Human CHMP4B protein (Recombinant) (N-His-SUMO & C-Strep) (STJP016331)
SPECIFICATIONS
HostE.coli
ImmunogenHomo sapiens (Human)
General Information
| Short Description | Recombinant-Human CHMP4B-N-His-SUMO & C-Strep protein was developed from e.coli for the region N-His-SUMO & C-Strep. For use in research applications. |
| Applications | ELISA/Immunogen/SDS-PAGE/WB |
| Host | E.coli |
| Note | STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
Product Properties
| Dilution Range | Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details. |
| Formulation | Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol. |
| Storage Instruction | Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at-20 to-80°C for twelve months from the date of receipt. |
| Endotoxin | Please contact us for further information. |
Target Information
| Gene Symbol | CHMP4B |
| Gene ID | 128866 |
| Uniprot ID | CHM4B_HUMAN |
| Immunogen | Homo sapiens (Human) |
| Immunogen Region | Asp121-Met224 |
Additional Info
| Post Translational Modifications | ISGylated. Isgylation weakens its interaction with VPS4A. |
| 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. Together with SPAST, the ESCRT-III complex promotes nuclear envelope sealing and mitotic spindle disassembly during late anaphase. Plays a role in the endosomal sorting pathway. ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. When overexpressed, membrane-assembled circular arrays of CHMP4B filaments can promote or stabilize negative curvature and outward budding. CHMP4A/B/C are required for the exosomal release of SDCBP, CD63 and syndecan. Majority of the protein exists in a folded closed conformation. (Microbial infection) The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the budding of enveloped viruses (HIV-1 and other lentiviruses). Via its interaction with PDCD6IP involved in HIV-1 p6- and p9-dependent virus release. |
| Protein Name | Charged Multivesicular Body Protein 4bChromatin-Modifying Protein 4bChmp4bSnf7 Homolog Associated With Alix 1Snf7-2Hsnf7-2Vacuolar Protein Sorting-Associated Protein 32-2Vps32-2Hvps32-2 |
| Database Links | Reactome: R-HSA-162588Reactome: R-HSA-1632852Reactome: R-HSA-5620971Reactome: R-HSA-917729Reactome: R-HSA-9610379Reactome: R-HSA-9615710Reactome: R-HSA-9668328Reactome: R-HSA-9679504Reactome: R-HSA-9694676 |
| Cellular Localisation | CytoplasmCytosolLate Endosome MembranePeripheral Membrane ProteinMidbodyNucleus EnvelopeRecruited To The Nuclear Envelope By Chmp7 During Late AnaphaseLocalizes Transiently To The Midbody Arms Immediately Before Abscission |
| Alternative Protein Names | Charged Multivesicular Body Protein 4b proteinChromatin-Modifying Protein 4b proteinChmp4b proteinSnf7 Homolog Associated With Alix 1 proteinSnf7-2 proteinHsnf7-2 proteinVacuolar Protein Sorting-Associated Protein 32-2 proteinVps32-2 proteinHvps32-2 proteinCHMP4B proteinC20orf178 proteinSHAX1 protein |
Information sourced from Uniprot.org