PRAP1 Protein, Human (HEK293, His)

Proline-rich acidic protein 1 (PRAP1) is a lipid-binding protein which promotes lipid absorption; negatively regulates the apoptotic process; gets involved in p53/TP53-dependent cell survival after DNA damage; causes cell cycle arrest; maintains normal growth homeostasis in epithelial cells and suppress mitotic spindle assembly checkpoint in hepatocellular carcinomas. PRAP1 Protein, Human (HEK293, His) is the recombinant human-derived PRAP1 protein, expressed by HEK293 , with C-6*His labeled tag.

Proline-rich acidic protein 1 (PRAP1) is a lipid-binding protein which promotes lipid absorption by facilitating MTTP-mediated lipid transfer (mainly triglycerides and phospholipids) and MTTP-mediated apoB lipoprotein assembly and secretion. PRAP1 also negatively regulates the apoptotic process, gets involved in p53/TP53-dependent cell survival after DNA damage and may cause cell cycle arrest. PRAP1 may play an important role in maintaining normal growth homeostasis in epithelial cells and may down-regulate the expression of MAD1L1, exerting a suppressive role in mitotic spindle assembly checkpoint in hepatocellular carcinomas^[1][2][3].

Human

HEK293

C-6*His

Q96NZ9/AAL16670.1 (V21-Q151)

118471  [NCBI]

VPAPKVPIKMQVKHWPSEQDPEKAWGARVVEPPEKDDQLVVLFPVQKPKLLTTEEKPRGQGRGPILPGTKAWMETEDTLGRVLSPEPDHDSLYHPPPEEDQGEERPRLWVMPNHQVLLGPEEDQDHIYHPQ

Approximately 20.0 kDa

Greater than 95% as determined by reducing SDS-PAGE.

Lyophilized powder.

Lyophilized from a 0.2 μm filtered solution of 20 mM PB, 150 mM NaCl, pH 7.4.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

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.