HSP70 cDNA ORF Clone in Cloning Vector, Human

Cat: HG11660-M
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HSP70 cDNA ORF Clone in Cloning Vector, Human General Information
Gene
Species
Human
NCBI Ref Seq
RefSeq ORF Size
1926 bp
Sequence Description
Identical with the Gene Bank Ref. ID sequence except for two point mutations: 12 C/A, 222 T/C not causing the amino acid variation.
Description
Full length Clone DNA of Human heat shock 70kDa protein 1A.
Plasmid
Vector
pMD18-T Simple Vector
Sequencing Primers
M13-47 and RV-M
Quality Control
The plasmid is confirmed by full-length sequencing.
Screening
Antibiotic in E.coli
Ampicillin
Storage & Shipping
Shipping
Each tube contains lyophilized plasmid.
Storage
The lyophilized plasmid can be stored at ambient temperature for three months.
HSP70 cDNA ORF Neucleotide Sequence and Amino Acid Sequence Information

**Sino Biological guarantees 100% sequence accuracy of all synthetic DNA constructs we deliver, but we do not guarantee protein expression in your experimental system. Protein expression is influenced by many factors that may vary between experiments or laboratories.**

HSP70 cDNA ORF Clone in Cloning Vector, Human Alternative Names
HEL-S-103 cDNA ORF Clone, Human;HSP70-1 cDNA ORF Clone, Human;HSP70-1A cDNA ORF Clone, Human;HSP70I cDNA ORF Clone, Human;HSP72 cDNA ORF Clone, Human;HSPA1 cDNA ORF Clone, Human
HSP70 Background Information

HSPA1A is a member of the Hsp70 protein family. The 70 kilodalton heat shock proteins (Hsp70s) are a family of ubiquitously expressed heat shock proteins. HSP are abundant and conserved proteins present in all cells. Upon temperature shock or other stress stimuli, HSP are synthesized intracellularly, which may protect cells from protein denaturation or from death. Extracellularly, HSP can serve a cytokine function to initiate both innate and adaptive immunity through activation of APC. HSP serves also a chaperone function and facilitates presentation of antigen peptide to T cells. Molecular chaperones of the Hsp70 family have diverse functions in cells. They assist the folding of newly synthesized and stress-denatured proteins, as well as the import of proteins into organelles, and the dissociation of aggregated proteins. The well-conserved Hsp70 chaperones are ATP dependent: binding and hydrolysis of ATP regulates their interactions with unfolded polypeptide substrates, and ATPase cycling is necessary for their function. All cellular functions of Hsp70 chaperones use the same mechanism of ATP-driven polypeptide binding and release. 

Full Name
heat shock 70kDa protein 1A
References
  • Heck TG, et al. (2011) HSP70 expression: does it a novel fatigue signalling factor from immune system to the brain Cell Biochem Funct. 29 (3): 215-26.
  • Chen T, et al. (2010) Stress for maintaining memory: HSP70 as a mobile messenger for innate and adaptive immunity. Eur J Immunol. 40 (6): 1541-4.
  • Young JC. (2010) Mechanisms of the Hsp70 chaperone system. Biochem Cell Biol. 88 (2): 291-300.
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