Human PFD2 / PFDN2 Protein (His Tag)

PFDN2, PFD2

• 100ug (NPP2394) Please inquiry

Catalog Number	P14349-H07E
Organism Species	Human
Host	E. coli
Synonyms	PFDN2, PFD2
Molecular Weight	The recombinant human PFDN2 consists of 169 amino acids and predicts a molecular mass of 18.5 KDa. It migrates as an approximately 18-20 KDa band in SDS-PAGE under reducing conditions.
predicted N	His
SDS-PAGE
Purity	> 95 % as determined by SDS-PAGE
Protein Construction	A DNA sequence encoding the mature form of human PFDN2 (Q9UHV9) (Met1-Ser154) was expressed with a polyhistide tag at the N-terminus.
Bio-activity
Research Area	Immunology |Signal Transduction |Protein Trafficking |Chaperones |Other Chaperones
Formulation	Lyophilized from sterile PBS, pH 7.4 1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background	PFD2, also known as PFDN2, belongs to the prefoldin beta subunit family. PFD2 is one of six subunits of prefoldin, a molecular chaperone complex that binds and stabilizes newly synthesized polypeptides, thereby allowing them to fold correctly. The complex, consisting of two alpha and four beta subunits, forms a double beta barrel assembly with six protruding coiled-coils. PFD2 binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. PFD2 also binds to a nascent polypeptide chain and promotes folding in an setting in which there are many competing pathways for nonnative proteins.
Reference	Gerhard DS, et al. (2004) The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) . Genome Res. 14(10B):2121-7. Bauch A, et al. (2004) A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway. Nat Cell Biol. 6(2):97-105. Nogaj LA, et al. (2005) Cellular levels of glutamyl-tRNA reductase and glutamate-1-semialdehyde aminotransferase do not control chlorophyll synthesis in Chlamydomonas reinhardtii. Plant Physiol. 139(1):389-96.