All Photos(3)



Hemoglobin human

lyophilized powder

CAS Number:
MDL number:

Quality Level

biological source



lyophilized powder


enzyme immunoassay: suitable


HIV and hepatitis B antigen, tested negative


H2O: soluble 20 mg/mL

storage temp.


General description

Hemoglobin is the major component of red blood cells, and is responsible for their red color. Its normal concentration in erythrocytes is 34%. Hemoglobin is the most important respiratory protein of vertebrates by virtue of its ability to transport oxygen from the lungs to body tissues, and to facilitate the return transport of carbon dioxide.


Hemoglobin was used in the development of a rapid enzyme immunoassay for the detection of retinol-binding protein. It was also used in the inhibition of human platelet reactivity by endothelium-derived relaxing factor.


1, 5, 10 g in poly bottle

Biochem/physiol Actions

The Fe2+/Fe3+ balance is a physiological indicator of blood oxygenation. Deoxygenated hemoglobin accessorizes a feedback loop by reducing nitrite to NO, a vasodilator which enhances blood flow to oxygen-deprived tissues.
Oxygen transporter, NO scavenger


Since native hemoglobin is readily oxidized in air, these preparations may be predominantly methemoglobin.

Storage Class Code

11 - Combustible Solids



Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis

Enter Lot Number to search for Certificate of Analysis (COA).

Certificate of Origin

Enter Lot Number to search for Certificate of Origin (COO).

Product Information Sheet

Quotes and Ordering

  1. Which document(s) contains shelf-life or expiration date information for a given product?

    If available for a given product, the recommended re-test date or the expiration date can be found on the Certificate of Analysis.

  2. How do I get lot-specific information or a Certificate of Analysis?

    The lot specific COA document can be found by entering the lot number above under the "Documents" section.

  3. Is Product H7379, Hemoglobin human, methemoglobin?

    Yes. The iron in hemoglobin will oxidize by exposure to air unless special handling and packaging is used.  Because this product is exposed to air during purification and packaging, it will be predominantly methemoglobin.

  4. How can Product H7379, Hemoglobin human, be reduced?

    A procedure for reduction of methemoglobin may be found in the product sheet.

  5. How many donors are used to make a batch of Product H7379, Hemoglobin human?

    This will vary with the batch size, but may come from as many as several hundred donors. All donors are tested and found negative for antibodies to HIV-1/HIV-2, HCV, for HBSAG, and for syphilis.

  6. How do I find price and availability?

    There are several ways to find pricing and availability for our products. Once you log onto our website, you will find the price and availability displayed on the product detail page. You can contact any of our Customer Sales and Service offices to receive a quote.  USA customers:  1-800-325-3010 or view local office numbers.

  7. What is the Department of Transportation shipping information for this product?

    Transportation information can be found in Section 14 of the product's (M)SDS.To access the shipping information for this material, use the link on the product detail page for the product. 

  8. My question is not addressed here, how can I contact Technical Service for assistance?

    Ask a Scientist here.

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Leila Pishkar et al.
Journal of biomolecular structure & dynamics, 35(3), 603-615 (2016-05-07)
In this study, a novel method to probe molecular interactions and binding of human hemoglobin (Hb) with nanodiamond (ND) was introduced based on the surface tension measurement. This method complements conventional techniques, which are basically done by zeta potential and
Hsuan-Shun Huang et al.
The Journal of pathology, 240(4), 484-494 (2016-10-30)
Fallopian tube fimbrial epithelium is considered to be the major site of origin of ovarian high-grade serous carcinoma, with p53 loss being the earliest and universal change. We previously reported that reactive oxygen species (ROS) in the ovulatory follicular fluids
Chiao-Wang Sun et al.
Circulation, 139(23), 2654-2663 (2019-03-25)
Nitrosation of a conserved cysteine residue at position 93 in the hemoglobin β chain (β93C) to form S-nitroso (SNO) hemoglobin (Hb) is claimed to be essential for export of nitric oxide (NO) bioactivity by the red blood cell (RBC) to


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