BBS4 Antibody (Center)
Purified Mouse Monoclonal Antibody (Mab)
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Application ![]()
| WB |
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Primary Accession | Q96RK4 |
Reactivity | Human, Mouse, Rat |
Host | Mouse |
Clonality | Monoclonal |
Calculated MW | 58282 Da |
Isotype | IgG1 |
Antigen Source | HUMAN |
Gene ID | 585 |
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Antigen Region | 1-240 aa |
Other Names | Bardet-Biedl syndrome 4 protein, BBS4 |
Dilution | WB~~1:1000 |
Target/Specificity | This BBS4 antibody is generated from a mice immunized with a recombinant protein between 1-240 amino acids from human BBS4. |
Format | Purified monoclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein G column, followed by dialysis against PBS. |
Storage | Maintain 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. |
Precautions | BBS4 Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | BBS4 |
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Function | The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of the ciliary membrane. The BBSome complex, together with the LTZL1, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation. Required for proper BBSome complex assembly and its ciliary localization. Required for microtubule anchoring at the centrosome but not for microtubule nucleation. May be required for the dynein-mediated transport of pericentriolar proteins to the centrosome. |
Cellular Location | Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cell projection, cilium membrane. Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q8C1Z7}. Cell projection, cilium {ECO:0000250|UniProtKB:Q8C1Z7}. Note=Localizes to the pericentriolar material. Centrosomal localization requires dynein (By similarity) Localizes to the connecting cilium of photoreceptor cells (By similarity). {ECO:0000250|UniProtKB:Q8C1Z7} |
Tissue Location | Ubiquitously expressed. The highest level of expression is found in the kidney |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of the ciliary membrane. The BBSome complex, together with the LTZL1, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation. Required for proper BBSome complex assembly and its ciliary localization. Required for microtubule anchoring at the centrosome but not for microtubule nucleation. May be required for the dynein-mediated transport of pericentriolar proteins to the centrosome.
REFERENCES
Mykytyn K.,et al.Nat. Genet. 28:188-191(2001).
Ye X.,et al.DNA Seq. 15:213-218(2004).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Zody M.C.,et al.Nature 440:671-675(2006).
Badano J.L.,et al.Nature 439:326-330(2006).

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