Recombinant Human CRABP2 protein (Tag Free)
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(1 Publication)
Recombinant Human CRABP2 protein (Tag Free) is a Human Full Length protein, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE.
View Alternative Names
Cellular retinoic acid-binding protein 2, Cellular retinoic acid-binding protein II, CRABP-II, CRABP2
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human CRABP2 protein (Tag Free) (AB74527)
15% SDS-PAGE showing ab74527 (3μg)
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
CRABP2 participates in modulating the availability of RA which influences gene expression by binding to nuclear receptors. Although CRABP2 functions independently rather than as part of a larger protein complex it holds a significant role in gene transcription regulation. This active role in regulating RA levels impacts cellular differentiation and proliferation processes essential for tissue development and homeostasis.
Pathways
CRABP2 is an important participant in the retinoic acid signaling pathway. This pathway impacts important biological processes such as embryonic development and cell growth. CRABP2 closely interacts with the retinoic acid receptor (RAR) guiding RA to RARs and contributing to the regulation of gene expression. Moreover it is linked to the transforming growth factor-beta (TGF-beta) pathway playing a role in managing cellular apoptosis and differentiation.
Specifications
Form
Liquid
Additional notes
ab74527 was purified by using conventional chromatography techniques.
General info
Function
Transports retinoic acid to the nucleus. Regulates the access of retinoic acid to the nuclear retinoic acid receptors.
Sequence similarities
Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family.
Post-translational modifications
Sumoylated in response to retinoic acid binding, sumoylation is critical for dissociation from ER and subsequent nuclear translocation.
Subcellular localisation
Nucleus
Target data
Publications (1)
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Molecular bioSystems 6:1700-6 PubMed20523938
2010
Applications
WB
Species
Human
Product promise
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