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C6653

Supelco

Carbonic Anhydrase I from human erythrocytes

Isoelectric focusing marker, pI 6.6

Synonym(s):

Carbonate Dehydratase, Carbonate Hydrolyase, Carbonic Anhydrase Isozyme I

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About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.25

Quality Level

form

powder

pI 

6.6

storage temp.

−20°C

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Application

Carbonic Anhydrase I from human erythrocytes has been used as a pI (isoelectric point) marker in two-dimensional gel electrophoresis.

Biochem/physiol Actions

Carbonic Anhydrase I from human erythrocytes is a protein which is used as a standard pI (isoelectric point) marker for isoelectric focussing experiments.

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

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

Certificates of Analysis (COA)

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The focusing positions of polypeptides in immobilized pH gradients can be predicted from their amino acid sequences.
Bjellqvist B, et al.
Electrophoresis, 14, 1023-1031 (1993)
Two-dimensional gel isoelectric focusing.
Stastna M and Slais K
Electrophoresis, 26, 3586-3591 (2005)
Forskolin and camptothecin induce a 30 kDa protein associated with melatonin production in Y79 human retinoblastoma cells.
Janavs JL, et al.
The Journal of Neuroscience, 15, 298-309 (1995)
Yuzhu Bian et al.
Artificial cells, nanomedicine, and biotechnology, 41(1), 60-68 (2013-01-26)
Even though erythrocytes transport both oxygen and carbon dioxide, research on blood substitutes has concentrated on the transport of oxygen and its vasoactivity and oxidative effects. Recent study in a hemorrhagic shock animal model shows that the degree of tissue
A Mayer et al.
British journal of cancer, 108(2), 402-408 (2013-01-17)
Experimental studies have established a causal connection between tumour hypoxia, hypoxia-associated proteome changes and downregulation of E-cadherin, the final common pathway of epithelial-to-mesenchymal transition (EMT). Our study aimed at elucidating the interrelationship of these processes in cancers of the uterine

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