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Validated All-in-One™ qPCR Primer for FHL2(NM_001039492.3) Search again
Product ID:
HQP153853
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
AAG11, DRAL, FHL-2, SLIM-3, SLIM3
Gene Description:
four and a half LIM domains 2
Target Gene Accession:
NM_001039492.3(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Summary
LIM proteins contain a highly conserved double zinc finger motif called the LIM domain.[supplied by OMIM].
Gene References into function
- Insulin-like growth factor-binding protein 5 (IGFBP-5) interacts with a four and a half LIM protein 2 (FHL2).
- TUCAN/CARDINAL and DRAL participate in a common pathway for modulation of NF-kappaB activation.
- evidence of a functional interaction between the promyelocytic leukemia zinc finger protein (PLZF) and DRAL/FHL2
- FHL2 might enforce beta-catenin transactivation activity in cancer cells
- -FHL2 interaction may be involved in transcriptional regulation and play a significant role in cancer cell growth
- both the recombinant and the natural proteins are post-translationally modified and indicate that such modifications may lead to an abnormal electrophoretic behavior of natural human FHL2
- FHL2 and FHL3, respectively, are colocalized with alpha(7)beta(1) integrin receptor at the periphery of Z-discs, suggesting a role in mechanical stabilization of muscle cells
- pp125FAK and FHL2 form a protein complex in human ovarian carcinoma.
- The interaction and functional cooperation between FHL2, CITED4, and CTNNB were studied.
- FHL2 inhibits FOXO1 activity in prostate cancer cells by promoting the deacetylation of FOXO1 by SIRT1
- In conclusion, our findings are consistent with the hypothesis that FHL-2 and ADAM-9 are important modulators of IGFBP-5 actions and are, in part, regulated in a coordinated manner in bone.
- Overall, our findings indicate that FHL2 can also regulate p53 via a direct association with HIPK2.
- FHL2 plays an important role in osteoblast differentiation and bone formation.
- specific expression in tumor tissue points to an important functional role of FHL2 in human breast cancer
- findings show that full-length E4F1 protein but not its E1A-activated & truncated form interacts in vitro & in vivo with FHL2; this E4F1-FHL2 association occurs in the nuclear compartment & inhibits the capacity of E4F1 to block cell proliferation
- the interaction of FHL2 with HPV-16 E7 leads to a promoter-specific impairment of FHL2 function and this may contribute to cell transformation.
- Data suggest that nuclear FHL2 may serve as a novel biomarker predictive for prostate cancer with aggressive biology and point to a role of FHL2 in constitutive activation of AR-mediated growth signals.
- PELP1 functions as a molecular adaptor, coupling FHL2 with nuclear receptors, and PELP1-FHL2 interactions may have a role in prostate cancer progression.
- Suppression of FHL2 induces cell differentiation and inhibits tumorigenesis in gastrointestinal cancers.
- Functional analysis demonstrated that the FHL2 mutation affected the binding to titin/connectin.
- Data indicate that overexpression of the transcriptional cofactor FHL2 contributes to breast cancer development by mediating transcriptional activation of MAPK target genes known to be involved in cancer progression, such as p21.
- These results suggest a novel indirect mechanism of androgen action on FHL2 expression and provide evidence that SRF is an important determinant of AR action in prostate cancer cells.
- Data suggest that IL-1beta is involved in the regulation of various cytoskeletal components in human chondrocytes including the multifunctional protein FHL2, which might be relevant for the pathogenesis of osteoarthritis.
- Role of FHL2 in bundling of focal adhesion structures, in integrin-mediated ERK activation, and subsequently in proper allocation of matrix proteins on the cell surface.
- Overexpression of FHL2 increases the tumorigenicity of glioblastoma cells in nude mice and decreases the mRNA levels of p53.
- FHL2-beta-catenin interaction potentiates beta-catenin nuclear translocation and TCF/LEF transcription, resulting in increased Runx2 and alkaline phosphatase expression, which was inhibited by the Wnt inhibitor DKK1.
- The physiological implication of HERG-FHL2 interaction showed a significant increase in the HERG current amplitude and a faster deactivation of the tail current in human embryonic kidney 293 cells co-expressing HERG and FHL2.
- Human four-and-a-half LIM family members suppress tumor cell growth through a TGF-beta-like signaling pathway.