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anti-Human BMPR1A Antikörper:
anti-Mouse (Murine) BMPR1A Antikörper:
anti-Rat (Rattus) BMPR1A Antikörper:
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Human Polyclonal BMPR1A Primary Antibody für IHC (p), WB - ABIN1882067
Waite, Eng: BMP2 exposure results in decreased PTEN protein degradation and increased PTEN levels. in Human molecular genetics 2003
Show all 8 Pubmed References
Human Polyclonal BMPR1A Primary Antibody für CyTOF, FACS - ABIN4899788
Bleuming, Kodach, Garcia Leon, Richel, Peppelenbosch, Reitsma, Hardwick, van den Brink: Altered bone morphogenetic protein signalling in the Helicobacter pylori-infected stomach. in The Journal of pathology 2006
Show all 6 Pubmed References
Human Polyclonal BMPR1A Primary Antibody für FACS, WB - ABIN4899787
Huse, Bakkebø, Oksvold, Forfang, Hilden, Stokke, Smeland, Myklebust: Bone morphogenetic proteins inhibit CD40L/IL-21-induced Ig production in human B cells: differential effects of BMP-6 and BMP-7. in European journal of immunology 2011
Show all 4 Pubmed References
Human Polyclonal BMPR1A Primary Antibody für IHC (p), WB - ABIN388732
Kan, Liu, McGuire, Berger, Awatramani, Dymecki, Kessler: Dysregulation of local stem/progenitor cells as a common cellular mechanism for heterotopic ossification. in Stem cells (Dayton, Ohio) 2009
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Human Monoclonal BMPR1A Primary Antibody für ICC, FACS - ABIN1724745
Nickel, Kotzsch, Sebald, Mueller: Purification, crystallization and preliminary data analysis of the ligand-receptor complex of the growth and differentiation factor 5 variant R57A (GDF5R57A) and BMP receptor IA (BRIA). in Acta crystallographica. Section F, Structural biology and crystallization communications 2011
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Human Monoclonal BMPR1A Primary Antibody für FACS, IHC - ABIN1724746
Nieminen, Abdel-Rahman, Ristimäki, Lappalainen, Lahermo, Mecklin, Järvinen, Peltomäki: BMPR1A mutations in hereditary nonpolyposis colorectal cancer without mismatch repair deficiency. in Gastroenterology 2011
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Human Polyclonal BMPR1A Primary Antibody für FACS, WB - ABIN388737
Tominaga, Abe, Ueda, Goto, Nakahara, Murakami, Matsubara, Mima, Nagai, Araoka, Kishi, Fukushima, Jishage, Doi: Activation of bone morphogenetic protein 4 signaling leads to glomerulosclerosis that mimics diabetic nephropathy. in The Journal of biological chemistry 2011
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Human Polyclonal BMPR1A Primary Antibody für ELISA, WB - ABIN188547
Keller, Nickel, Zhang, Sebald, Mueller: Molecular recognition of BMP-2 and BMP receptor IA. in Nature structural & molecular biology 2004
Human Monoclonal BMPR1A Primary Antibody für CyTOF, ELISA - ABIN4284948
Bolander, Ji, Geris, Bloemen, Chai, Schrooten, Luyten: The combined mechanism of bone morphogenetic protein- and calcium phosphate-induced skeletal tissue formation by human periosteum derived cells. in European cells & materials 2016
Human Polyclonal BMPR1A Primary Antibody für FACS - ABIN4896654
He, Dong, Wang, Xu, Dai, Ma, Zhu: Bone morphogenetic protein receptor IB as a marker for enrichment of osteogenic precursor-like cells in human dermis. in Archives of dermatological research 2011
both bone morphogenetic protein 2 (BMP2 (zeige BMP2 Antikörper)) and BMP6 (zeige BMP6 Antikörper) are proangiogenic in vitro and ex vivo and that the BMP type I receptors, activin receptor-like kinase 3 (ALK3) and ALK2 (zeige ACRV1 Antikörper), play crucial and distinct roles in this process.
BMPR1A and the ubiquitous isoform of BMPR1B differed in mode of translocation into the endoplasmic reticulum; and (ii) BMPR1A was N-glycosylated while BMPR1B was not, resulting in greater efficiency of processing and plasma membrane expression of BMPR1A.
Several germline variants in Hamartomatous Polyposis Syndrome genes were detected, among them three in ENG (zeige ENG Antikörper), two in BMPR1A, one in PTEN (zeige PTEN Antikörper), and one in SMAD4 (zeige SMAD4 Antikörper). Although some of the detected variants have been reported previously none could be definitely pathogenic or likely pathogenic.
The present study suggests that HNF-4alpha has a suppressive effect on hepcidin expression by inactivating the BMP pathway, specifically via BMPR1A, in HepG2 cells.
In solid ameloblastoma, positive correlations were observed between the stromal and parenchymal expression of BMP-2 (zeige BMP2 Antikörper) and between the stromal expression of BMP-2 (zeige BMP2 Antikörper) and BMP-4 (zeige BMP4 Antikörper), as well as between the stromal expression of BMPR-II (zeige BMPR2 Antikörper) and BMP-4 (zeige BMP4 Antikörper) and the stromal and parenchymal expression of BMPR-II (zeige BMPR2 Antikörper).
