M6194
Monoclonal Anti-Munc13/1 antibody produced in mouse
~2 mg/mL, clone Munc13-71, purified immunoglobulin, buffered aqueous solution
Sign Into View Organizational & Contract Pricing
All Photos(1)
About This Item
Recommended Products
biological source
mouse
conjugate
unconjugated
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
Munc13-71, monoclonal
form
buffered aqueous solution
species reactivity
rat, mouse
concentration
~2 mg/mL
technique(s)
microarray: suitable
western blot: 1-2 μg/mL using cytosolic rat brain S1 fraction
isotype
IgG2b
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
mouse ... Unc13a(382018)
rat ... Unc13a(64829)
General description
Monoclonal Anti-Munc13-1 (mouse IgG2b isotype) is derived from the hybridoma Munc13-71 produced by the fusion of mouse myeloma cells (NS1 cells) and splenocytes from BALB/c mice immunized with a synthetic peptide of rat Munc13-1, conjugated to KLH. Protein unc-13 homolog A (Munc13-1) contains a diacylglycerol (DAG)/b phorbol ester-binding C1 domain. Munc13-1 are expression in axon is observed at various synapse populations.
Munc13/1 is a diacylglycerol receptor which is expressed in the presynaptic area.
Immunogen
synthetic peptide corresponding to amino acid 10-27 of rat munc13/1, conjugated to KLH.
Application
Monoclonal Anti-Munc13/1 antibody produced in mouse has been used in enzyme linked immunosorbent assay (ELISA) and immunoblotting.
Biochem/physiol Actions
Munc13/1 has a crucial role in synaptic vesicle priming. It interacts with Syntaxin 1A and helps it to bind to soluble NSF attachment protein receptor (SNARE) proteins. Thus it contributes to the stability of the SNARE complex. Deletion of Munc13/1 leads to complete arrest synaptic transmission.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Not finding the right product?
Try our Product Selector Tool.
Storage Class Code
10 - Combustible liquids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
ELKS/Voltage-dependent Ca2+ channel-beta subunit module regulates polarized Ca2+ influx in pancreatic beta cells
Ohara-Imaizumi M, et al.
Testing, 26(5), 1213-1226 (2019)
Differential control of vesicle priming and short-term plasticity by Munc13 isoforms
Rosenmund C, et al.
Neuron, 33(3), 411-424 (2002)
Edwin P Kwan et al.
Diabetes, 55(5), 1421-1429 (2006-04-29)
Munc13-1 is a diacylglycerol (DAG) receptor that is essential for synaptic vesicle priming. We recently showed that Munc13-1 is expressed in rodent and human islet beta-cells and that its levels are reduced in islets of type 2 diabetic humans and
Lijun Kang et al.
Cell metabolism, 3(6), 463-468 (2006-05-16)
Munc13-1 is a presynaptic protein that is essential for synaptic vesicle priming. Deletion of Munc13-1/unc13 causes total arrest of synaptic transmission due to a complete loss of fusion-competent synaptic vesicles. The requirement of Munc13-1 for large dense-core vesicles (LDCVs), however
Stefan Kalla et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 26(50), 13054-13066 (2006-12-15)
GFP (green fluorescent protein) fusion proteins have revolutionized research on protein dynamics at synapses. However, corresponding analyses usually involve protein expression methods that override endogenous regulatory mechanisms, and therefore cause overexpression and temporal or spatial misexpression of exogenous fusion proteins
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service