Purified Protein in ready-to-use SDS sample buffer.
Produktmerkmale
Cyto4-selective antibodies were generated against a peptide taken from the human Cytohesin 4 protein. The Cyto4-selective antibodies are affinity purified on an immobilized antigen based affinity matrix, the isolated antibodies were then stabilized in antibody stabilization buffer for long-term storage. The anti-Cyto4-selective antibodies are fully characterized for applications in western blotting and ELISA at the recommended dilutions. The Supplier provides Cyto4 western blot positive control samples in SDS-PAGE sample buffer. Synonyms: Sec7 and coiled coiled domain containg protein 4, /PSCD4
CYTH4
Spezies: Human
Wirt: Tobacco (Nicotiana tabacum)
Recombinant
>80 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot.
WB, SDS, ELISA
CYTH4
Spezies: Human
Wirt: HEK-293 Cells
Recombinant
> 80 % as determined by SDS-PAGE and Coomassie blue staining
AbP, STD
Applikationshinweise
Antibodies were tested in ELISA and western blotting applications at 1:500 dilution using ABIN1686770 samples. Antibody dilutions for these antibodies are for reference only, investigators are expected to determine the optimal conditions. Application of this antibody in other protocols has not yet tested. WB: > 1:500 IMM & IP pull-down assays: N.D. . IHC: N.D. . Investigators using this antibody in protocols other than listed above can request a complimentary sample of this antibody. N.D. not necessarily means the antibody is not suitable for that application, it simply means we have not yet characterized the antibody in that application.
Beschränkungen
Nur für Forschungszwecke einsetzbar
Format
Liquid
Buffer
For 5 applications, volume varies from 100-200 μL in reduced SDS-PAGE sample buffer.
Cytohesin-4, also known as CYT4 or PSCD4 (pleckstrin homology, Sec7 and coiled-coil domains 4), is a 394 AA ADP-ribosylation factor (ARF) that functions as a guanine nucleotide-exchange protein (GEP) and is expressed primarily in blood leukocytes with minimal expression observed in the thymus and spleen, The newly cloned Cytohesin 4 is a 47 kDa protein with similar structural motifs as in Cytohesin 1, 2 and 3. Cytohesin-4 has a C-terminal pleckstrin homology (PH) domain, an N-terminal coiled-coil motif and a central Sec7 domain. The PH domain is responsible for membrane and phospholipid interaction, while the coiled-coil motif mediates homodimerization. The cytohesin 1 and 4 are very similar except for the 3 base pair (GAG) axon present in Cytohesin 1. The Sec7 domain of Cytohesin-4, wihich is the central domain of the guanosine exchange factors of the ADP-ribosylation factor family of small GTPases, exhibits the GEP activity which, in vitro, can promote guanine nucleotide-exchange with both ARF1 and ARF5 and also promotes the activation of ARF through replacement of GDP with GTP. Over expression of cytohesin 4 stimulated guanosine 5'-3-O-(thio)triphosphate binding to ARF1 and 5 but not to ARF6. The ARFs are approximately 20 kDa GTPases that are inactive in the GDP-bound from but become activated upon binding of GTP via GTP exchange proteins (GEPs). Cytohesins are identified as cytoplasmic ErbB receptor activators in certain cancers, exhibiting an important role in ErbB signaling. Cytohesin overexpression correlated with EGF signaling pathway activation in human lung adenocarcinomas. Cytohesin inhibition decreased ErbB receptor autophosphorylation and signaling, whereas Cytohesin overexpression stimulated receptor activation .