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Validated All-in-One™ qPCR Primer for BMP1(NM_001199.3) Search again
Product ID:
HQP017280
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
OI13, PCOLC, PCP, PCP2, TLD
Gene Description:
bone morphogenetic protein 1
Target Gene Accession:
NM_001199.3(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.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
This gene encodes a protein that is capable of inducing formation of cartilage in vivo. Although other bone morphogenetic proteins are members of the TGF-beta superfamily, this gene encodes a protein that is not closely related to other known growth factors. This gene is expressed as alternatively spliced variants that share an N-terminal protease domain but differ in their C-terminal region. [provided by RefSeq].
Gene References into function
- bone morphogenetic protein-1 (BMP-1), which exhibits procollagen C-proteinase activity, cleaves the C-terminal propeptide from human procollagen VII
- Post-translational modification is required for secretion and stability of the protein.
- the minimal domain structure for PCP activity is considerably shorter than expected and comprises the metalloproteinase domain and the CUB1 and CUB2 domains of BMP-1
- Pro-BMP-1 is cleaved in the trans-Golgi network
- Dermal wound healing in red Duroc pigs show unique mRNA expression of HSP47,BMP-1,TIMP1-3 and hypercontracted,hyperpigmented scars.
- cleaves LG3 from recombinant endorepellin at the physiologically relevant site and cleaves LG3 from endogenous perlecan in cultured mouse and human cells
- chordinase activity of BMP1 is not enhanced by PCPE-1
- tolloid-like 1 binds procollagen C-proteinase enhancer protein 1 and differs from bone morphogenetic protein 1 in the functional roles of homologous protein domains
- bone morphogenetic protein 1 is inhibited by native and altered forms of alpha2-macroglobulin
- the BMP1 prodomain specifically binds and regulates signaling by BMP2 and BMP4
- By mutating residues flanking the cleavage site of collagen type V alpha 1, we showed that the aspartate residue at position P2' is essential for BMP-1 activity.
- data support the concept that the C-terminal domains of BMP1 are important for substrate recognition and for controlling and restricting its proteolytic activity via exosite binding
- BMP1 processes PRL to a 17-kDa anti-angiogenic factor.
- vascular Bmp Msx2 Wnt signaling and oxidative stress have roles in arterial calcification [review]
- Expression of BMP1, BMP6, BMP7, and BMP-receptor 2 was significantly increased in advanced stages of myelofibrosis compared and enhanced levels of BMP6 expression were already evident in prefibrotic stages of primary myelofibrosis.
- The crystal structures of the protease domains of human BMP-1 and the closely related Tolloid-like protease 1 (TLL-1), are reported.