Chlorophyll a-b binding protein AB96 (AB96), Recombinant Protein

Full Product Name

Recombinant Pisum sativum Chlorophyll a-b binding protein AB96 (AB96)

Product Synonym Names

Recombinant Chlorophyll a-b binding protein AB96 (AB96); Chlorophyll a-b binding protein AB96; LHCII type I CAB-AB96; LHCP Major 15

Product Gene Name

AB96 recombinant protein

Product Synonym Gene Name

AB96

Purity

Greater or equal to 85% purity as determined by SDS-PAGE. (lot specific)

Sequence

TTKKVASSSS PWHGPDGVKY LGPFSGESPS YLTGEFPGDY GWDTAGLSAD PETFAKNREL EVIHSRWAML GALGCVFPEL LSRNGVKFGE AVWFKAGSQI FSEGGLDYLG NPSLVHAQSI LAIWATQVIL MGAVEGYRIA GGPLGEVVDP LYPGGSFDPL GLAEVPEAFA ELKVKELKNG RLAMFSMFGF FVPAIVTGKG PLENLADHLA DPVNNNAWSY ATNFVPGK

Sequence Positions

1-228

Format

Lyophilized or liquid (Format to be determined during the manufacturing process)

Host

E Coli or Yeast or Baculovirus or Mammalian Cell

Molecular Weight

24,328 Da

Storage

Store at -20℃. For extended storage, store at -20 or -80℃.

Protein Family

Chlorophyll a-b binding protein

NCBI Accession #

P04159.1

NCBI GI #

115773

NCBI Official Full Name

Chlorophyll a-b binding protein AB96

UniProt Gene Name

AB96  

UniProt Synonym Gene Names

LHCP  

UniProt Protein Name

Chlorophyll a-b binding protein AB96

UniProt Synonym Protein Names

LHCII type I CAB-AB96; LHCP; Major 15

UniProt Entry Name

CB21_PEA

UniProt Primary Accession #

P04159

UniProt Comments

Function: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.May channel protons produced in the catalytic Mn center of water oxidation into the thylakoid lumen.

Cofactor: Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin

By similarity.

Subunit structure: The LHC complex consists of chlorophyll a-b binding proteins.

Subcellular location: Plastid › chloroplast thylakoid membrane; Multi-pass membrane protein.

Domain: The N-terminus of the protein extends into the stroma where it is involved with adhesion of granal membranes and post-translational modifications; both are believed to mediate the distribution of excitation energy between photosystems I and II.

Post-translational modification: Photoregulated by reversible phosphorylation of its threonine residues

By similarity.

Sequence similarities: Belongs to the light-harvesting chlorophyll a/b-binding (LHC) protein family.