Recombinant Human Serine Protease HTRA2/HTRA2/Omi (C-6His)(Discontinued)

Product code: 32-7615

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Amount : 50 µg
Content : Supplied as a 0.2 µm filtered solution of 20mM Tris,150mM NaCl,pH7.5.
Storage condition : Store at -20°C, stable for 6 months after receipt. Please minimize freeze-thaw cycles.
AA sequence : AVPSPPPASPRSQYNFIADVVEKTAPAVVYIEILDRHPFLGREVPISNGSGFVVAADGLIVTNAHVVADRRRVRVRLLSGDTYEAVVTAVDPVADIATLRIQTKEPLPTLPLGRSADVRQGEFVVAMGSPFALQNTITSGIVSSAQRPARDLGLPQTNVEYIQTDAAIDFGNSGGPLVNLDGEVIGVNTMKVTAGISFAIPSDRLREFLHRGEKKNSSSGISGSQRRYIGVMMLTLSPSILAELQLREPSFPDVQHGVLIHKVILGSPAHRAGLRPGDVILAIGEQMVQNAEDVYEAVRTQSQLAVQIRRGRETLTLYVTPEVTEVDHHHHHH
Gene : HTRA2
Gene ID : 27429
Uniprot ID : O43464
Source: Human Cells.
MW :36kD.
Recombinant Human HTRA2 is produced by our Mammalian expression system and the target gene encoding Ala134-Glu458 is expressed with a 6His tag at the C-terminus. High temperature requirement protein A2(HTRA2) is a single-pass membrane protein .It contains 1 PDZ (DHR) domain and belongs to the peptidase S1C family. HtrA2 can be released from the mitochondria during apoptosis and uses its four most N-terminal amino acids to mimic a caspase and be recruited by IAP caspase inhibitors such as XIAP and CIAP1/2. It promotes or induces cell death either by direct binding to and inhibition of BIRC proteins (also called inhibitor of apoptosis proteins, IAPs), leading to an increase in caspase activity, or by a BIRC inhibition-independent, caspase-independent and serine protease activity-dependent mechanism. The protein cleaves THAP5 and promotes its degradation during apoptosis.

Endotoxin : Less than 0.1 ng/µg (1 IEU/µg) as determined by LAL test.

For Research Use Only. Not for use in diagnostic/therapeutics procedures.

Subcellular location: Mitochondrion intermembrane space, Mitochondrion membrane
Post transnational modification: Autoproteolytically activated.
Tissue Specificity: Isoform 1 is ubiquitous. Isoform 2 is expressed predominantly in the kidney, colon and thyroid.
BioGrid: 118165. 70 interactions.
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