Chlorophyll a-b binding protein 215, chloroplastic (CAB215), Recombinant Protein

Full Product Name

Recombinant Pisum sativum Chlorophyll a-b binding protein 215, chloroplastic (CAB215)

Product Synonym Names

Recombinant Chlorophyll a-b binding protein 215, chloroplastic (CAB215); Chlorophyll a-b binding protein 215, chloroplastic; LHCII type II CAB-215; LHCP

Product Gene Name

CAB215 recombinant protein

Product Synonym Gene Name

CAB215; LHCB2

Purity

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

Sequence

RRTVKSAPES IWYGPDRPKY LGPFSEQIPS YLTGEFPGDY GWDTAGLSAD PETFARNREL EVIHSRWAML GALGCTFPEL LEKNGVKFGE AVWFKAGSQI FAEGGLDYLG NPNLIHAQSI LAIWATQVVL MGFVEGYRVG GGPLGEGLDP LYPGGAFDPL GLADDPDSFA ELKVKELKNG RLAMFSMFGF FVQAIVTGKG PIQNLYDHVA DPVANNAWAF ATNFVPGQ

Sequence Positions

38-265

Format

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

Host

E Coli or Yeast or Baculovirus or Mammalian Cell

Molecular Weight

28,885 Da

Storage

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

Protein Family

Chlorophyll a-b binding protein

NCBI Accession #

P27520.1

NCBI GI #

115797

NCBI Official Full Name

Chlorophyll a-b binding protein 215, chloroplastic

UniProt Gene Name

CAB215  

UniProt Synonym Gene Names

LHCB2; LHCP  

UniProt Protein Name

Chlorophyll a-b binding protein 215, chloroplastic

UniProt Synonym Protein Names

LHCII type II CAB-215

UniProt Entry Name

CB215_PEA

UniProt Primary Accession #

P27520

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.