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P6835

Sigma-Aldrich

Poly(Glu, Tyr)−Agarose

Glu:Tyr (4:1), saline suspension

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About This Item

MDL number:
UNSPSC Code:
12352200
NACRES:
NA.26

form

saline suspension

feed ratio

Glu:Tyr (4:1)

extent of labeling

12-15 mg per mL gel

matrix

cross-linked 4% beaded agarose

matrix activation

cyanogen bromide

matrix attachment

carboxyl

matrix spacer

8 atoms

storage temp.

2-8°C

Application

Useful for the purification of tyrosine kinase

Physical form

Suspension in 1.0 M NaCl containing preservative

Other Notes

For additional technical information on polyamino acids please visit the Polyamino acid FAQ resource.

Disclaimer

For U.S. Customers: Contains mercury; Do not place in trash - dispose according to local, state, or federal laws.

Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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S Braun et al.
Archives of biochemistry and biophysics, 247(2), 424-432 (1986-06-01)
Three membranous protein tyrosine kinases (PTKs) have been partially purified from human placenta and pig brain. The two placental enzymes (PTK-1 and -2) are distinct with respect to solubility in detergents, molecular weight, and enzymatic properties. The brain protein tyrosine
K Uma Devi et al.
Andrologia, 32(2), 95-106 (2001-02-07)
Genistein, tyrphostin and piceatannol, which are specific inhibitors of protein tyrosine kinase, were screened for their effects on the motility of intact and demembranated hamster spermatozoa. Of the three inhibitors only piceatannol inhibited the motility of intact spermatozoa. None of
Claudia Lalancette et al.
Proteomics, 6(16), 4523-4540 (2006-07-19)
Numerous sperm proteins have been identified on the basis of their increase in tyrosine phosphorylation during capacitation. However, the tyrosine kinases present in spermatozoa that are responsible for this phosphorylation remain unknown. As spermatozoa are devoid of transcriptional and translational
S R Mullapudi et al.
The Biochemical journal, 351 Pt 2, 393-402 (2000-10-12)
We showed recently that human O(6)-alkylguanine-DNA alkyltransferase (AGT), an important target for improving cancer chemotherapy, is a phosphoprotein and that phosphorylation inhibits its activity [Srivenugopal, Mullapudi, Shou, Hazra and Ali-Osman (2000) Cancer Res. 60, 282-287]. In the present study we

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