Hemoglobin γ (D4K7X) Rabbit mAb (PE Conjugate) #81136

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Supporting Data

REACTIVITY	H
SENSITIVITY	Endogenous
MW (kDa)
Source/Isotype	Rabbit IgG

Application Key:

F-Flow Cytometry

Species Cross-Reactivity Key:

H-Human

Product Information

Product Description

This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometric analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Hemoglobin γ (D4K7X) Rabbit mAb #39386.

Product Usage Information

Application	Dilution
Flow Cytometry (Fixed/Permeabilized)	1:50

Storage

Supplied in PBS (pH 7.2), less than 0.1% sodium azide and 2 mg/ml BSA. Store at 4°C. Do not aliquot the antibody. Protect from light. Do not freeze.

Protocol

Specificity / Sensitivity

Hemoglobin γ (D4K7X) Rabbit mAb (PE Conjugate) recognizes endogenous levels of the hemoglobin γ subunit. This antibody recognizes both HBG1 and HBG2 isoforms, but does not cross-react with the hemoglobin β subunit.

Species Reactivity:

Human

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Val21 of human hemoglobin γ (HBG1) protein.

Background

Hemoglobin (Hb, Hbg) is a heme-containing transport protein found primarily in the red blood cells of humans and most other vertebrates. The primary function of hemoglobin is to transport oxygen from the external environment to body tissues. Hemoglobin also facilitates metabolic waste removal by assisting in the transport of carbon dioxide from tissues back to the respiratory organs (1). Mature hemoglobin is a tetrameric protein complex, with each subunit containing an oxygen-binding heme group (2). Multiple isoforms of hemoglobin exist, which vary in relative abundance depending on developmental stage. Adult hemoglobin (HbA) is composed of two α subunits and two β subunits and is the predominant hemoglobin found in red blood cells of children and adults. Fetal hemoglobin (HbF) contains two α subunits and two γ subunits and is the predominant isoform found during fetal and early postnatal development (2,3). Mutations that alter the structure or abundance of specific globin subunits can result in pathological conditions known as hemoglobinopathies (4). One such disorder is sickle cell disease, which is characterized by structural abnormalities that limit the oxygen carrying capacity of red blood cells. By contrast, thalassemia disorders are characterized by deficiencies in the abundance of specific hemoglobin subunits (4). Clinical treatments that are designed to alter the expression of specific hemoglobin subunits can be used to treat hemoglobinopathies (5).

Database Links

UniProt ID: P69891

Entrez-Gene Id: 3047

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