Serpin E1 Protein, Mouse (N172S, R253G, HEK293, His)

Serpin E1 Protein, a serine protease inhibitor, regulates TMPRSS7 and is a primary inhibitor for tissue-type plasminogen activator (PLAT) and urokinase-type plasminogen activator (PLAU). It crucially down-regulates fibrinolysis, controlling blood clot degradation. As a PLAU inhibitor, Serpin E1 regulates cell adhesion and spreading, contributing to keratinocyte migration in cutaneous injury repair. Beyond protease inhibition, it regulates cell migration, influencing senescence, alveolar type 2 cells' senescence in the lung, cementogenic differentiation in periodontal ligament stem cells, and odontoblast differentiation in odontogenesis. Serpin E1 forms a heterodimer with TMPRSS7, interacts with proteins like VTN, PPP1CB, SORL1, LRP1, and PLAUR, emphasizing its multifaceted regulatory role. Serpin E1 Protein, Mouse (N172S, R253G, HEK293, His) is the recombinant mouse-derived Serpin E1 protein, expressed by HEK293 , with C-6*His labeled tag and N172S, R253G mutation. The total length of Serpin E1 Protein, Mouse (N172S, R253G, HEK293, His) is 380 a.a., with molecular weight of ~48.54 kDa.

Serpin E1, a serine protease inhibitor, exerts its regulatory functions through various mechanisms. It inhibits TMPRSS7 and serves as a primary inhibitor for both tissue-type plasminogen activator (PLAT) and urokinase-type plasminogen activator (PLAU). Acting as a crucial PLAT inhibitor, it plays a vital role in down-regulating fibrinolysis and orchestrates the controlled degradation of blood clots. In its capacity as a PLAU inhibitor, Serpin E1 is implicated in the regulation of cell adhesion and spreading. Beyond its role as a protease inhibitor, it acts as a regulator of cell migration, notably contributing to the stimulation of keratinocyte migration during cutaneous injury repair. Furthermore, Serpin E1 is involved in cellular and replicative senescence, playing a role in alveolar type 2 cells' senescence in the lung. Additionally, it participates in the regulation of cementogenic differentiation of periodontal ligament stem cells and influences odontoblast differentiation and dentin formation during odontogenesis. Serpin E1 forms a heterodimer with TMPRSS7, interacts with various proteins like VTN, PPP1CB, SORL1, LRP1, and PLAUR, and engages in complex interactions in different cellular contexts, emphasizing its multifaceted regulatory role.

Data is not available

Mouse

HEK293

C-6*His

P22777 (T23-P402, N172S, R253G)

18787  [NCBI]

TLPLRESHTAHQATDFGVKVFQQVVQASKDRNVVFSPYGVSSVLAMLQMTTAGKTRRQIQDAMGFKVNEKGTAHALRQLSKELMGPWNKNEISTADAIFVQRDLELVQGFMPHFFKLFQTMVKQVDFSEVERARFIINDWVERHTKGMISDLLAKGAVDELTRLVLVNALYFSGQWKTPFLEASTHQRLFHKSDGSTVSVPMMAQSNKFNYTEFTTPDGLEYDVVELPYQGDTLSMFIAAPFEKDVHLSALTNILDAELIRQWKGNMTRLPRLLILPKFSLETEVDLRGPLEKLGMPDMFSATLADFTSLSDQEQLSVAQALQKVRIEVNESGTVASSSTAFVISARMAPTEMVIDRSFLFVVRHNPTETILFMGQVMEP

Approximately 48.54 kDa

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  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.