Recombinant Human AHSP Protein

Name: Recombinant Human AHSP Protein
Brand: Beta LifeScience
SKU: BLPSN-0111
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

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	HGNC: 18075 OMIM: 605821 KEGG: hsa:51327 STRING: 9606.ENSP00000307199 UniGene: Hs.274309
Tissue Specificity	Expressed in blood and bone marrow.

Gene Functions References

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 proteins.in 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
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
AHSP is predominantly expressed in erythroid precursors in bone marrow biopsy specimens from patients with hematologic malignancies. PMID: 25611244
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
In maturing RBC progenitors AHSP bind to free alpha-globin chains to increase the HbA production. (Review) PMID: 25648458
analysis showed binding of STAT3 to AHSP promoter and binding was significantly augmented with IL6 stimulation and upon alpha-globin overexpression PMID: 24740453
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
alpha-Hemoglobin-stabilizing protein (AHSP) perturbs the proximal heme pocket of oxy-alpha-hemoglobin and weakens the iron-oxygen bond. PMID: 23696640
alpha-Hemoglobin stabilizing protein (AHSP) markedly decreases the redox potential and reactivity of alpha-subunits of human HbA with hydrogen peroxide. PMID: 23264625
AHSP acts as a molecular chaperone by rapidly binding and stabilizing met-alpha hemichrome folding intermediates PMID: 22298770
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
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
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
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
analysis of the action of a human mutant, AHSPV56G, of alpha-hemoglobin stabilizing protein (AHSP) PMID: 20371604
Studies indicate that the interaction of alpha-Hb with AHSP involves surfaces normally employed in binding to beta-Hb. PMID: 20036801
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
An abundant erythroid protein that stabilizes free alpha-haemoglobin. PMID: 12066189
determination as a predominantly alpha-helical globular protein with a somewhat asymmetric shape PMID: 12192002
progesterone, corticotropin-releasing factor, and activin A have roles in paracrine regulation of endometrial function [review] PMID: 14667971
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
AHSP is a chaperone for transfer of human alpha- to beta-hemoglobin PMID: 15220346
identified an AHSP gene erythroid promoter with functionally important binding sites for GATA-1- and Oct-1-related proteins PMID: 16186125
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
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
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
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
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
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
An iron responsive element-like stem-loop regulates alpha-hemoglobin-stabilizing protein mRNA. PMID: 18676996
Reduced AHSP may identify women at risk of experiencing further miscarriages. PMID: 18704762
AHSP promotes alpha globin chain stability during human erythropoiesis PMID: 19349619
A cis-proline in alpha-hemoglobin stabilizing protein directs the structural reorganization of alpha-hemoglobin. PMID: 19706593

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.