AHSP / ERAF Protein (Native)

Sino Biological Inc. liefert AHSP / ERAF Protein (Native) mit höherer Qualität und günstiger Kosten im Vergleich mit anderen globalen Lieferanten.

Weitere Informationen über AHSP / ERAF Protein (Native) lesen Sie bitte:http://www.sinobiological.com/AHSP-ERAF-Protein-Antibody-a-6209.html

Produkt-Information von AHSP / ERAF Protein

QC Testing von AHSP / ERAF Protein

Purity	> 90 % as determined by SDS-PAGE	SDS-PAGE: AHSP protein
Endotoxin	Please contact us for more information.
Stability	Samples are stable for up to twelve months from date of receipt at -70℃
Predicted N terminal	Met
Molecular Mass	The recombinant human ERAF consists of  102 amino acids and predicts a molecular mass of 11.8 KDa. It migrates as an approximately 12 KDa band in SDS-PAGE under reducing conditions.
Formulation	Lyophilized from sterile PBS, pH 7.4. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA. Please contact us for any concerns or special requirements.

Usage Guide von AHSP / ERAF Protein

Verwandte Produkte & Themen von AHSP / ERAF Protein

Beschreibung von AHSP / ERAF Protein

AHSP, also known as ERAF, is a conserved mammalian erythroid protein which belongs to the AHSP family. It is expressed in blood and bone marrow. AHSP facilitates the production of Hemoglobin A by stabilizing free α-globin. It rapidly binds to ferrous α with association (k'(AHSP)) and dissociation (k(AHSP)) rate constants of ≈10 μm(-1) s(-1) and 0.2 s(-1), respectively, at pH 7.4 at 22 ℃. A small slow phase was observed when AHSP binds to excess ferrous αCO. This slow phase appears to be due to cis to trans prolyl isomerization of the Asp(29)-Pro(30) peptide bond in wild-type AHSP because it was absent when αCO was mixed with P30A and P30W AHSP, which are fixed in the trans conformation. This slow phase was also absent when met(Fe(3+))-α reacted with wild-type AHSP, suggesting that met-α is capable of rapidly binding to either Pro(30) conformer. Both wild-type and Pro(30)-substituted AHSPs drive the formation of a met-α hemichrome conformation following binding to either met- or oxy(Fe(2+))-α. The dissociation rate of the met-α·AHSP complex (k(AHSP) ≈ 0.002 s(-1)) is ～100-fold slower than that for ferrous α·AHSP complexes, resulting in a much higher affinity of AHSP for met-α. Thus, in vivo, AHSP acts as a molecular chaperone by rapidly binding and stabilizing met-α hemichrome folding intermediates. The low rate of met-α dissociation also allows AHSP to have a quality control function by kinetically trapping ferric α and preventing its incorporation into less stable mixed valence Hemoglobin A tetramers. Reduction of AHSP-bound met-α allows more rapid release to β subunits to form stable fully, reduced hemoglobin dimers and tetramers.

References

1. Miele G. et al., 2001, Nat Med. 7 (3): 361-4.
2. Kihm AJ. et al., 2002, Nature. 417 (6890): 758-63.
3. Florio P. et al., 2004, Steroids. 68 (10-13): 801-7.
4. Miele G. et al., 2001, Nat Med. 7 (3): 361-4.
5. Mollan TL. et al., 2012, J Biol Chem. 287 (14): 11338-50.