Cleaved-Caspase-3 p12 (D175) Rabbit Polyclonal Antibody

Cleaved-Caspase-3 p12 (D175) Rabbit Polyclonal Antibody

Size1:50μl Price1:$118
Size2:100μl Price2:$220
Size3:500μl Price3:$980
SKU: APRab08957 Category: Polyclonal Antibody Tags: , , , ,

Datasheet

Summary

Production Name

Cleaved-Caspase-3 p12 (D175) Rabbit Polyclonal Antibody

Description

Rabbit Polyclonal Antibody

Host

Rabbit

Application

WB,IHC,ELISA

Reactivity

Human,Rat,Mouse

 

Performance

Conjugation

Unconjugated

Modification

Unmodified

Isotype

IgG

Clonality

Polyclonal

Form

Liquid

Storage

Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles.

Buffer

Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% New type preservative N.

Purification

Affinity purification

 

Immunogen

Gene Name

CASP3

Alternative Names

CASP3; CPP32; Caspase-3; CASP-3; Apopain; Cysteine protease CPP32; CPP-32; Protein Yama; SREBP cleavage activity 1; SCA-1

Gene ID

836

SwissProt ID

P42574

 

Application

Dilution Ratio

WB 1:500-2000, IHC-p 1:50-300. ELISA 1:10000-20000

Molecular Weight

12 35kD

 

Background

This gene encodes a protein which is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This protein cleaves and activates caspases 6, 7 and 9, and the protein itself is processed by caspases 8, 9 and 10. It is the predominant caspase involved in the cleavage of amyloid-beta 4A precursor protein, which is associated with neuronal death in Alzheimer's disease. Alternative splicing of this gene results in two transcript variants that encode the same protein. [provided by RefSeq, Jul 2008],catalytic activity:Strict requirement for an Asp residue at positions P1 and P4. It has a preferred cleavage sequence of Asp-Xaa-Xaa-Asp-|- with a hydrophobic amino-acid residue at P2 and a hydrophilic amino-acid residue at P3, although Val or Ala are also accepted at this position.,enzyme regulation:Inhibited by isatin sulfonamides.,function:Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin.,PTM:Cleavage by granzyme B, caspase-6, caspase-8 and caspase-10 generates the two active subunits. Additional processing of the propeptides is likely due to the autocatalytic activity of the activated protease. Active heterodimers between the small subunit of caspase-7 protease and the large subunit of caspase-3 also occur and vice versa.,PTM:S-nitrosylated on its catalytic site cysteine in unstimulated human cell lines and denitrosylated upon activation of the Fas apoptotic pathway, associated with an increase in intracellular caspase activity. Fas therefore activates caspase-3 not only by inducing the cleavage of the caspase zymogen to its active subunits, but also by stimulating the denitrosylation of its active site thiol.,similarity:Belongs to the peptidase C14A family.,subunit:Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 17 kDa (p17) and a 12 kDa (p12) subunit.,tissue specificity:Highly expressed in lung, spleen, heart, liver and kidney. Moderate levels in brain and skeletal muscle, and low in testis. Also found in many cell lines, highest expression in cells of the immune system.,

 

Research Area

MAPK_ERK_Growth;MAPK_G_Protein;p53;Apoptosis_Inhibition;Apoptosis_Mitochondrial;Apoptosis_Overview;Natural killer cell mediated cytotoxicity;Alzheimer's disease;Parkinson's disease;Amyotrophic lateral sclerosis (ALS);Huntington's disease;Epithelial cell signaling in Helicobacter pylori infection;Pathways in cancer;Colorectal cancer;Viral myocarditis;