AHSP
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Official Full Name
alpha hemoglobin stabilizing protein
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Overview
Act 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. -
Synonyms
AHSP; alpha hemoglobin stabilizing protein; EDRF; ERAF; alpha-hemoglobin-stabilizing protein; erythroid associated factor; erythroid-associated factor; alpha hemoglobin stabilising protein; erythroid differentiation-related factor; erythroid differentiation associated factor;
- Recombinant Proteins
- Cell & Tissue Lysates
- Human
- Mouse
- Rat
- E.coli
- HEK293
- HEK293T
- GST
- His
- His|GST
- His|S
- Myc
- DDK
- N/A
Species | Cat.# | Product name | Source (Host) | Tag | Protein Length | Price |
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Human | AHSP-614H | Recombinant Human AHSP Protein, His-tagged | E.coli | His | Met1~Ser102 | |
Human | AHSP-1392H | Recombinant Human Alpha Hemoglobin Stabilizing Protein | E.coli | N/A | ||
Human | AHSP-26663TH | Recombinant Human AHSP | E.coli | N/A | ||
Human | aHSP-3367H | Recombinant Human aHSP, His-tagged, S tagged | E.coli | His/S | 102 | |
Human | AHSP-8959HCL | Recombinant Human AHSP 293 Cell Lysate | HEK293 | N/A | ||
Human | AHSP-0103H | Recombinant Human AHSP Protein (Met1-Ser102), His-tagged | E.coli | His | Met1-Ser102 | |
Human | AHSP-5962H | Recombinant Human AHSP Protein, Myc/DDK-tagged, C13 and N15-labeled | HEK293T | Myc/DDK | ||
Human | AHSP-4866H | Recombinant Human AHSP protein, GST-tagged | E.coli | GST | 1-102aa | |
Mouse | Ahsp-615M | Recombinant Mouse Ahsp Protein, His-tagged | E.coli | His | Ala2~Ser102 | |
Rat | Ahsp-616R | Recombinant Rat Ahsp Protein, His/GST-tagged | E.coli | His/GST | Ala2~Ser102 |
- Involved Pathway
- Protein Function
- Interacting Protein
- AHSP Related Articles
AHSP involved in several pathways and played different roles in them. We selected most pathways AHSP participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with AHSP were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
Pathway Name | Pathway Related Protein |
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AHSP has several biochemical functions, for example, hemoglobin binding, protein binding, unfolded protein binding. Some of the functions are cooperated with other proteins, some of the functions could acted by AHSP itself. We selected most functions AHSP had, and list some proteins which have the same functions with AHSP. You can find most of the proteins on our site.
Function | Related Protein |
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hemoglobin binding | AHSP;CUBN;HBB;HP;HPR;LRP2 |
protein binding | KIF13B;NUP85;WSB1;NRP1;CLTA;AIRE;MET;MC5R;SH3YL1 |
unfolded protein binding | CALR3;CLPXA;DNAJA2;HSPA1A;HSP104;HSP90B1;APCS;HSP90AA1;DNAJB5 |
AHSP has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with AHSP here. Most of them are supplied by our site. Hope this information will be useful for your research of AHSP.
ZC3H12A; FKBP1A; UBE3A; HBA1; GRINL1A; TMEM165
- Q&As
- Reviews
Q&As (10)
Ask a questionechniques such as isothermal titration calorimetry (ITC) and surface plasmon resonance (SPR) are commonly employed to quantify the binding affinity and kinetics of Ahsp-alpha-globin interactions.
Ahsp deficiency can lead to unstable alpha-globin chains, contributing to the development of certain hemoglobinopathies like alpha-thalassemia.
Ahsp expression may be upregulated during cellular stress to enhance its protective role in stabilizing alpha-globin chains and preventing protein aggregation.
Techniques such as nuclear magnetic resonance (NMR), X-ray crystallography, and molecular dynamics simulations are commonly used to study protein-protein interactions involving Ahsp and alpha-globin.
Ahsp can interact with molecular chaperones like Hsp70 to assist in protein folding and prevent misfolding of alpha-globin chains.
Ahsp binds to free alpha-globin chains, preventing their aggregation and degradation by maintaining their folded state.
Ahsp plays a role in preventing excess alpha-globin chains from aggregating and precipitating, which is a key factor in the pathogenesis of alpha-thalassemia.
Ahsp's role is unique, focusing specifically on stabilizing alpha-globin chains, whereas other chaperones have broader functions in assisting protein folding and transport.
Ahsp indirectly influences iron metabolism by stabilizing alpha-globin chains and preventing their degradation, which in turn maintains balanced globin chain production and minimizes iron waste.
Ahsp's role in stabilizing alpha-globin chains helps prevent the formation of toxic aggregates that could damage red blood cells and shorten their lifespan.
Customer Reviews (5)
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Exceptional quality product that doesn't break the bank. Fast delivery too!
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