catalog number :
MBS717039
products type :
Native Protein
products full name :
ovalbumin
products short name :
ovalbumin
products name syn :
Allergen Gal d II; Egg albumin; Plakalbumin
other names :
ovalbumin; Ovalbumin; ovalbumin; egg albumin; plakalbumin; allergen Gal d II; Allergen Gal d II; Egg albumin; Plakalbumin
other gene names :
SERPINB14; SERPINB14
uniprot entry name :
OVAL_CHICK
host :
Purified from chicken egg white
storage stability :
Aliquot and store at -20 degree C or -80 degree C. Avoid repeated freeze / thaw cycles.
tested application :
ELISA (EIA), Western Blot (WB)
other info1 :
Peptide: Full length native chicken egg ovalbumin
other info2 :
Storage Buffer: 20mM Tris-Hcl,50%glycerol
products description :
Storage protein of egg white. Lack protease inhibitory activity.
ncbi acc num :
NP_990483.1
ncbi gb acc num :
NM_205152.1
ncbi mol weight :
42,881 Da
uniprot summary :
Function: Non-inhibitory serpin. Storage protein of egg white. Ref.11 Ref.12. Subunit structure: Homodimer. Ref.17. Subcellular location: Secreted Ref.11. Tissue specificity: Major protein of egg white. Domain: The uncleaved signal peptide becomes available for membrane translocation of ovalbumin when the nascent chain is 50 to 60 residues long. The hydrophobic sequence, which lies between residues 27 and 43, folds back on the preceding residues to form an amphipathic hairpin structure which is the signal element recognized by the membrane.Unlike other serpins, after protease cleavage at the P-P' site, ovalbumin does not have the ability to undergo the conformational transition into the loop-inserted reactive-center-containing thermostabilized form. The bulky arginine residue (Arg-340) at the hinge region appears to be responsible for this lack of loop-inserted conformational change, but not for the absence of serpin inhibitory activity.During storage of fertilized and non-fertilized eggs or under alkaline conditions, the native ovalbumin conformer (N-ovalbumin) is transformed into a thermostabilized conformer, S-ovalbumin. Ser-165, Ser-237 and Ser-321 take on a D-configuration in this conformer and may be responsible for the thermostability. Post-translational modification: Undergoes proteolytic cleavage first at the canonical P1-P1' site, and then at the P8-P7 site by subtilisin. Allergenic properties: Can cause an allergic reaction in humans. Sequence similarities: Belongs to the serpin family. Ov-serpin subfamily.