Cathepsin D Antibody [H1J11] | Primary Antibodies

Application: Reactivity: Human, Mouse, Rat

Lane 1: Mouse brain, Lane 2: Rat brain

Usage Information

Dilution
WB1:1000 IHC1:75-1:300 IF1:400-1:800

Application
WB, IF, FCM

Reactivity
Human, Mouse, Rat

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW
46 kDa, 43 kDa, 28 kDa

Datasheet & SDS

Biological Description

Specificity
Cathepsin D (E5V4H) Rabbit mAb detects endogenous levels of total Cathepsin D protein.

Clone
H1J11

Synonym(s)
Cathepsin D; CTSD; CPSD

Background
Cathepsin D belongs to the aspartyl protease family and functions primarily as a lysosomal enzyme responsible for intracellular protein degradation, with emerging roles in signaling and cell death regulation. It features a bilobal structure with two aspartic acid residues in the active site that coordinate substrate cleavage at acidic pH, maturing from an inactive proenzyme through autocatalytic processing into disulfide-linked heavy and light chains. Cathepsin D traffics from lysosomes to the cytosol during apoptosis, where both active and catalytically inactive forms enhance caspase activation and cytochrome c release independently of proteolysis, interacting directly with apoptotic machinery to amplify death receptor signaling; in cancer cells, secreted procathepsin D binds to cell surface receptors like M6PR, triggering proinvasive PAR1/EGFR pathways that promote matrix remodeling via hepsin degradation and uPAR activation, while cytosolic forms cleave Bcl-2 to relieve anti-apoptotic suppression. Cathepsin D, with its dual lysosomal-cytosolic action, serves as a versatile executor of programmed cell death and tissue remodeling. This makes it an ideal target for researchers investigating lysosomal membrane permeabilization or tumor microenvironment dynamics, where pH gradients critically regulate its enzymatic activity. It supports neuronal protein turnover and autophagy flux critical for synaptic maintenance and metabolic homeostasis, with ubiquitous expression enabling broad organelle quality control. Dysregulation through overexpression correlates with breast cancer metastasis and tamoxifen resistance, particularly in ER-positive tumors where high levels predict recurrence and distant spread.

Background

Cathepsin D belongs to the aspartyl protease family and functions primarily as a lysosomal enzyme responsible for intracellular protein degradation, with emerging roles in signaling and cell death regulation. It features a bilobal structure with two aspartic acid residues in the active site that coordinate substrate cleavage at acidic pH, maturing from an inactive proenzyme through autocatalytic processing into disulfide-linked heavy and light chains. Cathepsin D traffics from lysosomes to the cytosol during apoptosis, where both active and catalytically inactive forms enhance caspase activation and cytochrome c release independently of proteolysis, interacting directly with apoptotic machinery to amplify death receptor signaling; in cancer cells, secreted procathepsin D binds to cell surface receptors like M6PR, triggering proinvasive PAR1/EGFR pathways that promote matrix remodeling via hepsin degradation and uPAR activation, while cytosolic forms cleave Bcl-2 to relieve anti-apoptotic suppression. Cathepsin D, with its dual lysosomal-cytosolic action, serves as a versatile executor of programmed cell death and tissue remodeling. This makes it an ideal target for researchers investigating lysosomal membrane permeabilization or tumor microenvironment dynamics, where pH gradients critically regulate its enzymatic activity. It supports neuronal protein turnover and autophagy flux critical for synaptic maintenance and metabolic homeostasis, with ubiquitous expression enabling broad organelle quality control. Dysregulation through overexpression correlates with breast cancer metastasis and tamoxifen resistance, particularly in ER-positive tumors where high levels predict recurrence and distant spread.

References
https://pubmed.ncbi.nlm.nih.gov/38578521/ https://pubmed.ncbi.nlm.nih.gov/18497069/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%