Human Folliculin (FLCN) Protein

Product specifications

Proteins and Peptides

Folliculin (FLCN)

E. coli

Human

Unconjugated

Molecular Weight: Calculated MW: 40.6 kDa  Observed MW: 41 kDa
Concentration: Prior to lyophilization: 200 µg/ml
Sequence Fragment: Arg341-Asn579
Tag: N-terminal His tag and SUMO tag

Recombinant

> 90%

10 µg

50 µg

100 µg

200 µg

500 µg

Lyophilized To keep the original salt concentration, we recommend reconstituting to the original concentration prior to lyophilization (see Concentration) in ddH2O. If a lower concentration is required, dilute in PBS, pH 7.4. If a higher concentration is required, the product can be reconstituted directly in PBS, pH 7.4, though please note that this will change the overall salt concentration. The stock concentration should be between 0.1-1.0 mg/ml. Do not vortex.

WB, SDS-PAGE

Prior to lyophilization: PBS, pH 7.4, containing 0.01% Sarcosyl, 1 mM DTT, 5% Trehalose and Proclin-300.

Shipped within 5-7 working days.

Store at 2-8 °C for up to one month. Store at -80 °C for up to one year. Avoid repeated freeze/thaw cycles.

No

BHD,FLCL,DENND8B,Birt-Hogg-Dube syndrome protein,BHD skin lesion fibrofolliculoma protein

Protein FLCN

RUO

This product is for research use only.   Not for human consumption, cosmetic, therapeutic or diagnostic use.

Descripción

Folliculin (FCLN) is a tumor suppressor protein encoded by the FLCN gene and plays a key role in cellular energy sensing, metabolic regulation, and mTOR signaling pathways. It is widely implicated in Birt-Hogg-Dubé syndrome (BHD), a rare autosomal dominant disorder associated with renal cell carcinoma, lung cysts, and fibrofolliculomas. FCLN functions as a GTPase-activating protein (GAP) for RagC and RagD GTPases, facilitating the activation of the mTORC1 complex on lysosomal membranes in response to nutrient availability. Dysregulation of FCLN can lead to abnormal mTORC1 signaling, promoting unchecked cellular proliferation and metabolic imbalances. Folliculin is expressed in a variety of tissues, with high levels in the kidney, lung, and skin, correlating with the phenotypic manifestations of BHD. Structural studies indicate that FCLN forms a complex with folliculin-interacting proteins (FNIP1 and FNIP2), enhancing its role in AMPK regulation and energy homeostasis. Emerging research suggests that FCLN also influences autophagy and lysosomal biogenesis, positioning it as a critical regulator of cellular stress responses. Loss of function or mutations in FCLN disrupt cellular homeostasis, making cells more susceptible to oncogenic transformation. FCLN's interactions with FNIPs and its role in integrating metabolic and nutrient signals highlight its significance in maintaining cellular and tissue-level equilibrium.

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