CA9 Antibody [J19A24]

Catalog No.: F1507

Application: Reactivity: Human

Lane 1: LN18, Lane 2: SW620

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代表番号: 045-509-1970|電子メール：sales@selleck.co.jp

使用情報

Dilution
WB1:1000 IP1:200 IHC1:50 - 1:200

Application
WB, IP, IHC

Source
Rabbit Monoclonal Antibody

Reactivity
Human

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
35-58 kDa

Datasheet & SDS

生物学的記述

Specificity
CA9 Antibody [J19A24] detects endogenous levels of total CA9 protein.

Clone
J19A24

Synonym(s)
Carbonic anhydrase 9; Carbonate dehydratase IX; Carbonic anhydrase IX (CA-IX; CAIX); Membrane antigen MN; P54/58N; Renal cell carcinoma-associated antigen G250 (RCC-associated antigen G250); pMW1; CA9; G250; MN

Background
CA9 (carbonic anhydrase 9) is a transmembrane glycoprotein of the α-class carbonic anhydrases, which are zinc metalloenzymes catalyzing the reversible hydration of CO₂ to HCO₃⁻ and H⁺. CA9 is predominantly upregulated in hypoxic tumor cells owing to HIF-1α activation under conditions of wild-type VHL suppression. CA9 is a 459-amino-acid protein containing an N-terminal proteoglycan-like (PG) domain (59 residues) unique among carbonic anhydrases for cell adhesion, followed by an extracellular catalytic domain (257 residues) organized around a 10-stranded antiparallel β-sheet core and a central zinc ion coordinated by His226, His228, and His251. It also features N-linked glycosylation at Asn309 (or Asn213 in catalytic domain terms), a 20-residue transmembrane domain, and a short C-terminal intracellular tail (25 residues) that includes phosphorylatable sites Thr443, Ser448, and Tyr449. CA9 plays a crucial role in tumor physiology by generating extracellular protons and bicarbonate, which help maintain alkaline intracellular pH and acidic extracellular pH. This supports CO₂ diffusion, tumor cell survival, proliferation, invasion, and metastasis by promoting extracellular matrix degradation, epithelial-mesenchymal transition (EMT), and modulating adhesion through PG-β-catenin interactions. Consequently, CA9 is central to hypoxic adaptation, metabolic reprogramming, and angiogenesis in solid tumors, including renal cell carcinoma and cervical cancer, making it both a valuable hypoxia biomarker and a therapeutic target, with inhibitors designed to disrupt tumor acidosis and progression.

Background

CA9 (carbonic anhydrase 9) is a transmembrane glycoprotein of the α-class carbonic anhydrases, which are zinc metalloenzymes catalyzing the reversible hydration of CO₂ to HCO₃⁻ and H⁺. CA9 is predominantly upregulated in hypoxic tumor cells owing to HIF-1α activation under conditions of wild-type VHL suppression. CA9 is a 459-amino-acid protein containing an N-terminal proteoglycan-like (PG) domain (59 residues) unique among carbonic anhydrases for cell adhesion, followed by an extracellular catalytic domain (257 residues) organized around a 10-stranded antiparallel β-sheet core and a central zinc ion coordinated by His226, His228, and His251. It also features N-linked glycosylation at Asn309 (or Asn213 in catalytic domain terms), a 20-residue transmembrane domain, and a short C-terminal intracellular tail (25 residues) that includes phosphorylatable sites Thr443, Ser448, and Tyr449. CA9 plays a crucial role in tumor physiology by generating extracellular protons and bicarbonate, which help maintain alkaline intracellular pH and acidic extracellular pH. This supports CO₂ diffusion, tumor cell survival, proliferation, invasion, and metastasis by promoting extracellular matrix degradation, epithelial-mesenchymal transition (EMT), and modulating adhesion through PG-β-catenin interactions. Consequently, CA9 is central to hypoxic adaptation, metabolic reprogramming, and angiogenesis in solid tumors, including renal cell carcinoma and cervical cancer, making it both a valuable hypoxia biomarker and a therapeutic target, with inhibitors designed to disrupt tumor acidosis and progression.

References
[1] Mahon BP, et al. Biochemistry. 2016 Aug 23;55(33):4642-53. [2] Sedlakova O, et al. Front Physiol. 2014 Jan 8;4:400.

PVDFメンブレン孔径参考表

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%