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H4131

Sigma-Aldrich

Hemoglobin porcine

lyophilized powder

Synonym(s):

Hb

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1 G
¥1,464.20

About This Item

CAS Number:
MDL number:
UNSPSC Code:
12352202
eCl@ss:
42030116
NACRES:
NA.61

¥1,464.20


In StockDetails


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biological source

Porcine

Quality Level

form

lyophilized powder

solubility

H2O: soluble 10 mg/mL

UniProt accession no.

storage temp.

2-8°C

Gene Information

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This Item
I339051471CI2911
form

liquid

form

liquid

form

liquid

form

liquid

sterility

sterile-filtered

sterility

sterile-filtered

sterility

sterile

sterility

sterile-filtered

technique(s)

cell culture | hybridoma: suitable, cell culture | mammalian: suitable

technique(s)

cell culture | hybridoma: suitable, cell culture | mammalian: suitable

technique(s)

cell culture | hybridoma: suitable, cell culture | mammalian: suitable, cell culture | stem cell: suitable

technique(s)

cell culture | hybridoma: suitable, cell culture | mammalian: suitable

components

glucose: yes
phenol red: yes
NaHCO3: yes
L-glutamine: yes

components

phenol red: yes
L-glutamine: no
glucose: yes

components

phenol red: 15.93 mg/L
NaHCO3: 3024 mg/L
L-glutamine: 582 mg/L
HEPES: 5958 mg/L
sodium pyruvate: 110 mg/L

components

NaHCO3: yes
glucose: yes
stable glutamine: yes
phenol red: yes

shipped in

ambient

shipped in

ambient

shipped in

ambient

shipped in

ambient

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

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.

Application

Hemoglobin from porcine was used to test the role of the L-arginine/nitric oxide pathway in relaxation of isolated human penile cavernous tissue and circumflex veins.[1] It was also used to study the role of nitric oxide in neurogenic vasodilation of porcine cerebral artery.[2]

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.

Caution

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

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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M J E Walenkamp et al.
Endocrine development, 24, 128-137 (2013-02-09)
Molecular defects of the insulin-like growth factor 1 gene (IGF1) are rare in the human. Only three homozygous and two families with heterozygous mutations of the IGF1 gene have been described, resulting in a variable degree of intrauterine and postnatal
Juan E Puche et al.
Journal of translational medicine, 10, 224-224 (2012-11-15)
Insulin-like growth factor I (IGF-I) is a polypeptide hormone produced mainly by the liver in response to the endocrine GH stimulus, but it is also secreted by multiple tissues for autocrine/paracrine purposes. IGF-I is partly responsible for systemic GH activities
Shu-Lin Liu et al.
Molecular cell, 71(6), 1092-1104 (2018-09-04)
Activation of class I phosphatidylinositol 3-kinase (PI3K) leads to formation of phosphatidylinositol-3,4,5-trisphophate (PIP3) and phosphatidylinositol-3,4-bisphophate (PI34P2), which spatiotemporally coordinate and regulate a myriad of cellular processes. By simultaneous quantitative imaging of PIP3 and PI34P2 in live cells, we here show
A comparison of the effects of equine luteinizing hormone (eLH), equine growth hormone (eGH) and human recombinant insulin-like growth factor (hrIGF-I) on steroid production in cultured equine Leydig cells during sexual maturation
Hess MF and Roser JF
Animal Reproduction Science, 89(1-4), 7-19 (2005)
An optimized system for studies of EPO-dependent murine pro-erythroblast development
Zhang D, et al.
Experimental Hematology, 29(11), 1278-1288 (2001)

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