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SRP6156

Sigma-Aldrich

BMP-4 human

recombinant, expressed in HEK 293 cells, ≥95% (SDS-PAGE)

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Synonym(s):
BMP-2B, Bone morphogenetic protein 2B, Bone morphogenetic protein 4
NACRES:
NA.32

biological source

human

recombinant

expressed in HEK 293 cells

Assay

≥95% (SDS-PAGE)

form

lyophilized

potency

2-10 ng/mL

mol wt

34 kDa (homodimer, glycosylated.)

packaging

pkg of 10 μg

storage condition

avoid repeated freeze/thaw cycles

impurities

<1 EU/μg protein Endotoxin level (LAL test)

NCBI accession no.

shipped in

dry ice

storage temp.

−20°C

Gene Information

human ... BMP4(652)

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SRP3017SRP6155SRP3279
BMP-4 human recombinant, expressed in HEK 293 cells, &#8805;95% (SDS-PAGE)

Sigma-Aldrich

SRP6156

BMP-4 human

BMP-6 human recombinant, expressed in HEK 293 cells, &#8805;95% (SDS-PAGE), &#8805;95% (HPLC), suitable for cell culture

Sigma-Aldrich

SRP3017

BMP-6 human

BMP-2 human recombinant, expressed in HEK 293 cells, &#8805;95% (SDS-PAGE)

Sigma-Aldrich

SRP6155

BMP-2 human

BMP-5 human recombinant, expressed in CHO cells, &#8805;95% (SDS-PAGE), &#8805;95% (HPLC)

Sigma-Aldrich

SRP3279

BMP-5 human

recombinant

expressed in HEK 293 cells

recombinant

expressed in HEK 293 cells

recombinant

expressed in HEK 293 cells

recombinant

expressed in CHO cells

assay

≥95% (SDS-PAGE)

assay

≥95% (HPLC), ≥95% (SDS-PAGE)

assay

≥95% (SDS-PAGE)

assay

≥95% (HPLC), ≥95% (SDS-PAGE)

form

lyophilized

form

lyophilized

form

lyophilized

form

lyophilized

potency

2-10 ng/mL

potency

0.03-0.06 μg/mL ED50

potency

20-100 ng/mL ED50

potency

0.5-1.0 μg/mL ED50

mol wt

34 kDa (homodimer, glycosylated.)

mol wt

26.2 kDa

mol wt

30-38 kDa (homodimer, glycosylated)

mol wt

31.2 kDa

General description

BMP4 (bone morphogenetic protein 4), a member of the highly conserved BMP family, is a growth factor and a pro-inflammatory and pro-atherogenic cytokine. BMPs are part of the TGFβ (tumor growth factor) superfamily of proteins. BMP4 gene is localized to human chromosome 14q22-q23.

Biochem/physiol Actions

BMP4 (bone morphogenetic protein 4) is involved in modulating cell development in a wide variety of cells. It promotes the proliferation and migration of hepatocellular carcinoma cells, and the multiplication of ALK3 (activin-like kinase)-positive cells in skeletal muscle. This protein prevents the proliferation of lung fibroblasts and induces their differentiation into myocytes. In Sertoli cells, it promotes DNA synthesis and hence, the proliferation of Sertoli cells through Smad1/5 (small mothers against decapentaplegic) and ID2/3 (DNA binding protein inhibitor) pathway, and aberration in BMP4 expression results in azoospermia. In human males, the serum levels of BMP4 is linked with coronary artery disease (CAD) severity. BMP4 is crucial for maintaining the self-renewal capacity of ES (embryonic stem) cells, and achieves so by inhibiting extracellular receptor kinase (ERK) and p38 mitogen-activated protein kinase (MAPK) pathways.

Physical form

Lyophilized from a PBS solution.

Preparation Note

Centrifuge the vial prior to opening.

Reconstitution

Reconstitute in sterile 4 mM HCl containing 0.1% endotoxin-free recombinant human serum albumin.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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Fine mapping of the human bone morphogenetic protein-4 gene (BMP4) to chromosome 14q22-q23 by in situ hybridization.
van den Wijngaard A et al
Genomics, 27(3), 559-560 (1995)
Bmp4 is required for the generation of primordial germ cells in the mouse embryo.
Lawson KA et al
Genes & Development, 13(4), 424-436 (1999)
BMP4 promotes human Sertoli cell proliferation via Smad1/5 and ID2/3 pathway and its abnormality is associated with azoospermia.
Hai Y et al
Discovery Medicine, 19(105), 311-325 (2015)
Serum Bone Morphogenic Protein-4 Contributes to Discriminating Coronary Artery Disease Severity.
Park CS et al
Medicine, 94(3), e1530-e1530 (2015)
BMP4 supports self-renewal of embryonic stem cells by inhibiting mitogen-activated protein kinase pathways.
Qi X et al
Proceedings of the National Academy of Sciences of the USA, 101(16), 6027-6032 (2004)

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