Rabbit HSP/Chaperone Sampler Kit Polyclonal Antibody

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Cat. No.: DAB-0012148

Size: 20 µL Size: 100 µL Size: Customer Size

Product Information
Clonality	Polyclonal
Host Species	Rabbit
Product Description	Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to human HSP70, and corresponding to residues at the carboxy-terminus of human HSF1 protein. Polyclonal antibodies are purified by protein A and peptide affinity chromatography. Rabbit monclonal antibodies are produced by immunizing rabbits with a synthetic peptide corresponding to residues surrounding Trp68 of human HSP60 protein, residues surrounding Gly584 of human BiP, surrounding Asn300 of HSP90, corresponding to Glu223 of human HSP40/Hdj1, corresponding to the sequence of human calnexin, and corresponding to the sequence of human PDI.
Format	Liquid
Purity	Affinity purity

Target Information
Gene Description	HSP70 and HSP90 are molecular chaperones expressed constitutively under normal conditions to maintain protein homeostasis and are induced upon environmental stress. HSP70 and HSP90 interact with unfolded proteins to prevent irreversible aggregation and catalyze the refolding of their substrates in an ATP-dependent manner. HSP40 family proteins bind unfolded proteins and prevent their aggregation, and deliver unfolded protiens to HSP70. HSP60 has primarily been known as a mitochondrial protein that is important for folding key proteins after import into the mitochondria. HSP60 is also present in the cytosol of many cells and is induced by stress, inflammatory and immune responses, autoantibodies correlated with Alzheimer's, coronary artery diseases, MS, and diabetes. Secretory and transmembrane proteins are synthesized on polysomes and translocate into the endoplasmic reticulum where they are often modified by the formation of disulfide bonds, amino-linked glycosylation and folding. The ER contains a pool of molecular chaperones including calnexin, BiP and protein disulfide isomerase. Calenxin is a calcium-binding protein embedded in the ER membrane that retains newly synthesized glycoproteins inside the ER to ensure proper folding and quality control. When protein folding is disturbed inside the ER, Bip synthesis is increased. Subsequently, BiP binds to misfolded proteins to prevent them from forming aggregates and assists them to refold properly. PDI catalyzes the formation and isomerization of disulfide bonds required to reach a proteins native state. Heat shock gene transcription is regulated by a familly of heat shock factors, transcriptional activators that bind to heat shock response elements located upstream of all heat shock genes. During attenuation from the heat shock response, HSF1 is repressed by direct binding of HSP70, HSP40/Hdj-1 and HSF binding protein 1 .

Target Information

Gene Description

HSP70 and HSP90 are molecular chaperones expressed constitutively under normal conditions to maintain protein homeostasis and are induced upon environmental stress. HSP70 and HSP90 interact with unfolded proteins to prevent irreversible aggregation and catalyze the refolding of their substrates in an ATP-dependent manner. HSP40 family proteins bind unfolded proteins and prevent their aggregation, and deliver unfolded protiens to HSP70. HSP60 has primarily been known as a mitochondrial protein that is important for folding key proteins after import into the mitochondria. HSP60 is also present in the cytosol of many cells and is induced by stress, inflammatory and immune responses, autoantibodies correlated with Alzheimer's, coronary artery diseases, MS, and diabetes. Secretory and transmembrane proteins are synthesized on polysomes and translocate into the endoplasmic reticulum where they are often modified by the formation of disulfide bonds, amino-linked glycosylation and folding. The ER contains a pool of molecular chaperones including calnexin, BiP and protein disulfide isomerase. Calenxin is a calcium-binding protein embedded in the ER membrane that retains newly synthesized glycoproteins inside the ER to ensure proper folding and quality control. When protein folding is disturbed inside the ER, Bip synthesis is increased. Subsequently, BiP binds to misfolded proteins to prevent them from forming aggregates and assists them to refold properly. PDI catalyzes the formation and isomerization of disulfide bonds required to reach a proteins native state. Heat shock gene transcription is regulated by a familly of heat shock factors, transcriptional activators that bind to heat shock response elements located upstream of all heat shock genes. During attenuation from the heat shock response, HSF1 is repressed by direct binding of HSP70, HSP40/Hdj-1 and HSF binding protein 1 .

Shipping & Storage
Shipping	Shipped at 4 °C.
Storage Instructions	Store at +4 °C short term (1-2 weeks). Store at -20 °C long term.
Storage Buffer	Constituent: 100% PBS

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