Chlorophyll a-b binding protein 151, chloroplastic (CAB-151), Recombinant Protein

Full Product Name

Recombinant Gossypium hirsutum Chlorophyll a-b binding protein 151, chloroplastic (CAB-151)

Product Synonym Names

Recombinant Chlorophyll a-b binding protein 151, chloroplastic (CAB-151); Chlorophyll a-b binding protein 151, chloroplastic; LHCII type II CAB-151; LHCP

Product Gene Name

CAB-151 recombinant protein

Product Synonym Gene Name

CAB-151

Purity

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

Sequence

RRTVKSAPTS IWYGPDRPKY LGPFSDQIPS YLTGEFPGDY GWDTAGLSAD PETFAKNREL EVIHCRWAML GALGCVFPEI LSKNGVKFGE AVWFKAGSQI FSEGGLDYLG NPNLIHAQSI LAIWACQVVL MGFVEGYRVG GGPLGEGLDP IYPGGAFDPL GLADDPDAFA ELKVKEIKNG RLAMFSMFGF FVQAIVTGKG PIENLFDHLA DPVANNAWAY ATNFVPGK

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

28,407 Da

Storage

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

Protein Family

Chlorophyll a-b binding protein

NCBI Accession #

P27518.2

NCBI GI #

1345698

NCBI Official Full Name

Chlorophyll a-b binding protein 151, chloroplastic

UniProt Gene Name

CAB-151  

UniProt Synonym Gene Names

LHCP  

UniProt Protein Name

Chlorophyll a-b binding protein 151, chloroplastic

UniProt Synonym Protein Names

LHCII type II CAB-151

UniProt Entry Name

CB21_GOSHI

UniProt Primary Accession #

P27518

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.

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.

Tissue specificity: Present at high levels in leaves and cotyledons.

Induction: Markedly increased by light.

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.