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Recombinant Rat Protein unc-13 homolog A (Unc13a), partial

Recombinant Rat Protein unc-13 homolog A (Unc13a), partial

Code
MSDS	MSDS Datasheet
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Source
Conjugate
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Target Background

Product Details

Abbreviation

Unc13a

Purity

>85% (SDS-PAGE)

Target Names

Unc13a

Uniprot NO.

Q62768

Alternative Names

Unc13a; Unc13h1; Protein unc-13 homolog A; Munc13-1

Species

Rattus norvegicus (Rat)

Source

Yeast

Expression Region

1-1735

Target Protein Sequence

MSLLCVGVKK AKFDGAQEKF NTYVTLKVQN VKSTTIAVRG SQPSWEQDFM FEINRLDLGL TVEVWNKGLI WDTMVGTVWI PLRTIRQSNE EGPGEWLTLD SQAIMADSEI CGTKDPTFHR ILLDAHFELP LDIPEEEARY WAKKLEQLNA MRDQDEYSFQ DQQDKPLPVP SSQCCNWNYF GWGEQNDDPD SAVDDRDSDY RSETSNSIPP PYYTTSQPNA SVHQYSVRPP PLGSRESYSD SMHSYEEFSE PRALSPTGSS RYASSGELSQ GSSQLSEDFD PDEHSLQGSE LDDERDRDSY HSCHSSVSYH KDSPRWDQDE EDLEDLEDLE DEELPEEEEL EEEELEEEEE LEEEELELEE EEEVPDDLAS YTQQEDTTVA EPKEFKRISF PTAAPQKEDK VSAVPIEAPD VSKGIPKAAT PEEKAAAECA QEAEPPKSEE SFRSREAEEG QEGQDAMSRA KANWLRAFNK VRMQLQEARG EGEMSKSLWF KGGPGGGLII IDSMPDIRKR KPIPLVSDLA MSLVQSRKAG ITSALASSTL NNEELKNHVY KKTLQALIYP ISCTTPHNFE VWTATTPTYC YECEGLLWGI ARQGMRCTEC GVKCHEKCQD LLNADCLQRA AEKSSKHGAE DRTQNIIMVL KDRMKIRERN KPEIFELIQE VFAVTKSAHT QQMKAVKQSV LDGTSKWSAK ISITVVCAQG LQAKDKTGSS DPYVTVQVGK TKKRTKTIYG NLNPVWEENF HFECHNSSDR IKVRVLDEDD DIKSRVKQRF KRESDDFLGQ TIIEVRTLSG EMDVWYNLDK RTDKSAVSGA IRLHISVEIK GEEKVAPYHV QYTCLHENLF HFVTDVQNNG VVKIPDAKGD DAWKVYYDET AQEIVDEFAM RYGVESIYQA MTHFACLSSK YMCPGVPAVM STLLANINAY YAHTTASTNV SASDRFAASN FGKERFVKLL DQLHNSLRID LSMYRNNFPA SSPERLQDLK STVDLLTSIT FFRMKVQELQ SPPRASQVVK DCVKACLNST YEYIFNNCHE LYGREYQTDP AKKGEVPPEE QGPSIKNLDF WSKLITLIVS IIEEDKNSYT PCLNQFPQEL NVGKISAEVM WSLFAQDMKY AMEEHDKHRL CKSADYMNLH FKVKWLYNEY VAELPTFKDR VPEYPAWFEP FVIQWLDENE EVSRDFLHGA LERDKKDGFQ QTSEHALFSC SVVDVFSQLN QSFEIIKKLE CPDPQIVGHY MRRFAKTISN VLLQYADIVS KDFASYCSKE KEKVPCILMN NTQQLRVQLE KMFEAMGGKE LDAEASGTLK ELQVKLNNVL DELSHVFATS FQPHIEECVR QMGDILSQVK GTGNVPASAC SSVAQDADNV LQPIMDLLDS NLTLFAKICE KTVLKRVLKE LWKLVMNTME RTIVLPPLTD QTMIGTLLRK HGKGLEKGRV KLPSHSDGTQ MIFNAAKELG QLSKLKDHMV REEAKSLTPK QCAVVELALD TIKQYFHAGG VGLKKTFLEK SPDLQSLRYA LSLYTQATDL LIKTFVQTQS AQVHGGKGTR FTLSEDVCPE MGSGVEDPVG EVSVHVELFT HPGTGEQKVT VKVVAANDLK WQTSGIFRPF IEVNIVGPQL SDKKRKFATK SKNNSWAPKY NESFQFSLSA DAGPECYELQ VCVKDYCFAR EDRTVELAVL QLRELAQRGS AACWLPLGRR IHMDDTGLTV LRILSQRSND EVAKEFVKLK SDTRSAEEGG AAPAP
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Protein Length

