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Gibco™ Human EGF Recombinant Protein

Codice prodotto. 10125414
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Quantity:
100 μg
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Each
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Codice prodotto. Quantity unitSize
10125414 100 μg Each
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Les retours ne sont pas autorisés pour ce produit. Consulta la politica di reso
For Research Use Only. All usage must comply with product instructions.
 
Codice prodotto. 10125414 Fornitore Gibco™ N. del fornitore PHG0311L

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Les retours ne sont pas autorisés pour ce produit. Consulta la politica di reso
For Research Use Only. All usage must comply with product instructions.
 

Recombinant Protein

Carrier-Free.

EGF (Epidermal growth factor) exerts its actions by binding to the EGF Receptor, a 170 kDa protein kinase. Activation of EGFR initiates diverse cellular pathways in response to toxic environmental stimuli, or to EGF binding to the receptor, the EGFR forms homo- or heterodimers with other family members. Each dimeric receptor complex initiates a distinct signaling pathway by recruiting different Src homology 2 (SH2) containing effector proteins. EGF is far and wide expressed in kidney, cerebrum, prostrate and salivary glands. EGF acts as a potent mitogenic factor and the phosphorylated receptor recruits adapter proteins like GRB2 that activates complex downstream signaling cascades. EGF activates at least 4 major downstream signaling cascades including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STAT modules. Research studies suggest the protein may also play important role in activating the NF-kappa-B signaling cascade. Defects in the EGGF gene are the cause of hypomagnesemia type 4 and dysregulation has been associated with the growth and progression of certain cancers.
TRUSTED_SUSTAINABILITY

Specifica

Accession Number P01133
Concentration 1 mg/mL
For Use With (Application) Bioactivity
Formulation PBS with no preservative
Gene ID (Entrez) 1950
Molecular Weight (g/mol) 6.2 kDa
Name Human EGF
Purification Method Purified
Quantity 100 μg
Storage Requirements -20°C, Avoid Freeze/Thaw Cycles
Regulatory Status RUO
Endotoxin Concentration <0.1 ng/μg
Gene Alias AI790464; beta-urogastrone; EGF; Epidermal growth factor; epidermal growth factor (beta-urogastrone); epidermal growth factor precursor; H-EGF; HOMG4; Pro-epidermal growth factor; Pro-epidermal growth factor precursor (EGF); sb:eu639; URG; Urogastrone
Common Name EGF
Gene Symbol EGF
Biological Activity ED50 < 0.4 ng/mL; determined by the dose-dependent proliferation of mouse BALB/3T3 cells.
Product Type Protein
Conjugate Unconjugated
Species Human
Recombinant Recombinant
Sequence NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW ELR
Content And Storage -20°C, Avoid Freeze/Thaw Cycles
Classification Carrier-Free
Activity ED50 < 0.4 ng/mL; determined by the dose-dependent proliferation of mouse BALB/3T3 cells.
Endotoxin Level <0.1 ng/μg
Indicator Cell Balb/3T3 cells
Reactivity Human
Shipping Condition Dry Ice
Specific Activity 1.0 x 107 - 2.5 x 106 units⁄mg
Expression System E. coli
Protein Family Growth Factors & Receptors
Protein Form Recombinant, Ligand
Form Liquid
Protein Subtype EGF (Epidermal Growth Factor)
Research Category Stem Cell Research, Oncology
Product Line Gibco
Purity or Quality Grade >95% by SDS-PAGE
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It looks like the recombinant protein vial I received from you is empty. Is this normal?

Gibco recombinant proteins are frequently formulated without carrier proteins or additives (e.g., BSA, HSA, sucrose, etc.) and no Gibco PeproTech recombinant protein contains a carrier protein. As a result, during lyophilization, the protein product may be deposited on the vial as a thin, and sometimes invisible, film instead of a pellet. The size of the pellet, if any, is not directly related to the quantity of the recombinant protein in the vial. Our quality control procedures assure that each vial contains the correct amount of product.

To ensure complete recovery of protein product, before opening a vial of lyophilized recombinant protein, we recommend centrifuging it in a microcentrifuge for 20-30 seconds to drive any protein that may be lodged in the cap or on the side to the bottom of the vial. After reconstitution, you can confirm the presence of product protein by running a small amount on SDS-PAGE. In general, a protein band with expected size should be visible with as little as 10 ng of protein loaded on an acrylamide gel.

Why does my recombinant protein not show activity in my own experiment?

Assay time is critical. Each assay needs to beoptimized and performed at the peak response time. Different cells may respond differently to a growth factor or cytokine. We suggest repeating our QC assay using same indicator cells as suggested in the manual to see if you can obtain a similar response. In addition, serum may be masking the response. Serum starvation might be needed for certain types of assays.

How should I store the reconstituted recombinant proteins?

Protein solutions are generally not very stable when frozen at low concentration. Upon freeze and thaw, some proteins in the solution may stick to the wall of the container, which results in significant reduction of protein concentration if the starting concentration was low. Therefore, carrier proteins are used to reduce such loss. The most commonly used carrier proteins include bovine serum albumin (BSA), human serum albumin (HSA), or fetal bovine serum (FBS). These carrier proteins are generally used at 0.1% concentration. As a rule of thumb, if the concentration of the recombinant protein is less than 0.5 mg/mL, it is a good idea to add some carrier protein

How do I store my lyophilized recombinant protein?

Lyophilized proteins can typically be stored at 2 to 8 degrees C for several weeks, or stored dessicated at -20 degrees C for long-term storage.

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