HSPA6 (NM_002155) Human Tagged ORF Clone Lentiviral Particle

CAT#: RC207795L4V

Lenti ORF particles, HSPA6 (mGFP-tagged) - Human heat shock 70kDa protein 6 (HSP70B') (HSPA6), 200ul, >10^7 TU/mL

Specifications

Product Data

• Type: Human Tagged ORF Clone Lentiviral Particle
• Tag: mGFP
• Symbol: HSPA6
• Synonyms: HSP70B'
• Mammalian Cell Selection: Puromycin
• Vector: pLenti-C-mGFP-P2A-Puro
• ACCN: NM_002155
• ORF Size: 1929 bp
• Sequence Data:
  ORF Nucleotide Sequence

  The ORF insert of this clone is exactly the same as(RC207795).
• OTI Disclaimer: The molecular sequence of this clone aligns with the gene accession number as a point of reference only. However, individual transcript sequences of the same gene can differ through naturally occurring variations (e.g. polymorphisms), each with its own valid existence. This clone is substantially in agreement with the reference, but a complete review of all prevailing variants is recommended prior to use. More info
• OTI Annotation: This clone was engineered to express the complete ORF with an expression tag. Expression varies depending on the nature of the gene.

Reference Data

• RefSeq: NM_002155.3, NP_002146.2
• RefSeq Size: 2664 bp
• RefSeq ORF: 1932 bp
• Locus ID: 3310
• UniProt ID: P17066
• Cytogenetics: 1q23.3
• Domains: HSP70
• Protein Pathways: Antigen processing and presentation, Endocytosis, MAPK signaling pathway, Spliceosome
• MW: 71 kDa
• Gene Summary: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release (PubMed:26865365).[UniProtKB/Swiss-Prot Function]