Partial

Tag Info

N-terminal His-tagged/Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Storage Condition

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Shelf Life

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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Target Background

Function(From Uniprot)

Plays a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. Involved in neurotransmitter release by acting in synaptic vesicle priming prior to vesicle fusion and participates in the activity-dependent refilling of readily releasable vesicle pool (RRP). Essential for synaptic vesicle maturation in most excitatory/glutamatergic but not inhibitory/GABA-mediated synapses. Facilitates neuronal dense core vesicles fusion as well as controls the location and efficiency of their synaptic release. Also involved in secretory granule priming in insulin secretion. Plays a role in dendrite formation by melanocytes.

Gene References into Functions

These results suggested that Munc13-1 has an inhibitory role in antigen-induced mast cell degranulation, which is performed in a Munc13-4-dependent manner. PMID:29225210
W22A, W22K, W22D, W22Y, and W22F substitutions were made in Munc13-1. The GFP-tagged constructs were expressed in Neuro-2a cells. Their membrane translocation in response to phorbol ester was observed in live cells by confocal microscopy. Munc13-1 translocated to the plasma membrane, the C1 domain translocated to internal membranes in response to phorbol ester. Trp-588 is important for ligand binding and translocation. PMID:29244485
The structure imposes key constraints for models of neurotransmitter release and suggests that Munc13-1 bridges the vesicle and plasma membranes from the periphery of the membrane-membrane interface. PMID:28177287
Overall, these results support a model whereby the multiple domains of Munc13 cooperate to coordinate synaptic vesicle docking, priming and fusion. PMID:27213521
Here, the authors identified two conserved residues (R151, I155) in the syntaxin-1 linker region as key sites for the Munc13-1 MUN domain interaction. This interaction is essential for SNARE complex formation in vitro and synaptic vesicle priming in neuronal cultures. PMID:28137749
The crystal structure of the rat Munc13-1 MUN domain now reveals an elongated, arch-shaped architecture formed by alpha-helical bundles, with a highly conserved hydrophobic pocket in the middle. PMID:26030875
The C-terminal module of Munc13-1 is important for Munc13 function, but full activity requires adjacent modules. PMID:22000513
The Munc13-1 MUN domain markedly accelerates the transition from the syntaxin-1-Munc18-1 complex to the SNARE complex. PMID:21499244
metabotropic glutamate receptor mGlu7 activates phospholipase C, translocates munc-13-1 protein, and potentiates glutamate release at cerebrocortical nerve terminals PMID:20375012
Data suggest that, during repeated action potentials, Ca(2+) and phosphatidylinositolphosphate binding to the Munc13 C(2)B domain potentiate synaptic vesicle exocytosis, thereby offsetting synaptic depression induced by vesicle depletion. PMID:20154707
Presynaptic silencing was accompanied by decreases in levels of the priming proteins Munc13-1 and Rim1. PMID:20130189
Munc13-1 regulates insulin exocytosis PMID:12871971
A conserved tryptophan residue occludes the diacylglycerol/phorbol ester-binding site in the munc13-1 C1 domain, and as a consequence, the munc13-1 C1 domain requires a considerable conformational change for ligand binding. PMID:15667202
Study shows that the Munc13-1 C(2)A domain homodimerizes, and that homodimerization competes with Munc13-1/RIM heterodimerization. PMID:16732694
Expression, purification and characterization of critical domains of Munc13-1 are reported. PMID:17687497
Munc13s may provide a template to assemble syntaxin-1/SNAP-25 heterodimers, leading to an acceptor complex for synaptobrevin PMID:18201107
These results suggest that Munc13-1 exists in pancreas islets during fetus development and its deficiency in the pancreas, as occurs in IUGR, was in accordance with decreased blood insulin level. PMID:18787382

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Subcellular Location

Cytoplasm. Cell membrane; Peripheral membrane protein. Cell junction, synapse, presynaptic cell membrane; Peripheral membrane protein. Cell junction, synapse, presynaptic active zone. Note=Translocated to the plasma membrane in response to phorbol ester binding.

Protein Families

Unc-13 family

Tissue Specificity

Expressed in brain, with highest levels in the olfactory bulb, striatum, cerebral cortex, hippocampus and cerebellum. Also expressed in pancreatic islet cells.

Database Links

UNIGENE: Rn.10126

KEGG: rno:64829

STRING: 10116.ENSRNOP00000025162

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