Anti-AHSP Antibody, Rabbit Polyclonal sinobiological 14391-T16
$243.00
In stock
SKU
14391-T16
| Catalog No. | Size | Price (USD) |
| 14391-T16-100 | 100 µL | $251.64 |
General Information
| Product name | Anti-AHSP Antibody, Rabbit Polyclonal |
| Validated applications | ELISA (FAQ Protocol) |
| Species reactivity | Reacts with: Human |
| Specificity | Human AHSP |
| Immunogen | Recombinant Human AHSP Protein (Catalog#14391-HNAE) |
| Preparation | Produced in rabbits immunized with purified, recombinant Human AHSP (rh AHSP; Catalog#14391-HNAE; Q9NZD4; Met1-Ser102). AHSP specific IgG was purified by Human AHSP affinity chromatography. |
| Source | Polyclonal Rabbit IgG |
| Purification | Protein A & Antigen Affinity |
| Formulation | 0.2 μm filtered solution in PBS |
| Conjugate | Unconjugated |
| Form | Liquid |
| Shipping | This antibody is shipped as liquid solution at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Storage | This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -80℃. Preservative-Free. Avoid repeated freeze-thaw cycles. |
Synonyms: Anti-EDRF Antibody; Anti-ERAF Antibody
Background Information
| Full Name | alpha hemoglobin stabilizing protein |
| Description | 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 α-globin. It rapidly binds to ferrous α 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 ℃. A small slow phase was observed when AHSP binds to excess ferrous αCO. 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 αCO was mixed with P3A and P3W AHSP, which are fixed in the trans conformation. This slow phase was also absent when met(Fe(3+))-α reacted with wild-type AHSP, suggesting that met-α is capable of rapidly binding to either Pro(3) conformer. Both wild-type and Pro(3)-substituted AHSPs drive the formation of a met-α hemichrome conformation following binding to either met- or oxy(Fe(2+))-α. The dissociation rate of the met-α·AHSP complex (k(AHSP) ≈ .2 s(-1)) is ～1-fold slower than that for ferrous α·AHSP complexes, resulting in a much higher affinity of AHSP for met-α. Thus, in vivo, AHSP acts as a molecular chaperone by rapidly binding and stabilizing met-α hemichrome folding intermediates. The low rate of met-α dissociation also allows AHSP to have a quality control function by kinetically trapping ferric α and preventing its incorporation into less stable mixed valence Hemoglobin A tetramers. Reduction of AHSP-bound met-α allows more rapid release to β subunits to form stable fully, reduced hemoglobin dimers and tetramers. |
| References |
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