NBP1-46267 Amphiregulin

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Product Description for Amphiregulin

Presentation: Purified

Properties for Amphiregulin

Product Category Proteins & Growth Factors
Target Category
Quantity 5 µg
Synonyms AREG, CRDGF, Colorectum cell-derived growth factor, SDGF, Schwannoma-Derived Growth Factor
Presentation Purified
Reactivity Hu
Molecular weight 29.3 kDa
Species (Protein) Human
Shipping to Not USA/Canada
PDF datasheet View Datasheet
Manufacturer Novus Biologicals Inc.

Datasheet Extract

Swiss Prot Num:
Background Amphiregulin is an epidermal growth factor (EGF)-related glycoprotein that is expressed in a variety of tissues including ovary, placenta, lung, kidney, stomach, colon and breast. As an EGF-related growth factor, Amphiregulin is involved in the differentiation and proliferation of a wide range of cell types and these actions are mediated through binding to the EGF receptor. Amphiregulin plays an important role in neoplastic disease states. It has been demonstrated that Amphiregulin is over-expressed in a wide spectrum of cancers including prostate, colorectal, mammary, kidney, bladder, ovary, pancreas, lung, and gliomas. Amphiregulin levels also correlate with reduced survival in patients with non-small cell lung cancer and pancreatic cancer. Therefore, Amphiregulin may promote tumor progression in an autocrine fashion. Conversely, studies have also shown that Amphiregulin can inhibit proliferation of certain cancer cell lines such as A431 human epidermoid cancer cells. Recent studies indicate that Amphiregulin may also act as a protective factor in response to liver damage. Amphiregulin is synthesized as a 252 amino acid precursor glycoprotein with 3 potential N-glycosylation sites. It comprises a 19 amino acid signal peptide and 2 propeptide domains at the N-terminus and C-terminus. The C-terminus propeptide acts as a potential transmembrane domain. The mature form of amphiregulin is reported to be 84aa in length, however the in vitro TACE cleavage site has been shown to be 3 aa downstream generating a mature protein of 87aa. Furthermore, the recombinant 87aa form has been shown to be more active than the recombinant 84aa form. Amphiregulin (mature form)has been confirmed to be 87aa. This is a HCX protein. HCX Expression System Details HCX proteins mimic the proteins in the human body because they are expressed from human, rather than animal, insect or bacterial cells. This process gives them human post-translational modifications. Recombinant DNA techniques allow a human protein with the correct amino acid sequence to be expressed in a non-human cell line. However, non-human cells lack the appropriate cellular machinery, such as specific glycosyltransferases, necessary to produce the correct human post-translational modifications of a protein. An extreme example is seen in E. coli cells, which produce recombinant proteins with no glycosylation, as the above figure illustrates. Rodent and yeast cells are able to glycosylate proteins, but they are still different from glycosylation in human cells. Expression System Resultant Proteins Human (e.g. K562, HEK293) Correct amino acid sequence Human post-translational modifications Rodent (e.g. CHO, NSO) Correct amino acid sequence Some natural glycosylation - not human-like Yeast (e.g. Pichia) Correct amino acid sequence Some natural glycosylation - not human-like E.Coli Correct amino acid sequence No PTMs Although there have been significant attempts to make non-human cell derived cytokines more human-like, there is a growing awareness that in many instances, particularly in therapeutics, cytokines should mimic those found in the body as closely as possible.
Concentration Lyoph mg/ml
General Readings Berasain C et al. (2005) J Biol Chem 280(19): 19012-20.
Storage Store at -80C. Avoid freeze-thaw cycles.
Buffer System:
Lyophilized: When reconstituted in 0.5 ml sterile 5mM acetic acid, the solution will contain 1% human serum albumin (HSA) and 10% trehalose.
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