Recombinant Human Annexin A8/ANXA8 Protein (His Tag) | PKSH030551

(No reviews yet) Write a Review
SKU:
575-PKSH030551
Weight:
1.00 KGS
€1,120.00
Frequently bought together:

Description

Recombinant Human Annexin A8/ANXA8 Protein (His Tag) | PKSH030551 | Gentaur US, UK & Europe Disrtribition

Synonyms: Annexin A8; Annexin VIII; Annexin-8; Vascular Anticoagulant-Beta; VAC-Beta; ANXA8; ANX8

Active Protein: N/A

Activity: A DNA sequence encoding the human ANXA8 (AAH73755.1) (Met1-Pro327) was expressed with a polyhistidine tag at the N-terminus.

Protein Construction: A DNA sequence encoding the human ANXA8 (AAH73755.1) (Met1-Pro327) was expressed with a polyhistidine tag at the N-terminus.

Fusion Tag: N-His

Species: Human

Expressed Host: E.coli

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

Purity: > 95 % as determined by reducing SDS-PAGE.

Endotoxin: Please contact us for more information.

Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

Molecular Mass: 39.1 kDa

Formulation: Lyophilized from sterile PBS, pH 7.4

Reconstitution: Please refer to the printed manual for detailed information.

Background: DPEP2 (MBD-2) belongs to the membrane-bound dipeptidase family. There are three members of this family as membrane-bound dipeptidase-1 (MBD-1), membrane-bound dipeptidase-2 (MBD-2) and membrane-bound dipeptidase-3 (MBD-3).MBD-2 is expressed at highest levels in lung, heart, and testis and at some what lower levels in spleen.MBD-2 is membrane-bound through a glycosylphosphatidyl-inositol linkage and probably is a metalloprotease which hydrolyzes leukotriene D4 (LTD4) into leukotriene E4 (LTE4).It is generally recognized that rapid cleavage of LTD4 is important in inactivating the broncho-and vaso-constrictive effects of cysteinyl LTs in asthmatic and inflammatory processes.

Research Area: N/A

View AllClose