Recombinant Human AHSP Protein

Beta LifeScience SKU/CAT #: BLPSN-0111

Recombinant Human AHSP Protein

Beta LifeScience SKU/CAT #: BLPSN-0111
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Product Overview

Tag N/A
Host Species Human
Accession Q9NZD4
Synonym EDRF, ERAF
Background 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 alpha-globin. It rapidly binds to ferrous alpha with association (k'(AHSP)) and dissociation (k(AHSP)) rate constants of ≈1 μm(-1) s(-1) and .2 s(-1), respectively, at pH 7.4 at 22 °C. A small slow phase was observed when AHSP binds to excess ferrous alphaCO. This slow phase appears to be due to cis to trans prolyl isomerization of the Asp(29)-Pro(3) peptide bond in wild-type AHSP because it was absent when alphaCO was mixed with P3A and P3W AHSP, which are fixed in the trans conformation. This slow phase was also absent when met(Fe(3+))-alpha reacted with wild-type AHSP, suggesting that met-alpha is capable of rapidly binding to either Pro(3) conformer. Both wild-type and Pro(3)-substituted AHSPs drive the formation of a met-alpha hemichrome conformation following binding to either met- or oxy(Fe(2+))-alpha. The dissociation rate of the met-alpha-·AHSP complex (k(AHSP) ≈ .2 s(-1)) is ~1-fold slower than that for ferrous alpha-·AHSP complexes, resulting in a much higher affinity of AHSP for met-alpha. Thus, in vivo, AHSP acts as a molecular chaperone by rapidly binding and stabilizing met-alpha hemichrome folding intermediates. The low rate of met-alpha dissociation also allows AHSP to have a quality control function by kinetically trapping ferric alpha and preventing its incorporation into less stable mixed valence Hemoglobin A tetramers. Reduction of AHSP-bound met-alpha allows more rapid release to beta subunits to form stable fully, reduced hemoglobin dimers and tetramers.
Description A DNA sequence encoding human ERAF (Q9NZD4) (Met1-Ser102) was expressed.
Source E.coli
Predicted N Terminal Met
AA Sequence Met1-Ser102
Molecular Weight The recombinant human ERAF consists of 102 a.a. and predicts a molecular mass of 11.8 KDa. It migrates as an approximately 12 KDa band in SDS-PAGE under reducing conditions.
Purity >90% as determined by SDS-PAGE
Endotoxin Please contact us for more information.
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile PBS, pH 7.4..
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function Acts as a chaperone to prevent the harmful aggregation of alpha-hemoglobin during normal erythroid cell development. Specifically protects free alpha-hemoglobin from precipitation. It is predicted to modulate pathological states of alpha-hemoglobin excess such as beta-thalassemia.
Subcellular Location Cytoplasm.
Protein Families AHSP family
Database References
Tissue Specificity Expressed in blood and bone marrow.

