a shed form of DPP6. The shed is the form found in serum. DPP6 has been found in highest abundance in the brain, but also in the kidney, liver and lung.

UOM: 1 * 100 µl

*Promo

Fournisseur: Merck

Description: AEBSF hydrochlorure (4-(2-Aminoéthyl)benzènesulfonylfluoride hydrochlorure), Supelco®

Référence Produit: (BOSSBS-9010R-CY3)

Fournisseur: Bioss

Description: DPP6 is a Type-II serine proteinase of the clan SC. The clan SC proteinases have a catalytic triad of Ser-Asp-His, and like other Serine proteinases, the active site serine is in a Gly-Xaa-Ser-Xaa -Gly orientation. DPP6 has an Asp instead of Ser in the catalytic site. DPP6 is a member of a broader family of dipeptidyl peptidases including DPP4, FAP/Seprase, DPP2, DPP8, DPP9, DPP10, which have differing substrate specificity and tissue localizations. The surface-bound DPP6 is a homodimer, and cleavage of in the stalk region releases a shed form of DPP6. The shed is the form found in serum. DPP6 has been found in highest abundance in the brain, but also in the kidney, liver and lung.

UOM: 1 * 100 µl

*Promo

Référence Produit: (BOSSBS-9010R-A555)

Fournisseur: Bioss

Description: DPP6 is a Type-II serine proteinase of the clan SC. The clan SC proteinases have a catalytic triad of Ser-Asp-His, and like other Serine proteinases, the active site serine is in a Gly-Xaa-Ser-Xaa -Gly orientation. DPP6 has an Asp instead of Ser in the catalytic site. DPP6 is a member of a broader family of dipeptidyl peptidases including DPP4, FAP/Seprase, DPP2, DPP8, DPP9, DPP10, which have differing substrate specificity and tissue localizations. The surface-bound DPP6 is a homodimer, and cleavage of in the stalk region releases a shed form of DPP6. The shed is the form found in serum. DPP6 has been found in highest abundance in the brain, but also in the kidney, liver and lung.

UOM: 1 * 100 µl

*Promo

Référence Produit: (BOSSBS-9010R-CY5.5)

Fournisseur: Bioss

Description: DPP6 is a Type-II serine proteinase of the clan SC. The clan SC proteinases have a catalytic triad of Ser-Asp-His, and like other Serine proteinases, the active site serine is in a Gly-Xaa-Ser-Xaa -Gly orientation. DPP6 has an Asp instead of Ser in the catalytic site. DPP6 is a member of a broader family of dipeptidyl peptidases including DPP4, FAP/Seprase, DPP2, DPP8, DPP9, DPP10, which have differing substrate specificity and tissue localizations. The surface-bound DPP6 is a homodimer, and cleavage of in the stalk region releases a shed form of DPP6. The shed is the form found in serum. DPP6 has been found in highest abundance in the brain, but also in the kidney, liver and lung.

UOM: 1 * 100 µl

*Promo

Référence Produit: (BOSSBS-9010R-A647)

Fournisseur: Bioss

Description: DPP6 is a Type-II serine proteinase of the clan SC. The clan SC proteinases have a catalytic triad of Ser-Asp-His, and like other Serine proteinases, the active site serine is in a Gly-Xaa-Ser-Xaa -Gly orientation. DPP6 has an Asp instead of Ser in the catalytic site. DPP6 is a member of a broader family of dipeptidyl peptidases including DPP4, FAP/Seprase, DPP2, DPP8, DPP9, DPP10, which have differing substrate specificity and tissue localizations. The surface-bound DPP6 is a homodimer, and cleavage of in the stalk region releases a shed form of DPP6. The shed is the form found in serum. DPP6 has been found in highest abundance in the brain, but also in the kidney, liver and lung.

UOM: 1 * 100 µl

*Promo

Référence Produit: (BOSSBS-11263R-CY7)

Fournisseur: Bioss

Description: The human complement subcomponent C1q associates with C1r and C1s in order to yield the first component of the serum complement system (SCS). The SCS contains over 30 glycoproteins that influence physiological mechanisms of the body in response to immune complex (the classical pathway), carbohydrate (the lectin pathway) or bacterial (alternative pathway) initiation. C1q binding protein (C1QBP), also designated gC1q-R, p32 (p33) or HABP1 (hyaluronan-binding protein 1), is known to bind the globular heads of C1q molecules and inhibit C1 activation. C1QBP has been described as a complement receptor for C1q on B cells, neutrophils and mast cells. The C1QBP protein may form homodimers. C1QBP is expressed in vascular endothelial cells and has been found to be a multifunctional protein interacting with elements of complement, coagulation and kinin systems. In addition, C1QBP is a subunit of pre-mRNA splicing factor SF2/ASF.

