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ELISA Kit for Rat Dysbindin

SKU : BHE13803646

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EIAAB SCIENCE INC, WUHAN

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Mfr.No.	E14962r
Alternative Names	Biogenesis of lysosome-related organelles complex 1 subunit 8 ; BLOC-1 subunit 8 ; Dysbindin-1 ; Dystrobrevin-binding protein 1 ; Bloc1s8
Categories	Elisa
Function	The BLOC-1 complex is required for normal biogenesis of lysosome-related organelles, such as platelet dense granules and melanosomes. Plays a role in intracellular vesicle trafficking. Plays a role in synaptic vesicle trafficking and in neurotransmitter release. May be required for normal dopamine homeostasis in the cerebral cortex, hippocampus, and hypothalamus. Plays a role in the regulation of cell surface exposure of DRD2. Contributes to the regulation of dopamine signaling. May play a role in actin cytoskeleton reorganization and neurite outgrowth. May modulate MAPK8 phosphorylation.
Specificity	Natural and recombinant Rat Dysbindin
Subcellular Location	Cytoplasm Cytoplasmic vesicle membrane Peripheral membrane protein Cytoplasmic side Cytoplasmic vesicle secretory vesicle synaptic vesicle membrane Peripheral membrane protein Cytoplasmic side Endosome membrane Peripheral membrane protein Cytoplasmic side Melanosome membrane Peripheral membrane protein Cytoplasmic side Nucleus Cell junction synapse postsynaptic cell membrane postsynaptic density Endoplasmic reticulum Detected at axon terminals and in dendrites. Detected at synapses, at post-synaptic density, at pre-synaptic vesicle membranes and microtubules. Detected at tubulovesicular elements in the vicinity of the Golgi apparatus and of melanosomes. Detected in neuron cell bodies, axons and dendrites. Detected at axon growth cones.
Detection Range	78-5000pg/mL
Entryname	DTBP1_RAT
Method Type	Sandwich
Platform	PF04440
Protein Name	Dysbindin
Sensitivity	29pg/mL
Sequence	50: MLETLRERLL ; SVQQDFTSGL ; KTLSDKSKEA ; KVKSRPRTAP ; YLPKYSAGLD ; 100: LLSRYEDTWA ; ALHRRAKECA ; DAGELVDSEV ; VMLSAHWEKK ; RTSLAELQEQ ; 150: LQQLPALLQD ; VESLMASLAH ; LETSFEEVEN ; HLLHLEDLCG ; QCELERHKQA ; 200: HARHLEDYKK ; SKRKELEAFK ; AELDTEHAQK ; ILEMEHTQQL ; KLKERQKFFE ; 250: EAFQQDMEQY ; LSTGHLQIAE ; RREPMGSMSS ; MEVNVDVLEQ ; MDLMDLSDQE ; 300: ALDVFLNSGG ; EDNTVISPGL ; EMESNPSQNE ; MNLQIPNPSE ; SASQPPASPS ; 350: ACTDLDTADA ; PLIQADEEEV ; QVDTALVTLN ; TDRKSTPGVS ; DDSDQCDSTQ ; 352: DI
Sequence Length	352
Sub Unit	Part of the biogenesis of lysosome-related organelles complex 1 (BLOC-1). The BLOC-1 complex is composed of BLOC1S1, BLOC1S2, BLOC1S3, DTNBP1, MUTED, PLDN, CNO/cappuccino and SNAPIN. Binds to DTNA and DTNB but may not be a physiological binding partner (PubMed:16448387). Interacts with RNF151, CMYA5, TRIM32 and AP3B2. Identified in a complex with the biogenesis of lysosome-related organelles complex 2 (BLOC-2). Interacts with the DNA-dependent protein kinase complex DNA-PK (By similarity). Identified in a complex with the adapter-related protein complex 3 (AP-3). Interacts with AP3M1.

Uniprot	Q5M834
Gene Name	Dtnbp1
Immunogen Species	Rattus norvegicus (Rat)
Kegg	rno:641528
Unigene	Rn.187290

Reference	1. "Identification of novel E2F1 target genes regulated in cell cycle-dependent and independent manners." Iwanaga R., Komori H., Ishida S., Okamura N., Nakayama K., Nakayama K., Ohtani K. Oncogene25:1786-1798(2006) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] 2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res.14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] tissue: Spleen. 3. "Dysbindin, a novel coiled-coil-containing protein that interacts with the dystrobrevins in muscle and brain." Benson M.A., Newey S.E., Martin-Rendon E., Hawkes R., Blake D.J. J. Biol. Chem.276:24232-24241(2001) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: TISSUE SPECIFICITY;INTERACTION WITH DTNA AND DTNB 4. "Reinvestigation of the dysbindin subunit of BLOC-1 (biogenesis of lysosome-related organelles complex-1) as a dystrobrevin-binding protein." Nazarian R., Starcevic M., Spencer M.J., Dell'Angelica E.C. Biochem. J.395:587-598(2006) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION;TISSUE SPECIFICITY;INTERACTION WITH DTNA; DTNB AND BLOC1S6 5. "BLOC-1 complex deficiency alters the targeting of adaptor protein complex-3 cargoes." Salazar G., Craige B., Styers M.L., Newell-Litwa K.A., Doucette M.M., Wainer B.H., Falcon-Perez J.M., Dell'Angelica E.C., Peden A.A., Werner E., Faundez V. Mol. Biol. Cell17:4014-4026(2006) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: IDENTIFICATION IN THE BLOC-1 COMPLEX;FUNCTION;IDENTIFICATION BY MASS SPECTROMETRY 6. "Evidence that the BLOC-1 protein dysbindin modulates dopamine D2 receptor internalization and signaling but not D1 internalization." Iizuka Y., Sei Y., Weinberger D.R., Straub R.E. J. Neurosci.27:12390-12395(2007) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION 7. "Dysbindin-1 and its protein family with special attention to the potential role of dysbindin-1 in neuronal functions and the pathophysiology of schizophrenia." Talbot K., Ong W.-Y., Blake D.J., Tang J., Louneva N., Carlson G.C., Arnold S.E. [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: REVIEW 8. "Hermansky-Pudlak syndrome protein complexes associate with phosphatidylinositol 4-kinase type II alpha in neuronal and non-neuronal cells." Salazar G., Zlatic S., Craige B., Peden A.A., Pohl J., Faundez V. J. Biol. Chem.284:1790-1802(2009) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: IDENTIFICATION IN A COMPLEX WITH AP-3 COMPLEX 9. "Direct interaction of dysbindin with the AP-3 complex via its mu subunit." Taneichi-Kuroda S., Taya S., Hikita T., Fujino Y., Kaibuchi K. Neurochem. Int.54:431-438(2009) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH AP3M1;FUNCTION;TISSUE SPECIFICITY;SUBCELLULAR LOCATION

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