Gene Functions References

  1. In the presence of free alpha subunits and H2O2, both HbA and HbE showed bCys93 oxidation which increased with higher H2O2 concentrations. In the presence of Alpha-hemoglobin stabilizing protein (AHSP)Cys93 oxidation was substantially reduced in both the presence of excess free alpha-subunit and under the same oxidative conditions, these events are substantially increased for HbE compared to HbA PMID: 26995402
  2. Findings indicate that alpha-hemoglobin-stabilizing protein (AHSP) expression is a biomarker of hemoglobin H (HbH) disease severity and infer an important role of AHSP in modulating the pathophysiology of this disease. PMID: 28337528
  3. AHSP is predominantly expressed in erythroid precursors in bone marrow biopsy specimens from patients with hematologic malignancies. PMID: 25611244
  4. AHSP expression was higher in patients with sickle cell anemia versus thalassemia, with no significant difference between BTM and BTI. Expression was higher in patients with NTDT and on hydroxyurea therapy. PMID: 26460260
  5. In maturing RBC progenitors AHSP bind to free alpha-globin chains to increase the HbA production. (Review) PMID: 25648458
  6. analysis showed binding of STAT3 to AHSP promoter and binding was significantly augmented with IL6 stimulation and upon alpha-globin overexpression PMID: 24740453
  7. The relationship between AHSP gene expression, disease severity, and the beta/alpha globin mRNA ratio was studied among different homozygote beta-thalassemia patients. PMID: 24795058
  8. alpha-Hemoglobin-stabilizing protein (AHSP) perturbs the proximal heme pocket of oxy-alpha-hemoglobin and weakens the iron-oxygen bond. PMID: 23696640
  9. alpha-Hemoglobin stabilizing protein (AHSP) markedly decreases the redox potential and reactivity of alpha-subunits of human HbA with hydrogen peroxide. PMID: 23264625
  10. AHSP acts as a molecular chaperone by rapidly binding and stabilizing met-alpha hemichrome folding intermediates PMID: 22298770
  11. AHSP could be a secondary compensatory mechanism in red blood cells to counterbalance the excess of alpha-globin chains in HbE/beta-thalassaemia individuals. PMID: 22079025
  12. NF-E2 may play an important role in AHSP gene regulation, providing new insights into the molecular mechanisms underlying the erythroid-specific expression of AHSP as well as new possibilities for beta-thalassemia treatment PMID: 21232177
  13. No significant association has been found between specific AHSP alleles or haplotypes and the disease severity of beta-thalassemia. Our study suggested that AHSP is not a significant genetic modifier of beta-thalassemia in southern China. PMID: 20627634
  14. Overexpression of human AHSP & 2 mutant versions with AA substitutions confering 3- or 13-fold higher affinity for alpha-globin had no major effects on hematologic parameters in beta-thalassemic mice. PMID: 20815047
  15. analysis of the action of a human mutant, AHSPV56G, of alpha-hemoglobin stabilizing protein (AHSP) PMID: 20371604
  16. Studies indicate that the interaction of alpha-Hb with AHSP involves surfaces normally employed in binding to beta-Hb. PMID: 20036801
  17. Different mechanisms may be responsible for the amount of abnormal Hb recovered, such as a highly unstable alpha chain or an impaired formation of the complex AHSP/alpha-Hb or a modification of the alphabeta dimer formation. PMID: 19482015
  18. An abundant erythroid protein that stabilizes free alpha-haemoglobin. PMID: 12066189
  19. determination as a predominantly alpha-helical globular protein with a somewhat asymmetric shape PMID: 12192002
  20. progesterone, corticotropin-releasing factor, and activin A have roles in paracrine regulation of endometrial function [review] PMID: 14667971
  21. Using gene mapping, direct genomic sequencing, and extended haplotype analysis, no mutation or specific association between haplotypes of AHSP and disease severity was found, suggesting that AHSP is not a disease modifier in Hb E-beta thalassemia PMID: 14715623
  22. AHSP is a chaperone for transfer of human alpha- to beta-hemoglobin PMID: 15220346
  23. identified an AHSP gene erythroid promoter with functionally important binding sites for GATA-1- and Oct-1-related proteins PMID: 16186125
  24. Review. AHSP specifically binds free alphaHb, stabilizes its structure, & limits its ability to generate reactive oxygen species. It binds the G & H helices of alphaHb on a surface that largely overlaps with the alpha1-beta1 interface of HbA. PMID: 16339656
  25. results reveal a plasticity of the alpha-Hb active site in the presence of the chaperone AHSP and indicate that the AHSP was still active at 300 MPa PMID: 17194704
  26. The 12391 G>A SNP is common and represents a potential mechanism through which genetically determined variations in AHSP expression could influence beta-thalassemia. PMID: 17874450
  27. the alpha2-globin mutation cod 117 TTC>TCC or alpha 117(GH5)Phe>Ser impairs the interaction of the alpha-chain variant with the AHSP and prevents its stabilizing effect, thus leading to the alpha-chain pool reduction PMID: 18166800
  28. The AHSP stabilizes the alphaHb chain, avoiding its precipitation and its ability to generate ROS, which implicate in cell death.Data indicate that AHSP may be significant for human hemoglobin formation and it is a key protein during human erythropoiesis. PMID: 18179859
  29. Placental AHSP mRNA level in HELLP & intrauterine fetal death were significantly decreased compared with controls. It may be involved in the pathogenic mechanisms leading to the adverse pregnancy outcome. PMID: 18347943
  30. An iron responsive element-like stem-loop regulates alpha-hemoglobin-stabilizing protein mRNA. PMID: 18676996
  31. Reduced AHSP may identify women at risk of experiencing further miscarriages. PMID: 18704762
  32. AHSP promotes alpha globin chain stability during human erythropoiesis PMID: 19349619
  33. A cis-proline in alpha-hemoglobin stabilizing protein directs the structural reorganization of alpha-hemoglobin. PMID: 19706593


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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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