HSPA1L ELISA Kit (Rat)

Enzyme-linked Immunosorbent assay-Sandwich

Wet Ice

heat shock protein family A (Hsp70) member 1 like

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. Positive regulator of PRKN translocation to damaged mitochondria.

NP_997711.1

Component: Amount
HSPA1L Microplate: 96 Wells (12 x 8 Well strips)HSPA1L Lyophilized Standard: 2100X HSPA1L HRP-Detector Anitbody: 1 x 120 uL100X Avidin-HRP Conjugate: 1 x 120 uLStandard Diluent: 1 x 20 mLDetector Antibody Diluent: 1 x 12 mLConjugate Diluent: 1 x 12 mL30X Wash Buffer: 1 x 20 mLTMB Substrate: 1 x 9 mLStop Solution: 1 x 6 mL

3h

Intra-assay Precision (Precision within an assay): 3 samples with low, middle and high level Heat Shock 70kDa Protein 1 Like Protein (HSPA1L) were tested 20 times on one plate, respectively. Inter-assay Precision (Precision between assays): 3 samples with low, middle and high level Heat Shock 70kDa Protein 1 Like Protein (HSPA1L) were tested on 3 different plates, 8 replicates in each plate. CV(%) = SD/meanX100 Intra-Assay: CV<10% Inter-Assay: CV<12%