Data show that protein kinase (zeige CDK7 Antikörper) LKB1 (zeige STK11 Antikörper) physically interacts with BMP type I receptors and requires Smad7 (zeige SMAD7 Antikörper) protein to promote downregulation of the receptor.
BMPR1A(+) ASCs show an enhanced ability for adipogenesis in vitro, as shown by gene expression and histological staining.
Duplication of 10q22.3-q23.3 encompassing BMPR1A gene is associated with congenital heart disease, microcephaly, and mild intellectual disability
Authors analyzed human databases from TCGA and survival data from microarrays to confirm BMPR1a tumor promoting functions, and found that high BMPR1a gene expression correlates with decreased survival regardless of molecular breast cancer subtype.
About half of BMPR1A-related polyps displayed loss of heterozygosity, predominantly in the epithelial compartment, compatible with BMPR1A acting as a tumour suppressor gene.
findings suggest that GJA1 may be one of the downstream targets of BMPR1A signaling in osteoclasts that mediates osteoclast-osteoblast communication during bone remodeling.
deletion of BMPR1a in oncogenic astrocytes resulted in decreased proliferation, decreased invasion, decreased migration, and increased expression of stemness markers
different levels of expression and subsequent activation of Smad (zeige SMAD1 Antikörper) signaling differentially contribute each BMP type I receptor to BMP-Smad (zeige SMAD1 Antikörper) signaling and craniofacial development.
BMP signaling mediated by coordination of ALK2/ACVR1 (zeige ACRV1 Antikörper), ALK3/BMPR1A, and BMPR2 (zeige BMPR2 Antikörper) is an essential proangiogenic cue for retinal vessels.
Gonadotrope-specific Bmpr1a knockout animals developed normally and had reproductive organ weights comparable with those of controls. Knockouts were fertile, with normal serum gonadotropins and pituitary gonadotropin subunit mRNA expression. Cre-mediated recombination of the floxed Bmpr1a allele was efficient and specific, as indicated by PCR analysis of diverse tissues and isolated gonadotrope cells.
CK2.1 peptide drives chondrogenesis and cartilage formation without induction of chondrocyte hypertrophy by releasing CK2 (zeige CSNK2A1 Antikörper) from distinct sites at BMPRIa
These results suggest that Pax8 (zeige PAX8 Antikörper) maybe the downstream molecule of ALK3, it mediates the murine heart development via cellular senescence, which may serve as a mechanism that compensates for the cell loss via apoptosis in heart development.
study suggested that Bmpr-Ia and Bmpr-Ib (zeige BMPR1B Antikörper) signaling regulates tooth formation via miR (zeige MLXIP Antikörper)-135a.
integrin alpha1beta1/BMPR IA may block BMP-2 (zeige BMP2 Antikörper)/BMPR IA complex information and interfere with the BMP-2 (zeige BMP2 Antikörper) signalling pathway in cells
signaling via activin (zeige Actbeta Antikörper)-like kinase 3 (ALK3/BMPR1A), a BMP type 1 receptor, is necessary for blastocyst attachment.
Report temporal regulation of BMPR1a mRNA expression in the oocyte, granulosa and theca cells of developing preovulatory follicles in the pig.
ALK3 and ALK6 (zeige BMPR1B Antikörper) both contribute to the gene regulatory network that regulates dorso-ventral patterning.
Data show that USP15 (zeige USP15 Antikörper) enhances BMP-induced phosphorylation of SMAD1 (zeige SMAD1 Antikörper) by interacting with and deubiquitylating ALK3.
The bone morphogenetic protein (BMP) receptors are a family of transmembrane serine/threonine kinases that include the type I receptors BMPR1A and BMPR1B and the type II receptor BMPR2. These receptors are also closely related to the activin receptors, ACVR1 and ACVR2. The ligands of these receptors are members of the TGF-beta superfamily. TGF-betas and activins transduce their signals through the formation of heteromeric complexes with 2 different types of serine (threonine) kinase receptors: type I receptors of about 50-55 kD and type II receptors of about 70-80 kD. Type II receptors bind ligands in the absence of type I receptors, but they require their respective type I receptors for signaling, whereas type I receptors require their respective type II receptors for ligand binding.
, BMP type-1A receptor
, activin A receptor, type II-like kinase 3
, activin receptor-like kinase 3
, bone morphogenetic protein receptor type-1A
, serine/threonine-protein kinase receptor R5
, BMP-2/BMP-4 receptor
, bone morphogenetic protein 4 receptor
, bone morphogenetic protein receptor, type 1A
, BMP receptor 1
, bone morphogenic protein receptor 1
, protein kinase
, bone morphogenetic protein receptor IA
, bone morphogenetic protein receptor, type IA
, bone morphogenetic protein receptor type-1A-like
, BMP receptor
, bone morphogenetic protein receptor type IA