VBP1 Protein (His tag)
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- Target See all VBP1 (PFDN3) Proteins
- VBP1 (PFDN3) (Prefoldin Subunit 3 (PFDN3))
- Protein Type
- Recombinant
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Origin
- Human
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Source
- Escherichia coli (E. coli)
- Purification tag / Conjugate
- This VBP1 protein is labelled with His tag.
- Application
- SDS-PAGE (SDS)
- Purification
- purified by chromatography
- Purity
- > 90 % by SDS - PAGE
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- Comment
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Synonyms: Prefoldin subunit 3, PFD3, PFDN3, VBP-1
- Restrictions
- For Research Use only
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- Format
- Liquid
- Concentration
- 0.5 mg/ml (determined by Bradford assay)
- Buffer
- 20 mM Tris-HCl buffer (pH 8.0) containing 0.2 M NaCl, 50% glycerol, 2 mM DTT
- Storage
- 4 °C
- Storage Comment
- Avoid repeated freezing and thawing cycles.
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- Target
- VBP1 (PFDN3) (Prefoldin Subunit 3 (PFDN3))
- Alternative Name
- VBP1 (PFDN3 Products)
- Synonyms
- DDBDRAFT_0218815 Protein, DDBDRAFT_0237722 Protein, DDB_0218815 Protein, DDB_0237722 Protein, PFD3 Protein, PFDN3 Protein, VBP-1 Protein, prefoldin subunit 3 Protein, prefoldin alpha-like domain containing protein Protein, hypothetical protein Protein, Prefoldin subunit 3 Protein, VHL binding protein 1 Protein, von Hippel-Lindau binding protein 1 Protein, LOC732997 Protein, ANI_1_1934064 Protein, PVX_096400 Protein, CpipJ_CPIJ013352 Protein, PTRG_03324 Protein, pfdn3 Protein, PGTG_00385 Protein, Vbp1 Protein, pfd3 Protein, LOC100283660 Protein, VBP1 Protein
- Background
- Prefoldin subunit 3, also known as VBP1, belongs to the prefoldin subunit alpha family. VBP1 interacts with the Von Hippel-Lindau protein to form an intracellular complex. Because it functions as a chaperone protein, it is suspected that it may play a role in the transport of the Von Hippel-Lindau protein from the perinuclear granules to the nucleus or cytoplasm. Recombinant human VBP1 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.
- Molecular Weight
- 25 kDa (220aa), confirmed by MALDI-TOF
- NCBI Accession
- NP_003363
- Pathways
- Unfolded Protein Response
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