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AB19362

HRP Anti-Hemoglobin antibody

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(5 Publications)

Goat Polyclonal Hemoglobin subunit alpha antibody - conjugated to HRP. Suitable for WB and reacts with Human samples. Cited in 5 publications. Immunogen corresponding to Full Length Protein corresponding to Human HBA1 conjugated to Bovine Serum Albumin.

View Alternative Names

HBA2, HBA1, Hemoglobin subunit alpha, Alpha-globin, Hemoglobin alpha chain

1 Images
Western blot - HRP Anti-Hemoglobin antibody (AB19362)
  • WB

Unknown

Western blot - HRP Anti-Hemoglobin antibody (AB19362)

All lanes:

Western blot - HRP Anti-Hemoglobin antibody (ab19362) at 1/1000 dilution

All lanes:

Western blot - Native Human Hemoglobin protein (ab77858) at 0.01 µg

Predicted band size: 15 kDa

true

Exposure time: 10s

Key facts

Host species

Goat

Clonality

Polyclonal

Isotype

IgG

Conjugation

HRP

Excitation/Emission
Carrier free

No

Reacts with

Human

Applications

WB

applications

Immunogen

Full Length Protein corresponding to Human HBA1 conjugated to Bovine Serum Albumin. The exact immunogen used to generate this antibody is proprietary information.

P69905

Specificity

The antibody has been tested in ELISA and IEP with a Human Hemaglobin Calibrator/Standard but has yet to be tested against endogenous protein.

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Reactivity data

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Product details

Molar enzyme/antibody protein ratio is 4:1.
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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Purification notes
Antibody concentration was determined by extinction coefficient prior to conjugation: absorbance at 280 nm of 1.4 equals 1.0 mg of IgG.
Storage buffer
pH: 6.8 - 7.4 Preservative: 0.01% Thimerosal (merthiolate) Constituents: 1.19% HEPES, 0.58% Sodium chloride
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
+4°C
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Hemoglobin also known as Hb or HBB is a protein found in red blood cells. It is a tetramer with a molecular mass of approximately 64.5 kDa composed of two alpha and two beta subunits. This protein is predominantly expressed in erythrocytes where it plays an important role in oxygen transport from the lungs to tissues and facilitates the return of carbon dioxide from tissues to the lungs for exhalation.
Biological function summary

Hemoglobin carries oxygen in blood and acts as a buffer in maintaining blood pH. Within the erythrocytes hemoglobin comprises one of the principal components of these cells each molecule binding up to four oxygen molecules. Hemoglobin exists as a complex with heme groups that directly interact with oxygen allowing hemoglobin to perform its respiratory function efficiently.

Pathways

Hemoglobin is important in the circulatory and respiratory pathways. It works in conjunction with proteins like myoglobin which assists with oxygen storage in muscles and cytochrome c which is important in the electron transport chain. Hemoglobin's function aligns with these pathways to maintain proper oxygen and energy levels throughout the body.

Hemoglobin abnormalities lead to conditions such as sickle cell anemia and thalassemia. Sickle cell anemia involves a mutation in the beta-globin gene resulting in deformed red blood cells that hinder oxygen delivery and cause pain due to blockages in blood vessels. Thalassemia results from reduced production of globin chains leading to anemia. These conditions involve aberrations in the hemoglobin or related proteins impacting overall health and requiring clinical management.
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Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:
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Target data

Involved in oxygen transport from the lung to the various peripheral tissues.. Hemopressin. Hemopressin acts as an antagonist peptide of the cannabinoid receptor CNR1 (PubMed : 18077343). Hemopressin-binding efficiently blocks cannabinoid receptor CNR1 and subsequent signaling (PubMed : 18077343).
See full target information HBA1
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Publications (5)

Recent publications for all applications. Explore the full list and refine your search

Scientific reports 14:8272 PubMed38594253

2024

Identification of small molecules affecting the interaction between human hemoglobin and Staphylococcus aureus IsdB hemophore.

Applications

Unspecified application

Species

Unspecified reactive species

Monica Cozzi,Mariacristina Failla,Eleonora Gianquinto,Sandra Kovachka,Valeria Buoli Comani,Carlotta Compari,Omar De Bei,Roberta Giaccari,Francesco Marchesani,Marialaura Marchetti,Luca Ronda,Barbara Rolando,Massimo Baroni,Gabriele Cruciani,Barbara Campanini,Stefano Bettati,Serena Faggiano,Loretta Lazzarato,Francesca Spyrakis

Laboratory investigation; a journal of technical m 100:986-1002 PubMed32054994

2020

Hemoglobin oxidation generates globin-derived peptides in atherosclerotic lesions and intraventricular hemorrhage of the brain, provoking endothelial dysfunction.

Applications

Unspecified application

Species

Unspecified reactive species

Niké Posta,Éva Csősz,Melinda Oros,Dávid Pethő,László Potor,Gergő Kalló,Zoltán Hendrik,Katalin Éva Sikura,Gábor Méhes,Csaba Tóth,József Posta,György Balla,József Balla

Frontiers in physiology 9:1595 PubMed30515102

2018

Heme Induces Endoplasmic Reticulum Stress (HIER Stress) in Human Aortic Smooth Muscle Cells.

Applications

Unspecified application

Species

Unspecified reactive species

Tamás Gáll,Dávid Pethő,Annamária Nagy,Zoltán Hendrik,Gábor Méhes,László Potor,Magnus Gram,Bo Åkerström,Ann Smith,Péter Nagy,György Balla,József Balla

Biochimica et biophysica acta. Molecular basis of disease 1865:464-475 PubMed30389578

2018

Oxidized hemoglobin forms contribute to NLRP3 inflammasome-driven IL-1β production upon intravascular hemolysis.

Applications

Unspecified application

Species

Unspecified reactive species

Benard Bogonko Nyakundi,Andrea Tóth,Enikő Balogh,Béla Nagy,Judit Erdei,Bernhard Ryffel,György Paragh,Mario D Cordero,Viktória Jeney

Oxidative medicine and cellular longevity 2018:3812568 PubMed29560080

2018

Hydrogen Sulfide Abrogates Hemoglobin-Lipid Interaction in Atherosclerotic Lesion.

Applications

Unspecified application

Species

Unspecified reactive species

László Potor,Péter Nagy,Gábor Méhes,Zoltán Hendrik,Viktória Jeney,Dávid Pethő,Anita Vasas,Zoltán Pálinkás,Enikő Balogh,Ágnes Gyetvai,Matthew Whiteman,Roberta Torregrossa,Mark E Wood,Sándor Olvasztó,Péter Nagy,György Balla,József Balla
View all publications
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