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>   首页   >   产品   >   一抗   >   微生物学   >   CHMP6 Antibody (N-term)   

CHMP6 Antibody (N-term)

Affinity Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - CHMP6 Antibody (N-term) AP12454a
    Western blot analysis of lysate from human spleen tissue lysate, using CHMP6 Antibody (N-term)(Cat. #AP12454a). AP12454a was diluted at 1:1000 at each lane. A goat anti-rabbit IgG H&L(HRP) at 1:5000 dilution was used as the secondary antibody. Lysate at 35ug per lane.
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, E
Primary Accession Q96FZ7
Other Accession NP_078867.2
Reactivity Human
Host Rabbit
Clonality Polyclonal
Isotype Rabbit IgG
Calculated MW 23485 Da
Antigen Region 1-30 aa
Additional Information
Gene ID 79643
Other Names Charged multivesicular body protein 6, Chromatin-modifying protein 6, Vacuolar protein sorting-associated protein 20, Vps20, hVps20, CHMP6, VPS20
Target/Specificity This CHMP6 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 1-30 amino acids from the N-terminal region of human CHMP6.
Dilution WB~~1:1000
E~~Use at an assay dependent concentration.
Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.
StorageMaintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsCHMP6 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name CHMP6
Synonyms VPS20
Function Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. In the ESCRT-III complex, it probably serves as an acceptor for the ESCRT-II complex on endosomal membranes.
Cellular Location Endomembrane system. Endosome membrane; Lipid- anchor. Late endosome membrane. Membrane; Lipid-anchor. Note=Localizes to endosomal membranes
Tissue Location Ubiquitously expressed.
Research Areas

For Research Use Only. Not For Use In Diagnostic Procedures.

BACKGROUND

CHMP6 belongs to the chromatin-modifying protein/charged multivesicular body protein (CHMP) family. These proteins are components of ESCRT-III (endosomal sorting complex required for transport III), a complex involved in degradation of surface receptor proteins and formation of endocytic multivesicular bodies (MVBs). Some CHMPs have both nuclear and cytoplasmic/vesicular distributions, and one such CHMP, CHMP1A (MIM 164010), is required for both MVB formation and regulation of cell cycle progression (Tsang et al., 2006 [PubMed 16730941]).

REFERENCES

Im, Y.J., et al. Dev. Cell 17(2):234-243(2009)
Fu, D., et al. Biosci. Biotechnol. Biochem. 73(3):494-501(2009)
Kieffer, C., et al. Dev. Cell 15(1):62-73(2008)
Lamesch, P., et al. Genomics 89(3):307-315(2007)
Ewing, R.M., et al. Mol. Syst. Biol. 3, 89 (2007) :

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