Recombinant Macaca mulatta (Rhesus macaque) Major prion protein (PRNP) | MyBioSource MBS964950 product information

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product summary

company name :

MyBioSource

product type :

protein

product name :

Recombinant Macaca mulatta (Rhesus macaque) Major prion protein (PRNP)

catalog :

MBS964950

quantity :

1 mg (E-Coli)

price :

1395 USD

product information

catalog number :

MBS964950

products type :

Recombinant Protein

products full name :

Recombinant Macaca mulatta (Rhesus macaque) Major prion protein (PRNP)

products short name :

(Rhesus macaque) Major prion protein (PRNP)

products name syn :

Recombinant (Rhesus macaque) Major prion protein (PRNP); Major prion protein; PrP; PrP27-30 PrP33-35C CD_antigen= CD230

other names :

major prion protein; Major prion protein; major prion protein; prP; prP27-30; prP33-35C; major prion protein preproprotein; PrP27-30; PrP33-35C

products gene name syn :

PRNP; PRP

other gene names :

PRNP; PRNP; PRP; PrP

uniprot entry name :

PRIO_MACMU

host :

E Coli or Yeast or Baculovirus or Mammalian Cell

sequence positions :

23-230

sequence length :

253

sequence :

KKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPH
GGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHNQWH
KPSKPKTSMKHMAGAAAAGAVVGGLGGYMLGSAMSRPLI
HFGNDYEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHD
CVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQ
YEKESQAYYQRGS

purity :

>90%

form :

Liquid containing glycerol; lyophilization may be available upon request.

storage stability :

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

other info1 :

Species: Macaca mulatta (Rhesus macaque)

ncbi gi num :

114051109

ncbi acc num :

NP_001040617.1

ncbi gb acc num :

NM_001047152.1

uniprot acc num :

P67997

ncbi mol weight :

27,676 Da

ncbi pathways :

Prion Diseases Pathway (101164); Prion Diseases Pathway (100065)

uniprot summary :

Function: May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu2+ or ZN2+ for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains . By similarity. Subunit structure: Monomer and homodimer. Has a tendency to aggregate into amyloid fibrils containing a cross-beta spine, formed by a steric zipper of superposed beta-strands. Soluble oligomers may represent an intermediate stage on the path to fibril formation. Copper binding may promote oligomerization. Interacts with APP, GRB2, ERI3/PRNPIP and SYN1. Mislocalized cytosolically exposed PrP interacts with MGRN1; this interaction alters MGRN1 subcellular location and causes lysosomal enlargement . By similarity. Interacts with KIAA1191 . By similarity. Subcellular location: Cell membrane; Lipid-anchor GPI-anchor . By similarity. Golgi apparatus . By similarity. Note: Targeted to lipid rafts via association with the heparan sulfate chains of GPC1. Colocates, in the presence of CU2+, to vesicles in para- and perinuclear regions, where both proteins undergo internalization. Heparin displaces PRNP from lipid rafts and promotes endocytosis . By similarity. Domain: The normal, monomeric form has a mainly alpha-helical structure. The disease-associated, protease-resistant form forms amyloid fibrils containing a cross-beta spine, formed by a steric zipper of superposed beta-strands. Disease mutations may favor intermolecular contacts via short beta strands, and may thereby trigger oligomerization . By similarity.Contains an N-terminal region composed of octamer repeats. At low copper concentrations, the sidechains of His residues from three or four repeats contribute to the binding of a single copper ion. Alternatively, a copper ion can be bound by interaction with the sidechain and backbone amide nitrogen of a single His residue. The observed copper binding stoichiometry suggests that two repeat regions cooperate to stabilize the binding of a single copper ion. At higher copper concentrations, each octamer can bind one copper ion by interactions with the His sidechain and Gly backbone atoms. A mixture of binding types may occur, especially in the case of octamer repeat expansion. Copper binding may stabilize the conformation of this region and may promote oligomerization . By similarity. Involvement in disease: Note=PrP is found in high quantity in the brain of humans and animals infected with the degenerative neurological diseases kuru, Creutzfeldt-Jakob disease (CJD), Gerstmann-Straussler syndrome (GSS), scrapie, bovine spongiform encephalopathy (BSE), transmissible mink encephalopathy (TME), etc. Sequence similarities: Belongs to the prion family.

size1 :

1 mg (E-Coli)

price1 :

1395 USD

size2 :

1 mg (Yeast)

price2 :

1850