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AR50185PU-N Human RTN4IP1 (41-396, His-tag) - Purified

Alternate names: NIMP, NOGO-interacting mitochondrial , -4-interacting protein 1 mitochondrial Quantity: 0.5 mg Concentration: 1.0 mg/ml (determined by Bradford assay) Background: RTN4IP1 is a novel mitochondrial protein that interacts with reticulon 4, which is a potent inhibitor of regeneration following . The interaction of reticulon 4 with mitochondrial may provide insight into the mechanisms for reticulon-induced inhibition of neurite growth. Uniprot ID: Q8WWV3 NCBI: NP_116119 GeneID: 84816 Species: Human Source: E. coli Format: State: Liquid purified protein Purity: >95% by SDS - PAGE Buffer System: 20 mM Tris-HCl buffer (pH8.0) containing 20% glycerol, 1mM DTT Description: Recombinant human RTN4IP1 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography. AA Sequence: MGSSHHHHHH SSGLVPRGSH MGSTVMPAWV IDKYGKNEVL RFTQNMMMPI IHYPNEVIVK VHAASVNPID VNMRSGYGAT ALNMKRDPLH VKIKGEEFPL TLGRDVSGVV MECGLDVKYF KPGDEVWAAV PPWKQGTLSE FVVVSGNEVS HKPKSLTHTQ AASLPYVALT AWSAINKVGG LNDKNCTGKR VLILGASGGV GTFAIQVMKA WDAHVTAVCS QDASELVRKL GADDVIDYKS GSVEEQLKSL KPFDFILDNV GGSTETWAPD FLKKWSGATY VTLVTPFLLN MDRLGIADGM LQTGVTVGSK ALKHFWKGVH YRWAFFMASG PCLDDIAELV DAGKIRPVIE QTFPFSKVPE AFLKVERGHA RGKTVINVV Molecular weight: 41.4 kDa (379aa), confirmed by MALDI-TOF Storage: Store undiluted at 2-8°C for one week or (in aliquots) at -20°C to -80°C for longer. Avoid repeated freezing and thawing. Shelf life: one year from despatch. General Readings: Huber A.B. et al. (2000) Biol. Chem. 381: 407-419.Hu W.H. et al. (2002) J. Neurochem. 81: 36-45.

For research and in vitro use only. Not for diagnostic or therapeutic work. Material Safety Datasheets are available at www.acris-antibodies.com or on request. OG/20121030 1 / 2 AR50185PU-N: Human RTN4IP1 (41-396, His-tag) - Purified

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For research and in vitro use only. Not for diagnostic or therapeutic work. Material Safety Datasheets are available at www.acris-antibodies.com or on request. OG/20121030 2 / 2

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