Recombinant Glycine max Beta-conglycinin alpha subunit 1(CG-3),partial CSB-EP318442GGV
Specifications
| 20ug / 100ug / 1mg price = 100ug |
Alternative Name(s):
(CG-alpha-1)(Beta-conglycinin alpha subunit)(allergen Gly m 5)
Species: (Organism)
Glycine max (Soybean) (Glycine hispida)
Gene Names:
CG-3
Tag info:
N-terminal 10xHis-tagged and C-terminal Myc-tagged
Target Protein AA Sequence:
NPFLFGSNRFETLFKNQYGRIRVLQRFNQRSPQLQNLRDYRILEFNSKPNTLLLPNHADADYLIVILNGTAILSLVNNDDRDSYRLQSGDALRVPSGTTYYVVNPDNNENLRLITLAIPVNKPGRFESFFLSSTEAQQSYLQGFSRNILEASYDTKFEEINKVLFSREEGQQQGEQRLQESVIVEISKEQIRALSKRAKSSSRKTISSEDKPFNLRSRDPIYSNKLGKFFEITPEKNPQLRDLDIFLSIVDMNEGALLLPHFNSKAIVILVINEGDANIELVGLKEQQQEQQQEEQPLEVRKYRAELSEQDIFVIPAGYPVVVNATSNLNFFAIGINAENNQRNFLAGSQDNVISQIPSQVQELAFPGSAQAVEKLLKNQRESYFVDAQPKKKEEGNKGRKGPLSSILRAFY
Expression Region:
194-605aa
Subcellular Location:
Tissue Specificity:
Protein Length:
Partial
Pathway:
Mol. Weight:
54.4 kDa
Purity:
Greater than 85% as determined by SDS-PAGE.
Form:
Liquid or Lyophilized powder
Buffer:
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Research Areas:
Cancer
Function:
Involvement in disease:
Relevance:
Seed storage protein. Accumulates during seed development and is hydrolyzed after germination to provide a carbon and nitrogen source for the developing seedling.
Reconstitution:
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Protein Families:
Reference:
"The composition of newly synthesized proteins in the endoplasmic reticulum determines the transport pathways of soybean seed storage proteins." Mori T., Maruyama N., Nishizawa K., Higasa T., Yagasaki K., Ishimoto M., Utsumi S. Plant J. 40:238-249(2004)
