RET Protein, Human (HEK293, His)

RET protein is a receptor tyrosine protein kinase that plays a key role in cell proliferation, neuronal navigation, and differentiation upon binding to glial cell-derived neurotrophic factor family ligands. It regulates the delicate balance between cell death and survival, influences positional information, and is critical for intestinal organogenesis, enteric nervous system development, renal organogenesis, and Peyer's patch formation. RET Protein, Human (HEK293, His) is the recombinant human-derived RET protein, expressed by HEK293 , with N-His labeled tag.

The RET protein, a receptor tyrosine-protein kinase, plays a crucial role in diverse cellular processes such as cell proliferation, neuronal navigation, migration, and differentiation upon binding with glial cell-derived neurotrophic factor family ligands. It phosphorylates PTK2/FAK1 and regulates the delicate balance between cell death and survival, as well as positional information. Essential for the molecular coordination during intestine organogenesis, RET is involved in the development of the enteric nervous system, renal organogenesis, and promotes the formation of Peyer's patch-like structures in the gut-associated lymphoid tissue. Furthermore, RET modulates cell adhesion, mediated by caspase cleavage in sympathetic neurons, and facilitates cell migration in an integrin-dependent manner. Operating as a dependence receptor, it triggers apoptosis in the absence of the ligand GDNF in somatotrophs but promotes survival and downregulates growth hormone production in its presence. RET is a key mediator in various diseases, particularly neuroendocrine cancers characterized by aberrant integrins-regulated cell migration. Additionally, it mediates GDF15-induced cell signaling in the brainstem through interaction with GFRAL, resulting in the inhibition of food intake and activation of MAPK- and AKT-signaling pathways. Notably, isoform 1 in complex with GFRAL induces higher activation of the MAPK-signaling pathway compared to isoform 2 in the same complex.

The enzyme activity of this recombinant protein is testing in progress, we cannot offer a guarantee yet.

Human

HEK293

N-His

P07949-1 (L29-R635)

5979  [NCBI]

LYFSRDAYWEKLYVDQAAGTPLLYVHALRDAPEEVPSFRLGQHLYGTYRTRLHENNWICIQEDTGLLYLNRSLDHSSWEKLSVRNRGFPLLTVYLKVFLSPTSLREGECQWPGCARVYFSFFNTSFPACSSLKPRELCFPETRPSFRIRENRPPGTFHQFRLLPVQFLCPNISVAYRLLEGEGLPFRCAPDSLEVSTRWALDREQREKYELVAVCTVHAGAREEVVMVPFPVTVYDEDDSAPTFPAGVDTASAVVEFKRKEDTVVATLRVFDADVVPASGELVRRYTSTLLPGDTWAQQTFRVEHWPNETSVQANGSFVRATVHDYRLVLNRNLSISENRTMQLAVLVNDSDFQGPGAGVLLLHFNVSVLPVSLHLPSTYSLSVSRRARRFAQIGKVCVENCQAFSGINVQYKLHSSGANCSTLGVVTSAEDTSGILFVNDTKALRRPKCAELHYMVVATDQQTSRQAQAQLLVTVEGSYVAEEAGCPLSCAVSKRRLECEECGGLGSPTGRCEWRQGDGKGITRNFSTCSPSTKTCPDGHCDVVETQDINICPQDCLRGSIVGGHEPGEPRGIKAGYGTCNCFPEEEKCFCEPEDIQDPLCDELCR

110-120 kDa

Greater than 90% as determined by reducing SDS-PAGE.

Lyophilized powder.

Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.