Sie suchten nach: 2-[(Cyclopropylcarbonyl)amino]-5-hydroxybenzoic acid

Beschreibung: Binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction. Promotes Arg-Gly-Asp-dependent cell attachment.

Artikel-Nr: BOSSBS-2668R-A647

UOM: 1 * 100 µl

Lieferant: Bioss

Aktion

Beschreibung: KIF13B is also known as Kinesin-like protein GAKIN or GAKIN and is a 1,826 amino acid protein that is widely expressed in tissues, with highest expression in brain and kidney. KIF13B is localized to the cytoplasm, as well as to the cytoskeleton, and is thought to be a microtubule-dependent motor protein which is able to bind to a variety of proteins in order to traffic them to various locations throughout the cell. KIF13B belongs to the kinesin-like protein family and possesses three domains typical of the kinesin-like protein family, namely an N-terminal motor domain with an ATP-binding motif, an FHA domain which is known to bind diverse cargos and a large stalk domain involved in protein-protein binding. Additionally, KIF13B has a microtubule-interacting sequence which is known as the CAP-Gly domain at its C-terminus. The CAP-Gly domain is highly conserved domain among eukaryotes, and in humans, defects in the CAP-Gly domain are implicated in many diseases affecting the trafficking of vesicles, neuromuscular junctions and lysosome proliferation.

Artikel-Nr: BOSSBS-12387R-A647

UOM: 1 * 100 µl

Lieferant: Bioss

Aktion

Beschreibung: KIF13B is also known as Kinesin-like protein GAKIN or GAKIN and is a 1,826 amino acid protein that is widely expressed in tissues, with highest expression in brain and kidney. KIF13B is localized to the cytoplasm, as well as to the cytoskeleton, and is thought to be a microtubule-dependent motor protein which is able to bind to a variety of proteins in order to traffic them to various locations throughout the cell. KIF13B belongs to the kinesin-like protein family and possesses three domains typical of the kinesin-like protein family, namely an N-terminal motor domain with an ATP-binding motif, an FHA domain which is known to bind diverse cargos and a large stalk domain involved in protein-protein binding. Additionally, KIF13B has a microtubule-interacting sequence which is known as the CAP-Gly domain at its C-terminus. The CAP-Gly domain is highly conserved domain among eukaryotes, and in humans, defects in the CAP-Gly domain are implicated in many diseases affecting the trafficking of vesicles, neuromuscular junctions and lysosome proliferation.

Artikel-Nr: BOSSBS-12387R-A350

UOM: 1 * 100 µl

Lieferant: Bioss

Aktion

Beschreibung: KIF13B is also known as Kinesin-like protein GAKIN or GAKIN and is a 1,826 amino acid protein that is widely expressed in tissues, with highest expression in brain and kidney. KIF13B is localized to the cytoplasm, as well as to the cytoskeleton, and is thought to be a microtubule-dependent motor protein which is able to bind to a variety of proteins in order to traffic them to various locations throughout the cell. KIF13B belongs to the kinesin-like protein family and possesses three domains typical of the kinesin-like protein family, namely an N-terminal motor domain with an ATP-binding motif, an FHA domain which is known to bind diverse cargos and a large stalk domain involved in protein-protein binding. Additionally, KIF13B has a microtubule-interacting sequence which is known as the CAP-Gly domain at its C-terminus. The CAP-Gly domain is highly conserved domain among eukaryotes, and in humans, defects in the CAP-Gly domain are implicated in many diseases affecting the trafficking of vesicles, neuromuscular junctions and lysosome proliferation.

Artikel-Nr: BOSSBS-12387R-A555

UOM: 1 * 100 µl

Lieferant: Bioss

Aktion

Beschreibung: N-(tert-Butoxycarbonyl)-L-propargylglycine 97%

Artikel-Nr: APOSOR14674-25G

UOM: 1 * 25 g

Lieferant: Apollo Scientific

Aktion

Beschreibung: Ethyl-N-{[(2-methyl-2-propanyl)oxy]carbonyl}glycinat

Artikel-Nr: APOSOR110664-100G

UOM: 1 * 100 g

Lieferant: Apollo Scientific

Aktion

Beschreibung: Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3beta in vitro. Involved in the formation of the fibrovascular tissues in association with MMP14. PEX, the C-terminal non-catalytic fragment of MMP2, posseses anti-angiogenic and anti-tumor properties and inhibits cell migration and cell adhesion to FGF2 and vitronectin. Ligand for integrinv/beta3 on the surface of blood vessels. MMP2 isoform 2 mediates the proteolysis of CHUK/IKKA and initiates a primary innate immune response by inducing mitochondrial-nuclear stress signaling with activation of the pro-inflammatory NF-kappaB, NFAT and IRF transcriptional pathways. Catalytic activity of MMP2 causes cleavage of gelatin type I and collagen types IV, V, VII, X. Cleaves the collagen-like sequence Pro-Gln-Gly-|-Ile-Ala-Gly-Gln. (Ref: uniprot.org).

Artikel-Nr: BSENR-1381-100

UOM: 1 * 100 µG

Lieferant: Biosensis

Aktion

Beschreibung: 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.

Artikel-Nr: BOSSBS-9010R

UOM: 1 * 100 µl

Lieferant: Bioss

Aktion

Beschreibung: 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.

Artikel-Nr: BOSSBS-9010R-CY7

UOM: 1 * 100 µl

Lieferant: Bioss

Aktion

Beschreibung: 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.

Artikel-Nr: BOSSBS-9010R-A488

UOM: 1 * 100 µl

Lieferant: Bioss

Aktion

Beschreibung: Binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction. Promotes Arg-Gly-Asp-dependent cell attachment.

Artikel-Nr: BOSSBS-2668R-A488

UOM: 1 * 100 µl

Lieferant: Bioss

Aktion

Beschreibung: Binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction. Promotes Arg-Gly-Asp-dependent cell attachment.

Artikel-Nr: BOSSBS-2668R-FITC

UOM: 1 * 100 µl

Lieferant: Bioss

Aktion

Beschreibung: 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.

Artikel-Nr: BOSSBS-9010R-A555

UOM: 1 * 100 µl

Lieferant: Bioss

Aktion

Beschreibung: 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.

Artikel-Nr: BOSSBS-9010R-CY5.5

UOM: 1 * 100 µl

Lieferant: Bioss

Aktion

Beschreibung: 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.

Artikel-Nr: BOSSBS-9010R-A647

UOM: 1 * 100 µl

Lieferant: Bioss

Aktion

Beschreibung: 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.

Artikel-Nr: BOSSBS-9010R-FITC

UOM: 1 * 100 µl

Lieferant: Bioss

Aktion