protein

Recombinant Human Synaptotagmin-1

MBS962491

0.05 mg (E-Coli)

190 USD

Recombinant Protein

Recombinant Human Synaptotagmin-1

Synaptotagmin-1

Synaptotagmin I; SytIp65

synaptotagmin-1 isoform 1; Synaptotagmin-1; synaptotagmin-1; synaptotagmin 1; Synaptotagmin I; SytI; p65

SYT1

SYT1; SYT1; P65; SYT; SVP65; SVP65; SYT; SytI

SYT1_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

99-416

422

KNAINMKDVKDLGKTMKDQALKDDDAETGLTDGEEKEEP
KEEEKLGKLQYSLDYDFQNNQLLVGIIQAAELPALDMGG
TSDPYVKVFLLPDKKKKFETKVHRKTLNPVFNEQFTFKV
PYSELGGKTLVMAVYDFDRFSKHDIIGEFKVPMNTVDFG
HVTEEWRDLQSAEKEEQEKLGDICFSLRYVPTAGKLTVV
ILEAKNLKKMDVGGLSDPYVKIHLMQNGKRLKKKKTTIK
KNTLNPYYNESFSFEVPFEQI

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Neuroscience

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 Ca2+-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 Ca2+-independent manner; these are neurexins, syntaxin and AP2.

Structural and functional conservation of synaptotagmin (p65) in Drosophila and humans.Perin M.S., Johnston P.A., Oezcelik T., Jahn R., Francke U., Suedhof T.C.J. Biol. Chem. 266:615-622(1991) Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. Genet. 36:40-45(2004) The full-ORF clone resource of the German cDNA consortium.Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.BMC Genomics 8:399-399(2007) Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Human SCAMP5, a novel secretory carrier membrane protein, facilitates calcium-triggered cytokine secretion by interaction with SNARE machinery.Han C., Chen T., Yang M., Li N., Liu H., Cao X.J. Immunol. 182:2986-2996(2009) System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.Sci. Signal. 4:RS3-RS3(2011) Identification of a human synaptotagmin-1 mutation that perturbs synaptic vesicle cycling.Baker K., Gordon S.L., Grozeva D., van Kogelenberg M., Roberts N.Y., Pike M., Blair E., Hurles M.E., Chong W.K., Baldeweg T., Kurian M.A., Boyd S.G., Cousin M.A., Raymond F.L.J. Clin. Invest. 0:0-0(2015)

209447070

NP_001129277.1

NM_001135805.1

P21579

40.4kD

Acetylcholine Neurotransmitter Release Cycle Pathway (1268773); Disease Pathway (1268854); Dopamine Neurotransmitter Release Cycle Pathway (1268772); Effects Of Botulinum Toxin Pathway (138028); GABA Synthesis, Release, Reuptake And Degradation Pathway (1268774); Glutamate Neurotransmitter Release Cycle Pathway (1268771); Infectious Disease Pathway (1269056); Neuronal System Pathway (1268763); Neurotoxicity Of Clostridium Toxins Pathway (1269145); Neurotransmitter Release Cycle Pathway (1268768)

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-1 participates in triggering neurotransmitter release at the synapse (Fernandez-Chacon et al., 2001 [PubMed 11242035]).[supplied by OMIM, Jul 2010]

SYT1: an integral membrane protein of synaptic vesicles thought to serve as a Ca(2+) sensor in the process of vesicular trafficking and exocytosis. Calcium binding to synaptotagmin I participates in triggering neurotransmitter release at the synapse. 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. Protein type: Vesicle; Calcium-binding; Membrane protein, integral. Chromosomal Location of Human Ortholog: 12cen-q21. Cellular Component: cell junction; excitatory synapse; integral to membrane; neuron projection; plasma membrane; presynaptic membrane; SNARE complex; synaptic vesicle; synaptic vesicle membrane; terminal button. Molecular Function: calcium ion binding; calcium-dependent phospholipid binding; calcium-dependent protein binding; calmodulin binding; clathrin binding; identical protein binding; low-density lipoprotein receptor binding; phosphatidylinositol binding; phosphatidylinositol-4,5-bisphosphate binding; phosphatidylserine binding; protein binding; protein C-terminus binding; SNARE binding; syntaxin-1 binding. Biological Process: brain development; detection of calcium ion; glutamate secretion; neurotransmitter secretion; positive regulation of calcium ion-dependent exocytosis; positive regulation of synaptic transmission; positive regulation of vesicle fusion; protein homooligomerization; regulation of exocytosis; regulation of synaptic transmission, glutamatergic; synaptic transmission; synaptic vesicle endocytosis; vesicle docking

0.05 mg (E-Coli)

190 USD

0.2 mg (E-Coli)

460

0.5 mg (E-Coli)

750

0.05 mg (Baculovirus)

1105

1 mg (E-Coli)

1180