CD133 Antibody [F19M17] | Primary Antibodies

Application: Reactivity: Human

Usage Information

Dilution
WB1:1000 IHC1:200 - 1:800 IF1:200 - 1:800

Application
WB, IHC, IF

Reactivity
Human

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
133 kDa

Positive Control	Human infiltrating papillary carcinoma of the breast tissue; Human breast carcinoma tissue; Human colon carcinoma tissue; Normal human kidney tissue; Human ovarian carcinoma tissue; WERI-Rb-1 cells
Negative Control	Jurkat cells; HeLa cells; MCF7 cells

Datasheet & SDS

Biological Description

Specificity
CD133 Antibody [F19M17] detects endogenous levels of total CD133 protein.

Clone
F19M17

Synonym(s)
Prominin-1; Antigen AC133; Prominin-like protein 1; CD133; PROM1; PROML1

Background
CD133, also known as prominin-1, is a member of the prominin family of pentaspan transmembrane glycoproteins that serve as markers for stem and progenitor cells in various tissues. The protein traverses the membrane five times, resulting in an N-terminal extracellular domain, two large extracellular loops with multiple N-glycosylation sites, two small intracellular loops, and a cytoplasmic C-terminal tail enriched with phosphorylation sites such as Tyr828. Extensive glycosylation increases its apparent molecular weight compared to its unglycosylated core. CD133 is localized to plasma membrane protrusions like microvilli, filopodia, and cilia, where it binds cholesterol and helps organize curved lipid domains. Phosphorylation at Tyr828 by Src kinases enables recruitment of the PI3K p85 subunit, enhancing the conversion of PIP2 to PIP3 and activating Akt signaling to promote cell proliferation and survival. This phosphorylation site also allows CD133 to interact with the Arp2/3 complex, fostering actin branching and the formation of microvillar structures. CD133 interacts with proteins such as Arl13b and HDAC6 through Lys138 to regulate the balance of microtubule assembly and disassembly, thus controlling cilium length. CD133’s presence in membrane protrusions facilitates the release of extracellular vesicles, which are important for intercellular signaling. CD133 interacts with several key signaling pathways, including Wnt/β-catenin, TGF-β/Smad, and MAPK/ERK, to govern stem cell differentiation, migration, and polarity. High levels of CD133 are a hallmark of cancer stem cells in tumors such as glioblastoma and hepatoma, where it supports autophagy, glucose uptake, and tumor initiation, especially under stress conditions. Mutations that disrupt GM1 binding or alter Tyr828 phosphorylation can change microvillar morphology, leading to branched or shortened protrusions and are associated with retinal degeneration.

Background

CD133, also known as prominin-1, is a member of the prominin family of pentaspan transmembrane glycoproteins that serve as markers for stem and progenitor cells in various tissues. The protein traverses the membrane five times, resulting in an N-terminal extracellular domain, two large extracellular loops with multiple N-glycosylation sites, two small intracellular loops, and a cytoplasmic C-terminal tail enriched with phosphorylation sites such as Tyr828. Extensive glycosylation increases its apparent molecular weight compared to its unglycosylated core. CD133 is localized to plasma membrane protrusions like microvilli, filopodia, and cilia, where it binds cholesterol and helps organize curved lipid domains. Phosphorylation at Tyr828 by Src kinases enables recruitment of the PI3K p85 subunit, enhancing the conversion of PIP2 to PIP3 and activating Akt signaling to promote cell proliferation and survival. This phosphorylation site also allows CD133 to interact with the Arp2/3 complex, fostering actin branching and the formation of microvillar structures. CD133 interacts with proteins such as Arl13b and HDAC6 through Lys138 to regulate the balance of microtubule assembly and disassembly, thus controlling cilium length. CD133’s presence in membrane protrusions facilitates the release of extracellular vesicles, which are important for intercellular signaling. CD133 interacts with several key signaling pathways, including Wnt/β-catenin, TGF-β/Smad, and MAPK/ERK, to govern stem cell differentiation, migration, and polarity. High levels of CD133 are a hallmark of cancer stem cells in tumors such as glioblastoma and hepatoma, where it supports autophagy, glucose uptake, and tumor initiation, especially under stress conditions. Mutations that disrupt GM1 binding or alter Tyr828 phosphorylation can change microvillar morphology, leading to branched or shortened protrusions and are associated with retinal degeneration.

References
https://pubmed.ncbi.nlm.nih.gov/38532366/ https://pubmed.ncbi.nlm.nih.gov/30328220/

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%