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Merck

H7379

Hemoglobin human

lyophilized powder

Sinónimos:

Hb

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Número CAS:
9008-02-0
UNSPSC Code:
12352202
eCl@ss:
42030116
NACRES:
NA.61
MDL number:
MFCD00131282

Documentos clave

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Nombre del producto

Hemoglobin human, lyophilized powder

biological source

human

form

lyophilized powder

technique(s)

enzyme immunoassay: suitable

impurities

HIV and hepatitis B antigen, tested negative

solubility

H2O: soluble 20 mg/mL

UniProt accession no.

P02008
P02042
P02100
P09105
P68871
P69891
P69892
P69905

storage temp.

2-8°C

Quality Level

200

Gene Information

human ... HBA1(3039), HBA2(3040), HBB(3043), HBD(3045), HBE1(3046), HBG1(3047), HBG2(3048), HBQ1(3049), HBZ(3050)

Application

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.

Biochem/physiol Actions

Oxygen transporter, NO scavenger
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.

Disclaimer

RESEARCH USE ONLY. This product is regulated in France when intended to be used for scientific purposes, including for import and export activities (Article L 1211-1 paragraph 2 of the Public Health Code). The purchaser (i.e. enduser) is required to obtain an import authorization from the France Ministry of Research referred in the Article L1245-5-1 II. of Public Health Code. By ordering this product, you are confirming that you have obtained the proper import authorization.
Since native hemoglobin is readily oxidized in air, these preparations may be predominantly methemoglobin.

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.

Clase de almacenamiento

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

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Certificados de análisis (COA)

Lot/Batch Number
SLCK4141
SLCJ0443
SLCC1154
SLBX7566
SLBR9638V

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  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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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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