Merck
Todas as fotos(3)

Documentos

E5036

Sigma-Aldrich

Fator de crescimento epidérmico

EGF, recombinant, expressed in Escherichia coli, >97% (SDS-PAGE)

Faça loginpara ver os preços organizacionais e de contrato

Sinônimo(s):
EGF
Número CAS:
Número MDL:
NACRES:
NA.77

fonte biológica

human

Nível de qualidade

recombinante

expressed in E. coli

Ensaio

>97% (SDS-PAGE)

forma

lyophilized powder

potência

0.08-0.8 ng/mL EC50

peso molecular

~6 kDa

embalagem

pkg of 200 and 500 μg

condição de armazenamento

avoid repeated freeze/thaw cycles

Impurezas

≤1 EU/μg Endotoxin

cor

white

solubilidade

water: soluble 0.190-0.210, clear, colorless

nº de adesão UniProt

temperatura de armazenamento

−20°C

Informações sobre genes

human ... EGF(1950)

Procurando produtos similares? Visit Guia de comparação de produtos

Comparar Itens Semelhantes

Ver Comparação Total

Mostrar diferenças

1 of 4

Este Item
E9644E4643GF316
Fator de crescimento epidérmico EGF, recombinant, expressed in Escherichia coli, >97% (SDS-PAGE)

E5036

Fator de crescimento epidérmico

hEGF EGF, recombinant, expressed in E. coli, lyophilized powder, suitable for cell culture

E9644

hEGF

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

E4643

Heparin-Binding EGF-Like Growth Factor human

Sigma-Aldrich

GF316

EGF Protein, Human Recombinant Animal Free

biological source

human

biological source

human

biological source

human

biological source

-

recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

expressed in baculovirus infected Sf21 cells

recombinant

expressed in E. coli

Quality Level

200

Quality Level

300

Quality Level

100

Quality Level

100

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

form

-

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

-

Descrição geral

Epidermal Growth Factor (EGF) is a small mitogenic polypeptide (∼6 kDa), which is present in many mammalian species and is distributed throughout a wide number of tissues and body fluids. Human EGF is identical to β-urogastrone, a polypeptide which was recognized and isolated on the basis of its ability to inhibit gastric acid secretion. EGF is a member of a growth factor family, which is characterized by the presence of 6 conserved cysteine motifs that form three disulfide bonds. The location of 3 intrachain disulfide bonds in recombinant human EGF is identical to that of mouse EGF. EGF is homologous to a sequence contained in a 19 kDa protein of vaccinia virus, which appears to utilize the EGF receptor to gain entry into cell† EGF is mitogenic for a variety of epidermal and epithelial cells, including fibroblasts, glial cells, mammary epithelial cells, vascular and corneal endothelial cells, bovine granulosa, rabbit chondrocytes, HeLa cells, and SV40-3T3 cells.
Epidermal growth factor (EGF) is synthesized in Henle′s loop and the distal convoluted tubule in the kidney. It is also produced in salivary glands and duodenum.

Aplicação

Epidermal Growth Factor, human, animal component free has been used:
  • as a supplement in in LHC-8 medium to culture liver cell lines
  • in the fetal bovine serum (FBS)-Dulbecco′s modified essential medium (DMEM) /F12 medium for primary culture of human glioma cells
  • as an additive in the conditional medium of normal fibroblasts (NFs) to study its effect on the migration and invasion of endometrial cancer (EC) cells
  • as a component in tumorsphere medium

Ações bioquímicas/fisiológicas

Epidermal growth factor (EGF) helps to induce cell growth, proliferation and differentiation. It participates in the repairing of renal tissues in the kidney. It promotes the reabsorption of magnesium with the help of the transient receptor potential cation channel 6 (TRMP6). EGF is known to participate in the pathophysiology of drug-induced renal magnesium loss.

Citação

1. Carpenter, G., and Cohen, S., Rapid enhancement of protein phosphorylation in A-431 cell membrane preparations by epidermal growth factor. Annu. Rev. Biochem., 48, 193-216 (1979).
2. Gregory, H., Isolation and structure of urogastrone and its relationship to epidermal growth factor. Nature, 257, 325-327 (1975).
3. George-Nascimento, C. et al., Characterization of recombinant human epidermal growth factor produced in yeast. Biochemistry, 27, 797-802 (1988).
4. Todaro, G.J. et al., Transforming growth factors produced by certain human tumor cells: polypeptides that interact with epidermal growth factor receptors. Proc. Natl. Acad. Sci. USA, 77, 5258-5262 (1980).
5. Blomquist, M.C. et al., Vaccinia virus 19-kilodalton protein: relationship to several mammalian proteins, including two growth factors. Proc. Natl. Acad. Sci. USA, 81, 7363-7367 (1984).
6. Eppstein, D.A. et al., Epidermal growth factor receptor occupancy inhibits vaccinia virus infection. Nature, 318, 663-665 (1985).

