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H4916

Sigma-Aldrich

BMP4, human

HumanKine®, recombinant, Xeno-free, >95% (SDS-PAGE), suitable for cell culture

Sinonimo/i:

Bone Morphogenetic Protein 4 human, BMP-4

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10 μG
CHF 466.00
100 μG
CHF 3’250.00

CHF 466.00


Spedizione prevista il08 aprile 2025



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Cambia visualizzazione
10 μG
CHF 466.00
100 μG
CHF 3’250.00

About This Item

Numero MDL:
Codice UNSPSC:
12352202
NACRES:
NA.77

CHF 466.00


Spedizione prevista il08 aprile 2025


Nome del prodotto

Bone Morphogenetic Protein 4 human, BMP-4, recombinant, expressed in HEK 293 cells, HumanKine®, suitable for cell culture

Origine biologica

human

Livello qualitativo

Ricombinante

expressed in HEK 293 cells

Saggio

>95% (SDS-PAGE)

Stato

lyophilized powder

Potenza

≤10 ng/mL EC50

Qualità

endotoxin tested

PM

dimer 34 kDa (glycosylated)

Confezionamento

pkg of 10 μg
pkg of 100 μg
pkg of 1000 μg

Condizioni di stoccaggio

avoid repeated freeze/thaw cycles

tecniche

cell culture | mammalian: suitable

Impurezze

<1 EU/μg Endotoxin level

N° accesso UniProt

Temperatura di conservazione

−20°C

Informazioni sul gene

human ... BMP4(652)

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Descrizione generale

BMP are members of the TGF-β superfamily of cytokines that affect bone and cartilage formation. Similar to other TGF-β family proteins, BMPs are highly conserved across animal species. Mature BMPs are 30-38 kDa proteins that assume a TGF-β-like cysteine knot configuration. Unlike TGF-β, BMPs do not form latent complexes with their propeptide counterparts. Most BMPs are homodimers, but bioactive natural heterodimers have been reported.
Bone morphogenetic protein 4 (BMP4) is a member of the transforming growth factor-β (TGF-β) superfamily.[1] It is a glycoprotein with cysteine knot and exists as homodimer corresponding to a molecular mass of 26 kDa.[2] BMP4 is mapped to human chromosome 14q22.2.[3] BMP4 is expressed in embryonic and adult tissues.[2] It is synthesized in the endoplasmic reticulum and in Golgi, it undergoes posttranslational modifications.[4]

Applicazioni

Bone morphogenetic protein 4 human has been used to induce cardiac myogenic differentiation in bone marrow-derived mesenchymal stem cells (MSC).[5]

Azioni biochim/fisiol

BMPs create an environment conducive for bone marrow development by stimulating the production of specific bone matrix proteins and altering stromal cell and osteoclast proliferation. In addition to stimulating ectopic bone and cartilage development, BMPs may be an important factor in the development of the viscera, with roles in cell proliferation, apoptosis, differentiation, and morphogenesis. BMPs also appear to be responsible for normal dorsal/ventral patterning. BMP-4 specifies the development of ventral structures (e.g., skin from ectoderm and connective tissue/blood from mesoderm). Dorsal structures (nervous system and muscle) apparently appear when BMP-4 signals are interrupted through the activities of binding proteins. BMPs are found in tissues that induce bone or cartilage growth, such as demineralized bone and urinary epithelium.

Cellular responses to BMP-4 are mediated by the formation of hetero-oligomeric complexes of type I and type II serine/threonine kinase receptors, which play significant roles in BMP binding and signaling. Two BMP type I receptors and one BMP type II receptor have been identified. Both BMP type I receptors bind BMP-4 with high-affinity in the absence of BMP receptor type II.
Bone morphogenetic protein 4 (BMP4) is essential for auditory neurogenesis.[1] It also mediates the mesenchyme formation and acts as a key differentiation factor for hematopoietic and nerve cells.[2] The BMP4 based signaling is upregulated in both. oligodendrocyte progenitor cells (OPCs) neural precursor cells (NPCs).[4] Cellular responses to BMP-4 are mediated by the formation of heterooligomeric complexes of type I and type II serine/threonine kinase receptors, which play significant roles in BMP binding and signaling.[6] Frameshift mutations in the BMP4 is implicated in the developmental anomalies especially with optic vesicle and digits.[7] BMP4 mutations have also been associated with orbicularis oris muscle (OOM) and lip morphological defects.[8]

Stato fisico

Lyophilized from a 0.2 μm filtered solution of 2x PBS + 6% Ethanol.

Nota sulla preparazione

This Bone Morphogenetic Protein-4 (BMP-4) is expressed in human HEK 293 cells as a glycosylated 34 kDa homodimer. Production in human HEK 293 cells offers authentic glycosylation. Glycosylation contributes to stability in cell growth media and other applications. Mature human and mouse BMP-4 are 98% and 100% identical, respectively, to mature rat BMP-4 in their amino acid sequence.

Risultati analitici

The specific activity was determined by its ability to induce alkaline phosphatase production in a dose response to BMP-4 in the ATDC-5 cell line (mouse chondrogenic cell line).

Note legali

HumanKine is a registered trademark of Proteintech Group, Inc. and Humanzyme, Inc

Inibitore

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Prodotto comparabile

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


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I clienti hanno visto anche

Solubilization and renaturation of biologically active human bone morphogenetic protein-4 from inclusion bodies
Gieseler GM, et al.
Biotechnology reports (Amsterdam, Netherlands), 18, e00249-e00249 (2018)
Mutations in BMP4 are associated with subepithelial, microform, and overt cleft lip
Suzuki S, et al.
American Journal of Human Genetics, 84(3), 406-411 (2009)
Induction of cardiac myogenic lineage development differs between mesenchymal and satellite cells and is accelerated by bone morphogenetic protein-4
Grajales L, et al.
Journal of Molecular and Cellular Cardiology, 53(3), 382-391 (2012)
The prodomain of BMP4 is necessary and sufficient to generate stable BMP4/7 heterodimers with enhanced bioactivity in vivo
Neugebauer JM, et al.
Proceedings of the National Academy of Sciences of the USA, 112(18), E2307-E2316 (2015)
Bone morphogenetic protein 4 signalling in neural stem and progenitor cells during development and after injury
Cole AE, et al.
Stem Cells International, 2016 (2016)

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