UOM: 1 * 100 µl

*Promo

Référence Produit: (BOSSBS-12333R-A647)

Fournisseur: Bioss

Description: ERMAP is a single-pass type one membrane protein that belongs to the immunoglobulin superfamily. Expressed in cord blood, fetal liver and adult bone marrow, ERMAP is thought to function as a cell adhesion molecule in erythroid cells and is responsible for expression of the Scianna/Radin (Sc/Rd) blood group antigen system. The Sc/Rd system is comprised of seven antigens that are present on the surface of red blood cells and have a variety of functions ranging from protein transport to cell adhesion. These seven blood antigens can differ in their expression within a population and may sometimes differ between mother and child. A fetus expressing different blood antigens than its mother may cause the mother to produce against the fetal blood. This condition is known as hemolytic disease of the newborn (HDN) and is characterized by jaundice, anemia and in some cases, infant death.

UOM: 1 * 100 µl

*Promo

Référence Produit: (BOSSBS-12333R-A680)

Fournisseur: Bioss

Description: ERMAP is a single-pass type one membrane protein that belongs to the immunoglobulin superfamily. Expressed in cord blood, fetal liver and adult bone marrow, ERMAP is thought to function as a cell adhesion molecule in erythroid cells and is responsible for expression of the Scianna/Radin (Sc/Rd) blood group antigen system. The Sc/Rd system is comprised of seven antigens that are present on the surface of red blood cells and have a variety of functions ranging from protein transport to cell adhesion. These seven blood antigens can differ in their expression within a population and may sometimes differ between mother and child. A fetus expressing different blood antigens than its mother may cause the mother to produce against the fetal blood. This condition is known as hemolytic disease of the newborn (HDN) and is characterised by jaundice, anemia and in some cases, infant death.

UOM: 1 * 100 µl

*Promo

Fournisseur: VWR Chemicals

Description: Standard de scandium, Solution étalon de scandium, 1000 mg/l de Sc dans un étalon d'acide nitrique dilué pour AAS AVS TITRINORM®, 1000 mg/L, VWR® AVS TITRINORM, Scandium, Matrice: Nitric acid dil., Applications: Étalons SAA

FDS (Fiche de données de sécurité) Certificats. *Promo

Référence Produit: (M182-500MG)

Fournisseur: VWR Chemicals

Description: AEBSF hydrochlorure (4-(2-Aminoéthyl)benzènesulfonylfluoride hydrochlorure) ≥98%, grade dédié à la protéomique

UOM: 1 * 500 mg

FDS (Fiche de données de sécurité) *Promo

Référence Produit: (BOSSBS-9010R-A680)

Fournisseur: Bioss

Description: DPP6 is a Type-II serine proteinase of the clan SC. The clan SC proteinases have a catalytic triad of Ser-Asp-His, and like other Serine proteinases, the active site serine is in a Gly-Xaa-Ser-Xaa -Gly orientation. DPP6 has an Asp instead of Ser in the catalytic site. DPP6 is a member of a broader family of dipeptidyl peptidases including DPP4, FAP/Seprase, DPP2, DPP8, DPP9, DPP10, which have differing substrate specificity and tissue localisations. The surface-bound DPP6 is a homodimer, and cleavage of in the stalk region releases a shed form of DPP6. The shed is the form found in serum. DPP6 has been found in highest abundance in the brain, but also in the kidney, liver and lung.

UOM: 1 * 100 µl

*Promo

Référence Produit: (BOSSBS-9010R-A350)

Fournisseur: Bioss

Description: DPP6 is a Type-II serine proteinase of the clan SC. The clan SC proteinases have a catalytic triad of Ser-Asp-His, and like other Serine proteinases, the active site serine is in a Gly-Xaa-Ser-Xaa -Gly orientation. DPP6 has an Asp instead of Ser in the catalytic site. DPP6 is a member of a broader family of dipeptidyl peptidases including DPP4, FAP/Seprase, DPP2, DPP8, DPP9, DPP10, which have differing substrate specificity and tissue localizations. The surface-bound DPP6 is a homodimer, and cleavage of in the stalk region releases a shed form of DPP6. The shed is the form found in serum. DPP6 has been found in highest abundance in the brain, but also in the kidney, liver and lung.

UOM: 1 * 100 µl

*Promo

Référence Produit: (BOSSBS-9010R-A750)

Fournisseur: Bioss

Description: DPP6 is a Type-II serine proteinase of the clan SC. The clan SC proteinases have a catalytic triad of Ser-Asp-His, and like other Serine proteinases, the active site serine is in a Gly-Xaa-Ser-Xaa -Gly orientation. DPP6 has an Asp instead of Ser in the catalytic site. DPP6 is a member of a broader family of dipeptidyl peptidases including DPP4, FAP/Seprase, DPP2, DPP8, DPP9, DPP10, which have differing substrate specificity and tissue localisations. The surface-bound DPP6 is a homodimer, and cleavage of in the stalk region releases a shed form of DPP6. The shed is the form found in serum. DPP6 has been found in highest abundance in the brain, but also in the kidney, liver and lung.

UOM: 1 * 100 µl

*Promo