Código de classe de armazenamento

13 - Non Combustible Solids

Classe de risco de água (WGK)

WGK 2

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable


Certificados de análise (COA)

Busque Certificados de análise (COA) digitando o Número do Lote do produto. Os números de lote e remessa podem ser encontrados no rótulo de um produto após a palavra “Lot” ou “Batch”.

Já possui este produto?

Os documentos relacionados aos produtos que você comprou no passado foram reunidos na Biblioteca de Documentos para sua conveniência.

Visite a Biblioteca de Documentos

Dificuldade em encontrar seu produto ou número de lote?

Os números dos produtos são combinados com os tamanhos/quantidades da embalagem quando exibidos no site (exemplo: T1503-25G). Por favor, certifique-se você insere APENAS o número do produto no campo Número do produto (exemplo: T1503).

Exemplo

T1503
Número do produto
-
25G
Tamanho/quantidade da embalagem

Exemplos adicionais:

705578-5MG-PW

PL860-CGA/SHF-1EA

MMYOMAG-74K-13

1000309185

inserir como 1.000309185)

Está com problemas? Sinta-se à vontade para entrar em contato Assistência Técnica para obter assistência

Os números de lote e remessa podem ser encontrados no rótulo de um produto após a palavra “Lot” ou “Batch”.

Produtos Aldrich

  • Se encontrar um número de lote como TO09019TO - insira o número do lote 09019TO sem as duas primeiras letras.

  • Se encontrar um número de lote com um código de preenchimento, como 05427ES-021 - insira o número do lote 05427ES sem o código de preenchimento -021.

  • Se encontrar um número de lote com um código de preenchimento como STBB0728K9 - digite o número do lote STBB0728 sem o código de preenchimento K9.

Não encontra o que está procurando?

Em alguns casos, um COA pode não estar disponível on-line. Se a sua pesquisa não encontrou o COA, você pode solicitar um.

Solicitar COA

Os clientes também visualizaram

Slide 1 of 6

1 of 6

EGF-receptor human recombinant, expressed in CHO cells, ≥95% (SDS-PAGE), ≥95% (HPLC), suitable for cell culture

Sigma-Aldrich

SRP3028

EGF-receptor human

Fibroblast Growth Factor-Basic FGF-Basic, from human, recombinant, expressed in E. coli, carrier free

Sigma-Aldrich

F3685

Fibroblast Growth Factor-Basic

Hidrocortisona BioReagent, suitable for cell culture

Sigma-Aldrich

H0888

Hidrocortisona

Epidermal Growth Factor Receptor human buffered aqueous glycerol solution, 5,000-30,000 units/mg protein (Lowry)

Sigma-Aldrich

E3641

Epidermal Growth Factor Receptor human

Sigma-Aldrich

Sigma-Aldrich

SRP4037

FGF-2 human

Epidermal growth factor and its influencing variables in healthy children and adults
Meybosch S, et al.
Testing, 14(1), e0211212-e0211212 (2019)
In vitro tumorsphere formation assays
Johnson S, et al.
Bio-protocol, 3(3), e325-e325 (2013)
Cancer-associated fibroblasts induce epithelial-mesenchymal transition through secreted cytokines in endometrial cancer cells
Wang X, et al.
Oncology Letters, 15(4), 5694-5702 (2018)
Gab3 overexpression in human glioma mediates Akt activation and tumor cell proliferation
Jia P, et al.
Testing, 12(3), e0173473-e0173473 (2017)
Isako Saga et al.
Neuro-oncology, 16(8), 1048-1056 (2014-05-27)
The metabolic preference of malignant glioma for glycolysis as an energy source is a potential therapeutic target. As a result of the cellular heterogeneity of these tumors, however, the relation between glycolytic preference, tumor formation, and tumor cell clonogenicity has

Artigos

Role of growth factors in stem cell differentiation and various growth factors for your research at sigmaaldrich.com

Nossa equipe de cientistas tem experiência em todas as áreas de pesquisa, incluindo Life Sciences, ciência de materiais, síntese química, cromatografia, química analítica e muitas outras.

Entre em contato com a assistência técnica