Recombinant Human Alpha-Hemoglobin-Stabilizing Protein (AHSP) Protein (GST)

Name: Recombinant Human Alpha-Hemoglobin-Stabilizing Protein (AHSP) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-08688P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Alpha-Hemoglobin-Stabilizing Protein (AHSP) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9NZD4
Target Symbol	AHSP
Synonyms	AHSP; AHSP_HUMAN; Alpha hemoglobin stabilizing protein; Alpha-hemoglobin-stabilizing protein; EDRF; ERAF; Erythroid associated factor; Erythroid differentiation associated factor; Erythroid differentiation related factor; Erythroid differentiation-related factor; Erythroid-associated factor
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MALLKANKDLISAGLKEFSVLLNQQVFNDPLVSEEDMVTVVEDWMNFYINYYRQQVTGEPQERDKALQELRQELNTLANPFLAKYRDFLKSHELPSHPPPSS
Expression Range	1-102aa
Protein Length	Full Length
Mol. Weight	38.8kDa
Research Area	Signal Transduction
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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: 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

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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.