ACA2 | Calcium-transporting ATPase 2

AS17 4155 | Clonality: Polyclonal | Host: Rabbit | Reactivity: Arabidopsis thaliana

Product Information

Immunogen GST-fusion of ACA2 peptide, purified by SDS-PAGE of Arabidopsis thaliana
ACA2 protein sequence, UniProt: O81108, TAIR: AT4G37640

Host

Rabbit

Clonality

Polyclonal

Purity Serum

Format Lyophilized

Quantity 50 µl

Reconstitution For reconstitution add 50 µl, of sterile water

Storage Store at -20°C; once reconstituted make aliquots to avoid repeated freeze-thaw cycles. Please remember to spin the tubes briefly prior to opening them to avoid any losses that might occur from material adhering to the cap or sides of the tube.

Tested applications

Western blot (WB)

Recommended dilution

1 : 10 000 (WB)

Expected | apparent MW

110 | 110 kDa

Reactivity

Confirmed reactivity Arabidopsis thaliana

Not reactive in No confirmed exceptions from predicted reactivity are currently known

Application examples

Additional information

ACA2 can be found in a good levels in: roots and flowers while the levels in leaves and siliques are very low. Harper et al. 1998.
This antibody is recognizing both full length and trunctated forms.

Background

Background ACA2 (Calcium-transporting ATPase 2) is a magnesium-dependent enzyme ((EC:3.6.3.8), which catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol into the endoplasmic reticulum. Alternative name: Ca(2+)-ATPase isoform 2

Product citations

Selected references Hwang et al. (2000). Calmodulin activation of an endoplasmic reticulum-located calcium pump involves an interaction with the N-terminal autoinhibitory domain.Plant Physiol. 2000 Jan;122(1):157-68.
Hwang et al. (2000). Calmodulin activation of an endoplasmic reticulum-located calcium pump involves an interaction with the N-terminal autoinhibitory domain.Plant Physiol. 2000 Jan;122(1):157-68.
Harper et al. (1998). A novel calmodulin-regulated Ca2+-ATPase (ACA2) from Arabidopsis with an N-terminal autoinhibitory domain. J Biol Chem. 1998 Jan 9;273(2):1099-106. (this paper contains a blot of tissue specific expression of ACA2).
Harper et al. (1998). A novel calmodulin-regulated Ca2+-ATPase (ACA2) from Arabidopsis with an N-terminal autoinhibitory domain. J Biol Chem. 1998 Jan 9;273(2):1099-106. (this paper contains a blot of tissue specific expression of ACA2)

additional information (application):	ACA2 can be found in a good levels in: roots and flowers while the levels in leaves and siliques are very low. Harper et al. 1998. This antibody is recognizing both full length and trunctated forms.
Confirmed reactivity:	Arabidopsis thaliana
not reactive in:	No confirmed exceptions from predicted reactivity are currently known
calculated \| apparent molecular mass [kDa]:	110 \| 110 kDa
Clonality:	Polyclonal
Format:	Lyophilized
Host:	Rabbit
immunogen:	GST-fusion of ACA2 peptide, purified by SDS-PAGE of Arabidopsis thaliana ACA2 protein sequence, UniProt: O81108, TAIR: AT4G37640
Purity:	Serum
Quantity:	50 µl
recommended dilution:	1 : 10 000 (WB)
Reconstitution:	For reconstitution add 50 µl, of sterile water
storage:	Store at -20°C; once reconstituted make aliquots to avoid repeated freeze-thaw cycles. Please remember to spin the tubes briefly prior to opening them to avoid any losses that might occur from material adhering to the cap or sides of the tube.
tested applications:	Western blot (WB)
All references:	Hwang et al. (2000). Calmodulin activation of an endoplasmic reticulum-located calcium pump involves an interaction with the N-terminal autoinhibitory domain.Plant Physiol. 2000 Jan;122(1):157-68. Hwang et al. (2000). Calmodulin activation of an endoplasmic reticulum-located calcium pump involves an interaction with the N-terminal autoinhibitory domain.Plant Physiol. 2000 Jan;122(1):157-68. Harper et al. (1998). A novel calmodulin-regulated Ca2+-ATPase (ACA2) from Arabidopsis with an N-terminal autoinhibitory domain. J Biol Chem. 1998 Jan 9;273(2):1099-106. (this paper contains a blot of tissue specific expression of ACA2). Harper et al. (1998). A novel calmodulin-regulated Ca2+-ATPase (ACA2) from Arabidopsis with an N-terminal autoinhibitory domain. J Biol Chem. 1998 Jan 9;273(2):1099-106. (this paper contains a blot of tissue specific expression of ACA2)
background:	ACA2 (Calcium-transporting ATPase 2) is a magnesium-dependent enzyme ((EC:3.6.3.8), which catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol into the endoplasmic reticulum. Alternative name: Ca(2+)-ATPase isoform 2

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