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anti-Human PDGFD Antikörper:
anti-Rat (Rattus) PDGFD Antikörper:
anti-Mouse (Murine) PDGFD Antikörper:
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Human Polyclonal PDGFD Primary Antibody für IP, WB - ABIN529260
Rizvi, Mertens, Bronk, Hirsova, Dai, Roberts, Kaufmann, Gores: Platelet-derived growth factor primes cancer-associated fibroblasts for apoptosis. in The Journal of biological chemistry 2014
Human Polyclonal PDGFD Primary Antibody für IF (p), IHC (p) - ABIN714581
Hurley, Adams, Wang, Jiang, Meo Burt, Du, Xiao: Accelerated Fracture Healing in Transgenic Mice Overexpressing an Anabolic Isoform of Fibroblast Growth Factor 2. in Journal of cellular biochemistry 2015
We report the first recurrent molecular variant of dermatofibrosarcoma protuberans involving PDGFD
PDGF-C and PDGF-D are relatively new members of the PDGF family and are potent angiogenic and survival factors. Recent studies have demonstrated their important roles in different types of eye diseases. [review]
Numerous studies have shown that PDGF-C and PDGF-D are critical regulators of the cardiovascular system as angiogenic and survival factors. PDGF-C and PDGFD are widely expressed in many different types of cells with pleotropic effects. [review]
PDGF-D and its PDGF receptor beta (PDGFR-beta) are expressed in colorectal cancer.
PDGF-D overexpression is an independent predictor of platinum-based chemotherapy resistance and it may also be a potential biomarker for targeted therapy and poor prognosis.
PDGF-D promotes tumor growth and aggressiveness of colorectal carcinoma. Down-regulation of PDGF-D inactivates Notch1/Twist1 axis, which could reverse epithelial mesenchymal transformation and prevent CRC progression.
significant correlations between DNA methylation of the PDGFD gene promoter and the risk of developing either IA or BAVM
This study suggested that epithelial-mesenchymal transition process can be triggered by the PDGF-D/PDGFRb axis in tongue squamous cell carcinoma, and then involved in the tumor cell invasion via activation of p38/AKT/ERK/ epithelial-mesenchymal transition pathway.
No specific genotype of rs974819 of Platelet-derived growth factor D demonstrated increased cardiovascular mortality in the total population, however, the male group with genotypes A/A and G/A demonstrated an increased risk that persisted in a multivariate evaluation where adjustments were made for well-known cardiovascular risk factors.
There are four platelet-derived growth factor (PDGF) genes (PDGFA, PDGFB, PDGFC and PDGFD) that reside on chromosomes 7, 22, 4 and 11.
upregulated in kidney fibrosis, may mediate renal scarring, and is dispensable for normal kidney development and physiological functions
polymorphism of rs7950273 in the PDGFD gene is not associated with ischaemic stroke in the Chinese Han population
Novel findings reveal a new paradigm in matriptase activation involving PDGF-D-specific signal transduction leading to extracellular acidosis.
PDGF-D expression is associated with miR-106a and Twist1 in HCC patients
PDGF-D is highly expressed by ASCs, where it acts as a potent mitogenic factor.
PDGFD, CDH1 and SLIT2 are upregulated in low grade meningiomas and schwannomas compared with healthy tissue.
PDGF-DD secreted by gastric cancer derived mesenchymal stem cells is capable of promoting gastric cancer cell progression in vitro and in vivo.
Data suggest that targeting platelet-derived growth factor-D as a strategy for endometrial cancer treatment.
Compared with matched normal endometrial cases, PDGF-D was up-regulated in endometrial cancer. Expression of PDGF-D protein, found in 78% of the cases, was associated with nonendometrioid histologic type.
PDGFD-PDGFRbeta signalling is required for human neocortical development and local production of growth factors by radial glia supports the expanded germinal region and progenitor heterogeneity of species with large brains
Data (including data from studies using transgenic/mutant mice and cells from such mice) suggest that Pdgfd promotes cell proliferation, cell migration, and expression of inflammatory factors in adventitial fibroblasts; in obese mice, inhibition of Pdgfd significantly reduces aortic aneurysm formation (induced by infusion of angiotensin II).
Inactivation of the Pdgfd gene resulted in a mild phenotype in C57BL/6 mice, and the offspring was viable, fertile and generally in good health.
PDGF-D intensifies fibrogenesis by interfering with the fibrolytic activity of the TIMP-1/MMP-2/MMP-9 system, and PDGF-D signaling is mediated through both PDGF-alpha and -beta receptors.
Radial glia require PDGFD-PDGFRbeta signalling in human but not mouse neocortex
PDGF D represents a potentially promising target for prostate carcinoma treatment resistance in the absence of PTEN function, and warrants further laboratory evaluation and clinical study.
Data indicate that the proteolytic processing of full-length PDGF-D is required for PDGF-D activation of preosteoclasts, and that beta-PDGFR is present in activated osteoclasts.
identified PDGF-DD as an important target gene for antiangiogenic therapy due to its pleiotropic effects on vascular and non-vascular cells. PDGF-DD inhibition may offer new therapeutic options to treat neovascular diseases
Failure of laminin alpha4-mediated down-regulation of PDGF activity contributes to the progressive renal lesions in this animal model.
These results suggest that PDGF-D induce cellular transformation and promote tumour growth by accelerating the proliferation rate of the tumour cells, and by stimulation of tumour neovascularization.
splicing variant results in significant differences in peptide expression and function
PDGF-D plays an important role in the pathogenesis of tubulointerstitial injury through binding of PDGF-Rbeta in obstructive ureteral nephropathy
PDGF-DD, a novel mediator of smooth muscle cell phenotypic modulation, is upregulated in endothelial cells exposed to atherosclerosis-prone flow patterns.
The protein encoded by this gene is a member of the platelet-derived growth factor family. The four members of this family are mitogenic factors for cells of mesenchymal origin and are characterized by a core motif of eight cysteines, seven of which are found in this factor. This gene product only forms homodimers and, therefore, does not dimerize with the other three family members. It differs from alpha and beta members of this family in having an unusual N-terminal domain, the CUB domain. Two splice variants have been identified for this gene.
, iris-expressed growth factor
, platelet-derived growth factor D
, spinal cord derived growth factor B
, spinal cord-derived growth factor B
, spinal cord-derived growth factor-B
, platelet-derived growth factor, D polypeptide
, spinal-cord derived growth factor-B protein
, platelet derived growth factor D
, platelet-derived growth factor D-like