Matriptase/ST14 Catalytic Domain 蛋白, Mouse (His)

The Matriptase/ST14 catalytic domain protein exhibits serine-type endopeptidase activity and is critical in processes as diverse as placental branching and neural tube closure. It is an extrinsic component of the plasma membrane and is expressed in structures such as the digestive system, early concepts, genitourinary system, pituitary gland, and sense organs. Matriptase/ST14 Catalytic Domain Protein, Mouse (His) is the recombinant mouse-derived Matriptase/ST14 Catalytic Domain protein, expressed by E. coli , with N-6*His labeled tag.

Matriptase/ST14 蛋白的催化结构域表现出丝氨酸型内肽酶活性，并在各种过程的上游发挥着至关重要的作用，包括参与胎盘分支和神经管闭合的上皮细胞形态发生。该蛋白作为质膜的外在成分位于细胞外区域，在多种结构中表达，例如消化系统、早期概念、泌尿生殖系统、垂体和感觉器官。对 Matriptase/ST14 功能的研究对于了解其在生理过程中的参与具有重要意义，并可能有助于深入了解干燥综合征等疾病。该基因的人类直系同源物 ST14（ST14 跨膜丝氨酸蛋白酶基质酶）与常染色体隐性遗传先天性鱼鳞病 11 有关，突出了其在遗传性疾病中的潜在意义。

Measured by its ability to cleave the fluorogenic peptide substrate BOC-Gln-Ala-Arg-AMC (HY-134432A) that incubate at room temperature for 5 min. The specific activity is 16782.82 pmol/min/µg.

Mouse

E. coli

N-6*His

NP_035306 (G596-V855)

19143

GSDEKNCDCGLRSFTKQARVVGGTNADEGEWPWQVSLHALGQGHLCGASLISPDWLVSAAHCFQDDKNFKYSDYTMWTAFLGLLDQSKRSASGVQELKLKRIITHPSFNDFTFDYDIALLELEKSVEYSTVVRPICLPDATHVFPAGKAIWVTGWGHTKEGGTGALILQKGEIRVINQTTCEDLMPQQITPRMMCVGFLSGGVDSCQGDSGGPLSSAEKDGRMFQAGVVSWGEGCAQRNKPGVYTRLPVVRDWIKEHTGV

Approximately 28 kDa (major) and minor auto-activation fragments

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

无菌粉末

Lyophilized from a 0.22 μm filtered solution of PBS, 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.