DNAJB1 / HSP40 (His-tag) Human Protein

CAT#: AR09036PU-N

DNAJB1 / HSP40 (His-tag) human recombinant protein, 0.1 mg

Product Images

Specifications

Product Data

• Species: Human
• Expression Host: E. coli
• Expression cDNA Clone or AA Sequence:
  Protein Sequence

  MGSSHHHHHH SSGLVPRGSH MGKDYYQTLG LARGASDEEI KRAYRRQALR YHPDKNKEPG AEEKFKEIAE AYDVLSDPRK REIFDRYGEE GLKGSGPSGG SGGGANGTSF SYTFHGDPHA MFAEFFGGRN PFDTFFGQRN GEEGMDIDDP FSGFPMGMGG FTNVNFGRSR SAQEPARKKQ DPPVTHDLRV SLEEIYSGCT KKMKISHKRL NPDGKSIRNE DKILTIEVKK GWKEGTKITF PKEGDQTSNN IPADIVFVLK DKPHNIFKRD GSDVIYPARI SLREALCGCT VNVPTLDGRT IPVVFKDVIR PGMRRKVPGE GLPLPKTPEK RGDLIIEFEV IFPERIPQTS RTVLEQVLPI
• Tag: His-tag
• Predicted MW: 40.2 kDa
• Concentration: lot specific
• Purity: >95% >/= 95% by SDS PAGE
• Buffer: Presentation State: Purified
  State: Liquid purified protein
  Buffer System: 20 mM Tris (pH 8.0), 2 mM DTT, 0.2 mM PMSF, 10% glycerol
• Preparation: Liquid purified protein
• Protein Description: Recombinant human HSP40, his-tagged, is overexpressed in E.coli and purified by using the conventional column chromatography techniques.
• Storage: Store (in aliquots) at -20°C. Avoid repeated freezing and thawing.
• Stability: Shelf life: one year from despatch.

Reference Data

• RefSeq: NP_001287843
• Locus ID: 3337
• UniProt ID: P25685
• Cytogenetics: 19p13.12
• Synonyms: Hdj1; Hsp40; HSPF1; RSPH16B; Sis1
• Summary: 'This gene encodes a member of the DnaJ or Hsp40 (heat shock protein 40 kD) family of proteins. DNAJ family members are characterized by a highly conserved amino acid stretch called the 'J-domain' and function as one of the two major classes of molecular chaperones involved in a wide range of cellular events, such as protein folding and oligomeric protein complex assembly. The encoded protein is a molecular chaperone that stimulates the ATPase activity of Hsp70 heat-shock proteins in order to promote protein folding and prevent misfolded protein aggregation. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Sep 2015]'