Hledali jste: 6-ROX+C2+maleimide

Katalogové číslo: (PRSI30-372)

Dodavatel: ProSci Inc.

Popis: IGFBP7 contains 1 Ig-like C2-type (immunoglobulin-like) domain, 1 IGFBP N-terminal domain and 1 Kazal-like domain. It binds IGF-I and IGF-II with a relatively low affinity. IGFBP7 stimulates prostacyclin (PGI2) production.

Měrná jednotka: 1 * 50 µG

Akce

Katalogové číslo: (PRSI26-227)

Dodavatel: ProSci Inc.

Popis: LRRN3 is a single-pass type I membrane protein. It contains 1 fibronectin type-III domain, 1 Ig-like C2-type (immunoglobulin-like) domain and 12 LRR (leucine-rich) repeats. The function of the LRRN3 protein remains unknown.

Měrná jednotka: 1 * 50 µG

Akce

Katalogové číslo: (ROCK600-401-D87)

Dodavatel: Rockland Immunochemicals

Popis: Anti-NMDA R1, Splice Variant C2' (Rabbit) Antibody is suitable for use in Western Blotting and IHC. Specific conditions for reactivity should be optimized by the end user. Expect a band of approximately 120 kDa in size corresponding to the NMDA receptor.

Měrná jednotka: 1 * 25 µG

Akce

Katalogové číslo: (ROCK600-401-D86)

Dodavatel: Rockland Immunochemicals

Popis: Anti-NMDA R1, Splice Variant C2 (Rabbit) Antibody is suitable for use in Western Blotting and IHC. Specific conditions for reactivity should be optimized by the end user. Expect a band of approximately 120 kDa in size corresponding to the NMDA Receptor.

Měrná jednotka: 1 * 25 µG

Akce

Katalogové číslo: (PRSI30-833)

Dodavatel: ProSci Inc.

Popis: Calcium-dependent membrane-binding proteins may regulate molecular events at the interface of the cell membrane and cytoplasm. This gene is one of several genes that encode a calcium-dependent protein containing two N-terminal type II C2 domains and an integrin A domain-like sequence in the C-terminus.Calcium-dependent membrane-binding proteins may regulate molecular events at the interface of the cell membrane and cytoplasm. This gene is one of several genes that encode a calcium-dependent protein containing two N-terminal type II C2 domains and an integrin A domain-like sequence in the C-terminus.

Měrná jednotka: 1 * 50 µG

Akce

Katalogové číslo: (PRSI56-149)

Dodavatel: ProSci Inc.

Popis: LRRN3 is a single pass type I membrane protein. It contains 1 fibronectin type III domain, 1 Ig like C2 type (immunoglobulin like) domain and 12 LRR (leucine rich) repeats. The function of the LRRN3 protein remains unknown.

Měrná jednotka: 1 * 400 µl

Akce

Katalogové číslo: (BOSSBS-1906R-A488)

Dodavatel: Bioss

Popis: The synaptotagmins are integral membrane proteins of synaptic vesicles thought to serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. Calcium binding to synaptotagmin participates in triggering neurotransmitter release at the synapse. The first C2 domain mediates Ca(2+)-dependent phospholipid binding. The second C2 domain mediates interaction with Stonin 2. Synaptotagmin may have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2.

Měrná jednotka: 1 * 100 µl

Akce

Katalogové číslo: (BOSSBS-1906R-A350)

Dodavatel: Bioss

Popis: The synaptotagmins are integral membrane proteins of synaptic vesicles thought to serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. Calcium binding to synaptotagmin participates in triggering neurotransmitter release at the synapse. The first C2 domain mediates Ca(2+)-dependent phospholipid binding. The second C2 domain mediates interaction with Stonin 2. Synaptotagmin may have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2.

Měrná jednotka: 1 * 100 µl

Akce

Katalogové číslo: (BOSSBS-1906R-A647)

Dodavatel: Bioss

Popis: The synaptotagmins are integral membrane proteins of synaptic vesicles thought to serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. Calcium binding to synaptotagmin participates in triggering neurotransmitter release at the synapse. The first C2 domain mediates Ca(2+)-dependent phospholipid binding. The second C2 domain mediates interaction with Stonin 2. Synaptotagmin may have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2.

Měrná jednotka: 1 * 100 µl

Akce

Katalogové číslo: (BOSSBS-1906R-CY3)

Dodavatel: Bioss

Popis: The synaptotagmins are integral membrane proteins of synaptic vesicles thought to serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. Calcium binding to synaptotagmin participates in triggering neurotransmitter release at the synapse. The first C2 domain mediates Ca(2+)-dependent phospholipid binding. The second C2 domain mediates interaction with Stonin 2. Synaptotagmin may have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2.

Měrná jednotka: 1 * 100 µl

Akce

Katalogové číslo: (BOSSBS-1906R-A555)

Dodavatel: Bioss

Popis: The synaptotagmins are integral membrane proteins of synaptic vesicles thought to serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. Calcium binding to synaptotagmin participates in triggering neurotransmitter release at the synapse. The first C2 domain mediates Ca(2+)-dependent phospholipid binding. The second C2 domain mediates interaction with Stonin 2. Synaptotagmin may have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2.

Měrná jednotka: 1 * 100 µl

Akce

Katalogové číslo: (PRSI91-793)

Dodavatel: ProSci Inc.

Popis: Neurotrimin localizes to the cell membrane and contains three Ig-like C2-type (immunoglobulin-like) domains. Neurotrimin acts as a glycosylphosphatidylinositol (GPI)-anchored neural cell adhesion molecule. Neurotrimin may promote neurite outgrowth and adhesion via homophilic and heterophilic interactions.

Měrná jednotka: 1 * 50 µG

Akce

Katalogové číslo: (BOSSBS-1906R-CY5)

Dodavatel: Bioss

Popis: The synaptotagmins are integral membrane proteins of synaptic vesicles thought to serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. Calcium binding to synaptotagmin participates in triggering neurotransmitter release at the synapse. The first C2 domain mediates Ca(2+)-dependent phospholipid binding. The second C2 domain mediates interaction with Stonin 2. Synaptotagmin may have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2.

Měrná jednotka: 1 * 100 µl

Akce

Katalogové číslo: (BOSSBS-1906R-HRP)

Dodavatel: Bioss

Popis: The synaptotagmins are integral membrane proteins of synaptic vesicles thought to serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. Calcium binding to synaptotagmin participates in triggering neurotransmitter release at the synapse. The first C2 domain mediates Ca(2+)-dependent phospholipid binding. The second C2 domain mediates interaction with Stonin 2. Synaptotagmin may have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2.

Měrná jednotka: 1 * 100 µl

Akce

Katalogové číslo: (BOSSBS-1906R)

Dodavatel: Bioss

Popis: The synaptotagmins are integral membrane proteins of synaptic vesicles thought to serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. Calcium binding to synaptotagmin participates in triggering neurotransmitter release at the synapse. The first C2 domain mediates Ca(2+)-dependent phospholipid binding. The second C2 domain mediates interaction with Stonin 2. Synaptotagmin may have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2.

Měrná jednotka: 1 * 100 µl

Akce

Katalogové číslo: (BOSSBS-1906R-CY5.5)

Dodavatel: Bioss

Popis: The synaptotagmins are integral membrane proteins of synaptic vesicles thought to serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. Calcium binding to synaptotagmin participates in triggering neurotransmitter release at the synapse. The first C2 domain mediates Ca(2+)-dependent phospholipid binding. The second C2 domain mediates interaction with Stonin 2. Synaptotagmin may have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2.

Měrná jednotka: 1 * 100 µl

Akce