D2820
Monoclonal Anti-DYNLT3 antibody produced in mouse
~1.0 mg/mL, clone R1, purified immunoglobulin, buffered aqueous solution
Synonym(s):
Anti-Dynein, light chain, Tctex-type-3, Anti-RP3, Anti-TCTE1L, Anti-TCTEX1L
biological source
mouse
Quality Level
conjugate
unconjugated
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
R1, monoclonal
form
buffered aqueous solution
mol wt
antigen ~12.5 kDa
species reactivity
human, rat
concentration
~1.0 mg/mL
technique(s)
immunoprecipitation (IP): suitable
western blot: 2-4 μg/mL using rat brain S1 extract
isotype
IgG2a
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... DYNLT3(6990)
rat ... Dynlt3(363448)
General description
DYNLT3 has been located in both the cytoplasm and the nucleus, in cell- and tissue-specific manners. The subunit binds to SATB1 complex and the activity of this complex is independent of the dynein motor.
Monoclonal Anti-DYNLT3 (mouse IgG2a isotype) is derived from the hybridoma R1 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with rat dynein 3 light chain-myosin basic protein fusion protein. DYNLT3 belongs to the Tctex-light chain family. It is also known as rp3.
Immunogen
rat dynein 3 light chain myosin basic protein fusion protein.
Application
Monoclonal Anti-DYNLT3 antibody produced in mouse has been used in immunoblotting and immunoprecipitation.
Biochem/physiol Actions
Cytoplasmic dynein motor complex is responsible for minus-end, microtubule-based motile processes. It is thus involved in a wide range of eukaryotic cellular processes including trafficking of membranal vesicles, viruses and other intracellular particles. DYNLT3 is a light chain subunit of the complex that binds to Bub3, a spindle checkpoint protein and is depleted from the kinetochore during chromosome alignment. It contributes to dynein cargo binding specificity as dynein binds directly to a component of the spindle checkpoint complex through this light chain. The interaction of the Herpes simplex virus capsid protein VP26 with dynein light chains facilitates the binding of the virus capsid to cytoplasmic dynein during cellular infection.
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.
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Storage Class Code
12 - Non Combustible Liquids
WGK
nwg
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
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Identification of the dynein light chains required for human papillomavirus infection
Schneider MA, et al.
Cellular Microbiology, 13(1), 32-46 (2011)
Mark W Douglas et al.
The Journal of biological chemistry, 279(27), 28522-28530 (2004-05-01)
Cytoplasmic dynein is the major molecular motor involved in minus-end-directed cellular transport along microtubules. There is increasing evidence that the retrograde transport of herpes simplex virus type 1 along sensory axons is mediated by cytoplasmic dynein, but the viral and
K Kevin Pfister et al.
PLoS genetics, 2(1), e1-e1 (2006-01-28)
Cytoplasmic dyneins, the principal microtubule minus-end-directed motor proteins of the cell, are involved in many essential cellular processes. The major form of this enzyme is a complex of at least six protein subunits, and in mammals all but one of
Ting-Yu Yeh et al.
Journal of cell science, 118(Pt 15), 3431-3443 (2005-08-05)
Cytoplasmic dynein is a motor protein complex involved in microtubule-based cargo movement. Previous biochemical evidence suggests that dynein light chain subunits also exist outside the dynein complex. Here we show that the dynein light chain rp3 is present in both
N Hirokawa
Science (New York, N.Y.), 279(5350), 519-526 (1998-02-07)
Cells transport and sort proteins and lipids, after their synthesis, to various destinations at appropriate velocities in membranous organelles and protein complexes. Intracellular transport is thus fundamental to cellular morphogenesis and functioning. Microtubules serve as a rail on which motor
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