Recombinant Human INF2 GST (N-Term) Protein Summary
Description |
A recombinant protein with GST tag at N-terminal corresponding to the amino acids 1-337 of Human INF2 Source: Wheat Germ (in vitro) Amino Acid Sequence: MKAFRDLFLRALKENKDRKEQAAKAERRKQQLAEEEARRPRGEDGKPVRKGPGKQEEVCVIDALLADIRKGFQLRKTARGRGDTDGGSKAASMDPPRATEPVATSNPAGDPVGSTRCPASEPGLDATTASESRGWDLVDAVTPGPQPTLEQLEEGGPRPLERRSSWYVDASDVLTTEDPQCPQPLEGAWPVTLGDAQALKPLKFSSNQPPAAGSSRQDAKDPTSLLGVLQAEADSTSEGLEDAVHSRGARPPAAGPGGDEDEDEEDTAPESALDTSLDKSFSEDAVTDSSGSGTLPRARGRASKGTGKRRKKRPSRSQEEVPPDSDDNKTKKLCVIQ |
Preparation Method |
in vitro wheat germ expression system |
Details of Functionality |
This protein was produced in an in vitro wheat germ expression system that should preserve correct conformational folding that is necessary for biological function. While it is possible that this protein could display some level of activity, the functionality of this protein has not been explicitly measured or validated. |
Source |
Wheat germ |
Protein/Peptide Type |
Recombinant Protein |
Gene |
INF2 |
Purity |
>80% by SDS-PAGE and Coomassie blue staining |
Applications/Dilutions
Dilutions |
- ELISA
- Immunoaffinity Purification
- Protein Array
- SDS-Page
- Western Blot
|
Theoretical MW |
62.4 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
Packaging, Storage & Formulations
Storage |
Store at -80C. Avoid freeze-thaw cycles. |
Buffer |
50 mM Tris-HCl, 10 mM reduced Glutathione, pH 8.0 in the elution buffer. |
Preservative |
No Preservative |
Purity |
>80% by SDS-PAGE and Coomassie blue staining |
Notes
This product is produced by and distributed for Abnova, a company based in Taiwan.
Alternate Names for Recombinant Human INF2 GST (N-Term) Protein
Background
Actin filaments grow only when actin monomers have access to the fast-growing barbed end of the filament. The geometry of the filament network depends on the actions of the ARP2/3 complex (MIM 604221) and members of the formin family, such as INF2. The ARP2/3 complex binds to the sides of preexisting filaments and nucleates filaments whose barbed ends are quickly blocked by capping proteins, producing brush-like structures, such as those found at the leading edges of crawling cells. In contrast, formins bind to the barbed ends of growing filaments and protect them from capping, creating long filaments that can be cross-linked into bundles, such as those found in actin cables of yeast. Interaction of formins with actin barbed ends occurs through the formin homology-2 (FH2) domain. FH2 domains accelerate filament nucleation, move with the barbed end as the filament grows, and block capping of the barbed end by proteins such as gelsolin (GSN; MIM 137350). The FH1 domain of formins binds to profilin (see MIM 176610) and accelerates elongation from the FH2-bound barbed ends (Bindschadler and McGrath, 2004 [PubMed 15466701]; Chhabra and Higgs, 2006 [PubMed 16818491]).[supplied by OMIM]
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are
guaranteed for 3 months from date of receipt.
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