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Z0133-04 AZGP1 (Zinc-alpha-2-glycoprotein, Zn-alpha-2-GP, Zn-alpha-2-glycoprotein, ZAG, ZNGP1) CAS:

Specifications
References
Grade
Purified
Swiss Prot
P25311
Applications
E WB
Molecular Weight
33.5
EU Commodity Code
38220090
Shipping Temp
Dry Ice
Storage Temp
-70°C
ZA2G, ZAG, AZGP1, Zn-alpha-2-glycoprotein, Zn-alpha-2-GP, ZNGP1

Human recombinant Zinc-Alpha-2-Glycoprotein protein consisting of 291 amino acids with a molecular weight of 33.5kD (computed). The aa sequence (14-291) is identical to Swiss-Prot P25311 (aa18-295 of mature Zinc-Alfa-2-Glycoprotein). 13 extra amino acid were fused to the N-terminus (underline).

Applications
Suitable for use in ELISA, Western Blot and cell culture.
Amino Acid Sequence
PGDYKDDDDK PAGQENQDGR YSLTYIYTGL SKHVEDVPAF QALGSLNDLQ FFRYNSKDRK SQPMGLWRQV EGMEDWKQDSQLQKAREDIF METLKDIVEY YNDSNGSHVL QGRFGCEIEN NRSSGAFWKY YYDGKDYIEF NKEIPAWVPF DPAAQITKQK WEAEPVYVQR AKAYLEEECP ATLRKYLKYS KNILDRQDPP SVVVTSHQAP GEKKKLKCLA YDFYPGKIDV HWTRAGEVQE PELRGDVLHN GNGTYQSWVV VAVPPQDTAP YSCHVQHSSL AQPLVVPWEA S
Storage and Stability
Store lyophilized protein at -70°C or lower. Lyophilized product is stable for 12 months at -70°C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at -70°C or lower for long term storage. Reconstituted protein can be stored at 4°C for a week.
Source
HEK293 cells
Purity
≥ 90% by SDS-PAGE
Concentration
~0.5mg/ml (after reconstitution)
Form
Supplied as a powder lyophilized from a solution containing 0.5mg/ml protein in 20mM Tris and 50mM NaCl, pH 7.0. Reconstitute with deionized water to prepare a working stock solution of ~0.5mg/ml. Sterile-filter being using in cell culture.
Important Note
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.
References
1. Sanchez, L. M., Lopez, Otin, C., and Bjorkman, P. J. Biochemical characterization and crystalization of human Znalpha(2)-glycoprotein, a soluble class I major histocompatibility complex homolog. 2. Burmeister, W. P., Gastinel, L. N., Simister, N. E., Blum, M. L., and Bjorkman, P. J. Crystal structure at 2.2 Åresolution of the MHC-related neonatal Fc receptor. 3. Sanchez, L. M., Chirino, A. J., and Bjorkman, P. J. Crystal structure of human ZAG, a fat-depleting factor related toMHC molecules. 4. Bennett, M. J., Lebron, J. A., and Bjorkman, P. J. Crystal structure of the hereditary haemochromatosis protein HFE complexed with transferrin receptor.
USBio References
No references available
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