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Recombinant Human EGF Protein (FITC)

Bioactive

ActiBioPure™

Azide Free

Features and benefits

Expression System: Pichia pastoris
Protein Tag: No tag
Bioactivity: Binding EGFR

Item Number

rp170192

Grouped product items
SKU	Size	Availability	Price	Qty
rp170192-10μg (Trial Size) Apply for free trial size（?） Every year, as a valued customer, you have the exclusive opportunity to explore and enjoy three different trial products of your choice, absolutely free!	10μg	Available within 8-12 weeks(?) Production requires sourcing of materials. We appreciate your patience and understanding.	$599.90
rp170192-20μg	20μg	Available within 4-8 weeks(?) Items will be manufactured post-order and can take 4-8 weeks. Thank you for your patience!	$999.90

EGF-FITC, Active, Pichia pastoris, No tag, 971-1021aa

View related series

Click to view protein information: EGF

Accession#:P01133 EGF Gene ID:1950

Basic Description

Product Name	Recombinant Human EGF Protein (FITC)
Synonyms	beta-urogastrone \| EGF \| epidermal growth factor (beta-urogastrone) \| epidermal growth factor \| hEGF \| HOMG4 \| pro-epidermal growth factor \| URG \| Urogastrone \| EGF
Grade	ActiBioPure™, Azide Free, Bioactive
Product Description	Introduction: Epidermal growth factor (EGF) is a hormone that stimulates division of epidermal and other cells. EGF (FITC) conjugate, which remains fully active after conjugation and can be used to study EGF receptor in cells. Fluorescently labeled EGF has enabled researchers to investigate receptor-membrane interactions, study receptor distribution, calculate rate constants for the interaction of EGF with its receptor, and more. Conjugation: The EGF was conjugated with FITC under optimum conditions, and unreacted FITC was removed. The number of fluorophore molecules on each EGF molecule is 1.0. Recommended Usage： Fluorescence is typically monitored using a flow cytometer, fluorescence microscope, or fluorimeter. For immunofluorescent staining, the recommended use of this reagent is ≤ 0.5µg per million cells in 100 µl staining volume. It is recommended that the reagent be titrated for optimal performance for different cell lines.
Specifications & Purity	ActiBioPure™, Bioactive, Azide Free
Bioactivity	Binding EGFR
Expression System	Pichia pastoris
Species	Human
Amino Acids	971-1021 aa
Sequence	NSDSECPLSHDGYCLHDGVCMYIEALDKYACNCVVGYIGERCQYRDLKWWE
Protein Tag	No tag
Conjugation	FITC

Product Specifications

Form	Lyophilized
Reconstitution	This product should be reconstituted in 100μL of deionized water to make a 0.2mg/mL stock solution. Prepare working dilution on day of use. Stock solution is stable for about 8 weeks at 2-8°C as an undiluted liquid. Avoid freeze-thaw cycles. Protect fluor
Storage Temp	Protected from light,Store at -20°C
Shipped In	Ice chest + Ice pads
Stability And Storage	The lyophilized products should be stored at –20°C until use. Allow the product to warm to room temperature before opening. Protect from light. When stored properly, the products should be stable for at least 12 months.

Lot Number

Certificate Type

Date

Item

ZJ23R0700043

Certificate of Analysis

Jul 17, 2023

rp170192

References

1. Ogiso H, Ishitani R, Nureki O, Fukai S, Yamanaka M, Kim JH, Saito K, Sakamoto A, Inoue M, Shirouzu M et al.. (2002) Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains.. Cell, 110 (6): (775-87). [PMID:12297050] [10.1021/op500134e]
2. Lesuisse D, Mauger J, Nemecek C, Maignan S, Boiziau J, Harlow G, Hittinger A, Ruf S, Strobel H, Nair A, Ritter K, Malleron JL, Dagallier A, El-Ahmad Y, Guilloteau JP, Guizani H, Bouchard H, Venot C.. (2011) Discovery of the first non-ATP competitive IGF-1R kinase inhibitors: advantages in comparison with competitive inhibitors.. Bioorg Med Chem Lett, 21 (8): (2224-2228). [PMID:21441024] [10.1016/j.bmcl.2011.03.003]
3. Gregory, H H and Preston, B M BM.. (1977) The primary structure of human urogastrone.. International journal of peptide and protein research, [PMID:300079]
4. Hommel, U U, Harvey, T S TS, Driscoll, P C PC and Campbell, I D ID.. (1992) Human epidermal growth factor. High resolution solution structure and comparison with human transforming growth factor alpha.. Journal of molecular biology, (5): [PMID:1522591]
5. Furuya, M M, Akashi, S S and Hirayama, K K.. (1989) The primary structure of human EGF produced by genetic engineering, studied by high-performance tandem mass spectrometry.. Biochemical and biophysical research communications, (15): [PMID:2789514]
6. Bell, G I GI and 8 more authors.. (1986) Human epidermal growth factor precursor: cDNA sequence, expression in vitro and gene organization.. Nucleic acids research, (11): [PMID:3491360]
7. Lu, H S HS and 5 more authors.. (2001) Crystal structure of human epidermal growth factor and its dimerization.. The Journal of biological chemistry, (14): [PMID:11438527]
8. Ferguson, Kathryn M KM and 5 more authors.. (2003) EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization.. Molecular cell, [PMID:12620237]
9. Groenestege, Wouter M Tiel WM and 10 more authors.. (2007) Impaired basolateral sorting of pro-EGF causes isolated recessive renal hypomagnesemia.. The Journal of clinical investigation, [PMID:17671655]
10. Lu, Chafen C and 6 more authors.. (2010) Structural evidence for loose linkage between ligand binding and kinase activation in the epidermal growth factor receptor.. Molecular and cellular biology, [PMID:20837704]
11. Huang, Hsiao-Wen HW, Mohan, Sepuru K SK and Yu, C C.. (2010) The NMR solution structure of human epidermal growth factor (hEGF) at physiological pH and its interactions with suramin.. Biochemical and biophysical research communications, (26): [PMID:21029725]
12. Zettl, Markus M, Adrain, Colin C, Strisovsky, Kvido K, Lastun, Viorica V and Freeman, Matthew M.. (2011) Rhomboid family pseudoproteases use the ER quality control machinery to regulate intercellular signaling.. Cell, (1): [PMID:21439629]

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Recombinant Human EGF Protein (FITC)

Basic Description

Product Specifications

Certificates

Certificate of Analysis(COA)

Related Documents

References

Solution Calculators

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