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32-3531

CHMP4A Recombinant Protein

Abeomics

DETAILS

  • Amino Acid: MGSSHHHHHH SSGLVPRGSH MSRRRPEDGL GKAGPCVMRH HPPRSKAEVW RTLRGGGGRG ELAMSGLGRL FGKGKKEKGP TPEEAIQKLK ETEKILIKKQ EFLEQKIQQE LQTAKKYGTK NKRAALQALR RKKRFEQQLA QTDGTLSTLE FQREAIENAT TNAEVLRTME LAAQSMKKAY QDMDIDKVDE LMTDITEQQE VAQQISDAIS RPMGFGDDVD EDELLEELEE LEQEELAQEL LNVGDKEEEP SVKLPSVPST HLPAGPAPKV DEDEEALKQL AEWVS
  • Purification: Greater than 90% as determined by SDS-PAGE.
  • Product Content: The CHMP4A solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 200mM NaCl, 0.1mMPMSF, 1mM EDTA, 2mM DTT and 50% glycerol.
  • Alternative Name: Charged multivesicular body protein 4A||C14orf123||HSPC134||VPS32A||Vacuolar protein sorting-associated protein 32-1||chromatin modifying protein 4A||SHAX2||SNF7-1||SNF7 homolog associated with Alix-2||chromosome 14 open reading frame 123||CHMP4B||
  • Storage Condition: Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

DESCRIPTION

Source : E.coli. CHMP4A Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 285 amino acids (1-265 and having a molecular mass of 32.0kDa.CHMP4A is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques. CHMP4A is a member of the SNF7 family and operates as chromatin-modifying protein. CHMP4A is a key component of the endosomal sorting vital for transport complex III (ESCRT-III) which takes part in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. Additionally, during HIV-1 infection, the virus utilizes the ESCRT-III complex to facilitate budding and exocytosis of viral proteins through the connection of CHMP4 and a protein engaged by HIV-1 p6, which exists in viral Gag assembly and budding. CHMP4A is expressed in higher quantities in skeletal muscle, kidney, liver and heart.