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CRABP1 encodes a specific binding protein for a vitamin A family member and is thought to play an important role in retinoic acid-mediated differentiation and proliferation processes. Zusätzlich bieten wir Ihnen Cellular Retinoic Acid Binding Protein 1 Antikörper (75) und viele weitere Produktgruppen zu diesem Protein an.
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Holo-CRABPs had higher affinity for CYP26B1 (zeige CYP26B1 Proteine) than free atRA, but both apo (zeige C9orf3 Proteine)-CRABPs(CRABP-I and CRABP-II (zeige CRABP2 Proteine) ) inhibited the formation of 4-OH-RA by CYP26B1 (zeige CYP26B1 Proteine).
p75NTR (zeige NGFR Proteine) and CRABP1 modulate the effect of fenretinide on neuroblastoma (zeige ARHGEF16 Proteine) cells
miR (zeige MLXIP Proteine)-93/miR (zeige MLXIP Proteine)-106b/miR (zeige MLXIP Proteine)-375-CIC-CRABP1 is a novel key regulatory axis in prostate cancer progression
CRABP1 expression is maintained in ER- and triple-negative breast tumors, and that elevated levels of CRABP1 is a significant indicator of high tumor grade, Ki67 (zeige MKI67 Proteine) immunoreactivity, and poor prognosis.
the first evidence of pro-tumorigenic and pro-metastatic activity of CRABP1 in mesenchymal and neuroendocrine tumors.
we demonstrated significant changes in CRABP1 and CRABP2 (zeige CRABP2 Proteine) expression in non-small cell lung cancer samples
Factors involved in the retinoid pathway, in particular upregulation of CRBP (zeige RBP1 Proteine), CRABP1 and CRABP2 (zeige CRABP2 Proteine), also showed differential expression in tumors with different histological subtypes
Results describe the mRNA expression of CRABP1, RERG (zeige RERG Proteine), and GRP (zeige LSM4 Proteine) in pituitary adenomas.
reduced expression of CRABP1 has a potential as a prognostic marker for serous adenocarcinoma which is the most frequent histological ovarian tumor type and also for clear cell carcinoma that often exhibits chemo-resistance.
Loss of cellular retinoic acid binding protein 1 function due to hypermethylation of its promoter leads to pathogenesis of papillary thyroid carcinoma
Chromosome mapping of CRABP1 (zeige RBP1 Proteine) AND CRABP2 (zeige CRABP2 Proteine) in swine.
The physiological role of Crabp1 in modulating stem cell proliferation and hippocampus-dependent brain activities such as learning and memory.
This study reveals a physiological relevance of the non-genomic action of atRA, mediated by Crabp1, in modulating cell cycle progression and apoptosis induction
Only a small fraction of CRABP1 populates this functionally important but vulnerable conformation of CRABP1, enabling efficient ligand binding.
CRABPI binds to all-trans retinoic acid in the cytoplasm, resulting in rapid ERK1/2 activation that is independent of membrane signal and nuclear RA receptors.
These data suggest that CRABPI functions to regulate the intracellular concentrations of retinoic acid and to maintain high levels of oxidized retinoic acid metabolites such as 4-oxoretinoic acid within cells.
The expression of CRABP I in the embryonic cerebellum coincides with earliest cerebellar differentiation; its involvement in a complex network of regulatory genes expressed in the mes (zeige PTCH1 Proteine)/methencephalon is discussed in this review.
This study presents the first evidence that over-expressed receptor interacting protein 140 acts as a thyroid hormone (T3)-dependent negative co-regulator for T3 induction of the endogenous cellular retinoic acid binding I protein gene in P19 cells.
proline isomerization may not be responsible for the slowest folding phase of CRABP I so the loss of a slow refolding phase upon mutation may not be diagnostic for proline isomerization effects on protein folding
Increases in CRABPI and II transcripts in the absence of leukemia inhibitory factor (zeige LIF Proteine) may regulate aspects of embryonic stem cell differentiation in response to retinol.
This gene encodes a specific binding protein for a vitamin A family member and is thought to play an important role in retinoic acid-mediated differentiation and proliferation processes. It is structurally similar to the cellular retinol-binding proteins, but binds only retinoic acid at specific sites within the nucleus, which may contribute to vitamin A-directed differentiation in epithelial tissue.
cellular retinoic acid-binding protein 1
, cellular retinoic acid-binding protein I
, cellular retinoic acid binding protein 1
, cellular retinoic acid binding protein I (CRABP-I) homologue
, cellular retinol-binding protein III
, retinol-binding protein 5
, retinol-binding protein III, cellular
, retinol binding protein 5, cellular
, cellular retinoic acid binding protein I
, retinol-binding protein 5-like
, Cellular retinoic acid-binding protein 1
, Cellular retinoic acid-binding protein I