Product Name: COPZ1 Antibody
Species Reactivity: Human, Mouse
Tested Applications: WB
Applications: For WB starting dilution is: 1:1000
User Note: Optimal dilutions for each application to be determined by the researcher.
Predicted Molecular Weight: 20 kDa
Immunogen: This COPZ1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 24-53 amino acids from the N-terminal region of human COPZ1.
Host Species: Rabbit
Purification: This antibody is purified through a protein A column, followed by peptide affinity purification.
Physical State: Liquid
CAS NO.: 102767-28-2
Product: Levetiracetam
Buffer: Supplied in PBS with 0.09% (W/V) sodium azide.
Concentration: 0.5 mg/ml
Storage Conditions: Store at 4˚C for three months and -20˚C, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.
Clonality: Polyclonal
Conjugate: Unconjugated
Alternate Names: Coatomer subunit zeta-1, Zeta-1-coat protein, Zeta-1 COP, COPZ1, COPZ
Accession NO.: P61923
Protein Ino: 48428830
Official Symbol: COPZ1
Geneid: 22818
Background: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity).The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex.
PubMed ID:http://aac.asm.org/content/36/12/2639.abstract
