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E4643

Sigma-Aldrich

Heparin-Binding EGF-Like Growth Factor human

≥97% (SDS-PAGE and N-terminal analysis), recombinant, expressed in baculovirus infected Sf21 cells, lyophilized powder, suitable for cell culture

Synonim(y):

hHB-EGF, HB-EGF, Heparin-Binding Epidermal Growth Factor-Like Growth Factor

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About This Item

Numer MDL:
MFCD00212935
Kod UNSPSC:
12352202
NACRES:
NA.77

product name

Heparin-Binding EGF-Like Growth Factor human, HB-EGF, recombinant, expressed in baculovirus infected Sf21 cells, lyophilized powder, suitable for cell culture

pochodzenie biologiczne

human

Poziom jakości

100

rekombinowane

expressed in baculovirus infected Sf21 cells

Próba

≥97% (SDS-PAGE and N-terminal analysis)

Postać

lyophilized powder

siła działania

≤3 ng/mL

jakość

endotoxin tested

masa cząsteczkowa

9.5 kDa

opakowanie

pkg of 50 and 250 μg

warunki przechowywania

avoid repeated freeze/thaw cycles

metody

cell culture | mammalian: suitable

numer dostępu UniProt

Q99075

temp. przechowywania

−20°C

informacje o genach

human ... HBEGF(1839) , HBEGF(1839)

Działania biochem./fizjol.

Heparin-binding epidermal growth factor (HB-EGF), like BTC, is a heparin-binding EGF family member. Natural soluble HB-EGF is a 19 kDa glycoprotein of multiple forms due to heterogeneous truncations. Soluble HB-EGF is mitogenic and chemotactic for fibroblasts, keratinocytes, and smooth muscle cells but not capillary endothelial cells. Production of HB-EGF is detected in monocytes, macrophages, and vascular and aortic smooth muscle cells (SMC). HB-EGF may play a role in the pathogenesis of atherosclerosis. It may also be an effector of Jun-induced oncogenic transformation. HB-EGF binds to EGFR with high affinity and to ErbB with moderate affinity.

Postać fizyczna

Lyophilized from a 0.2 μm filtered solution in phosphate buffered saline containing 2.5 mg bovine serum albumin.

Komentarz do analizy

The biological activity is measured by its ability to stimulate 3H-thymidine incorporation in the EGF-responsive BALB/3T3 cells.
This page may contain text that has been machine translated.

Kod klasy składowania

11 - Combustible Solids

Klasa zagrożenia wodnego (WGK)

WGK 3

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable

Środki ochrony indywidualnej

Eyeshields, Gloves, type N95 (US)

Certyfikaty analizy (CoA)

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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

U Palmer et al.
The European respiratory journal, 14(2), 405-411 (1999-10-09)
Signalling through epidermal growth factor (EGF) receptor leads to several cellular responses including cell division and cell migration. Since EGF receptors are expressed on normal mesothelial cells, this study investigated whether EGF receptor ligands act as chemoattractants on these cells.
R Iwamoto et al.
The Journal of biological chemistry, 274(36), 25906-25912 (1999-08-28)
Heparin-binding epidermal growth factor-like growth factor (HB-EGF) transduces mitogenic signals through the EGF receptor (EGFR). There are two forms of HB-EGF, the membrane-anchored form (pro-HB-EGF) and the soluble form (sHB-EGF). We studied the biological activity of pro-HB-EGF by using a
F Vinante et al.
Blood, 94(9), 3169-3177 (1999-11-11)
Heparin-binding epidermal growth factor-like growth factor (HB-EGF) is a widely expressed EGF superfamily member that induces mitogenic and/or chemotactic activities toward different cell types through binding to EGF receptors 1 or 4. Membrane-bound HB-EGF exerts growth activity and adhesion capabilities
M Lanzrein et al.
The Biochemical journal, 310 ( Pt 1), 285-289 (1995-08-15)
Preincubation of Vero cells with 1 microM phorbol 12-myristate 13-acetate (PMA) decreased the specific binding of diphtheria toxin by about 50%, whereas the toxic effect, endocytic uptake and membrane translocation were completely blocked. Toxin bound to PMA-treated cells was released
Zizheng Li et al.
Communications biology, 4(1), 1076-1076 (2021-09-16)
Lysine-selective molecular tweezers are promising drug candidates against proteinopathies, viral infection, and bacterial biofilm. Despite demonstration of their efficacy in multiple cellular and animal models, important questions regarding their mechanism of action, including cell penetrance and intracellular distribution, have not
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