Human Alpha-Hemoglobin Stabilizing Protein (aHSP) Protein

Este producto es parte de AHSP - Alpha Hemoglobin Stabilizing Protein
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221€ (10 µg)

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935106861
info@markelab.com
name
Human Alpha-Hemoglobin Stabilizing Protein (aHSP) Protein
category
Proteins and Peptides
provider
Abbexa
reference
abx065284
tested applications
WB, SDS-PAGE

Description

Recombinant Alpha-Hemoglobin Stabilizing Protein (aHSP) is a recombinant Human protein produced in a Prokaryotic expression system (E. coli).

Documents del producto

Instrucciones
Data sheet
Descargar

Product specifications

Category
Proteins and Peptides
Immunogen Target
Alpha-Hemoglobin Stabilizing Protein (aHSP)
Host
E. coli
Origin
Human
Conjugation
Unconjugated
Observed MW
Molecular Weight: Calculated MW: 17.6 kDa
Concentration: Prior to lyophilization: 200 µg/ml
Sequence Fragment: Met1-Ser102
Tag: N-terminal His tag
Expression
Recombinant
Purity
> 95%
Size 1
10 µg
Size 2
50 µg
Size 3
100 µg
Size 4
200 µg
Size 5
500 µg
Form
Lyophilized To keep the original salt concentration, we recommend reconstituting to the original concentration prior to lyophilization (see Concentration) in ddH2O. If a lower concentration is required, dilute in PBS, pH 7.4. If a higher concentration is required, the product can be reconstituted directly in PBS, pH 7.4, though please note that this will change the overall salt concentration. The stock concentration should be between 0.1-1.0 mg/ml. Do not vortex.
Tested Applications
WB, SDS-PAGE
Buffer
Prior to lyophilization: PBS, pH 7.4, containing 0.01% Sarcosyl, 1 mM DTT, 5% Trehalose and Proclin-300.
Availability
Shipped within 5-12 working days.
Storage
Store at 2-8 °C for up to one month. Store at -80 °C for up to one year. Avoid repeated freeze/thaw cycles.
Dry Ice
No
UniProt ID
Q9NZD4
Alias
EDRF,ERAF
Background
Protein AHSP
Status
RUO
Note
This product is for research use only.   Not for human consumption, cosmetic, therapeutic or diagnostic use.

Descripción

Alpha Hemoglobin Stabilizing Protein (AHSP) is a molecular chaperone that specifically binds to free alpha-globin subunits during erythropoiesis, stabilizing them and preventing their aggregation or precipitation. This function is critical for maintaining the proper stoichiometry of alpha- and beta-globin chains required for the assembly of functional hemoglobin tetramers. AHSP also protects alpha-globin from oxidative damage by maintaining it in a reduced state. Dysregulation or deficiency of AHSP is associated with hematological disorders such as beta-thalassemia, where excess alpha-globin chains lead to oxidative stress and ineffective erythropoiesis. AHSP is highly expressed in erythroid precursor cells, and its expression is tightly regulated during red blood cell development. Therapeutic approaches that modulate AHSP levels or function are being explored as potential treatments for thalassemias and related hemoglobinopathies.

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