Product: Phospho-CaSR (Thr888) Mouse Monoclonal Antibody
Catalog: BF8409
Description: Mouse monoclonal antibody to Phospho-CaSR (Thr888)
Application: IF/ICC
Reactivity: Human
Prediction: Pig, Bovine, Horse, Sheep, Rabbit, Dog, Chicken
Mol.Wt.: 140kDa; 121kD(Calculated).
Uniprot: P41180

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 100ul $280 In stock
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Product Info

Source:
Mouse
Application:
IF/ICC 1:100-1:500
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human
Clonality:
Monoclonal [AFfirm8409]
Specificity:
Phospho-CaSR (Thr888) Mouse Monoclonal Antibody detects endogenous levels of total Calcium Sensing Receptor only when phosphorylated at Threonine 888
Conjugate:
Unconjugated.
Purification:
Affinity-chromatography.
Storage:
Mouse IgG1 in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

Ca sensing receptor; Ca2+ sensing receptor 1; Ca2+ sensing receptor; CAR; CaSR; CASR_HUMAN; EIG8; Extracellular calcium sensing receptor; Extracellular calcium sensing receptor [Precursor]; Extracellular calcium-sensing receptor; FHH; FIH; GPRC2A; HHC; HHC1; Hypocalciuric hypercalcemia 1; Hypocalciuric hypercalcemia 1 severe neonatal hyperparathyroidism; MGC138441; NSHPT; Parathyroid Ca(2+) sensing receptor 1; Parathyroid Cell calcium sensing receptor; Parathyroid Cell calcium-sensing receptor; PCAR 1; PCaR1;

Immunogens

Immunogen:
Uniprot:
Gene(ID):
Expression:
P41180 CASR_HUMAN:

Expressed in the temporal lobe, frontal lobe, parietal lobe, hippocampus, and cerebellum. Also found in kidney, lung, liver, heart, skeletal muscle, placenta.

Description:
The calcium-sensing receptor (CASR) functions as a sensor for parathyroid and kidney to determine the extracellular calcium concentration and thus helps to maintain a stable calcium concentration.
Sequence:
MAFYSCCWVLLALTWHTSAYGPDQRAQKKGDIILGGLFPIHFGVAAKDQDLKSRPESVECIRYNFRGFRWLQAMIFAIEEINSSPALLPNLTLGYRIFDTCNTVSKALEATLSFVAQNKIDSLNLDEFCNCSEHIPSTIAVVGATGSGVSTAVANLLGLFYIPQVSYASSSRLLSNKNQFKSFLRTIPNDEHQATAMADIIEYFRWNWVGTIAADDDYGRPGIEKFREEAEERDICIDFSELISQYSDEEEIQHVVEVIQNSTAKVIVVFSSGPDLEPLIKEIVRRNITGKIWLASEAWASSSLIAMPQYFHVVGGTIGFALKAGQIPGFREFLKKVHPRKSVHNGFAKEFWEETFNCHLQEGAKGPLPVDTFLRGHEESGDRFSNSSTAFRPLCTGDENISSVETPYIDYTHLRISYNVYLAVYSIAHALQDIYTCLPGRGLFTNGSCADIKKVEAWQVLKHLRHLNFTNNMGEQVTFDECGDLVGNYSIINWHLSPEDGSIVFKEVGYYNVYAKKGERLFINEEKILWSGFSREVPFSNCSRDCLAGTRKGIIEGEPTCCFECVECPDGEYSDETDASACNKCPDDFWSNENHTSCIAKEIEFLSWTEPFGIALTLFAVLGIFLTAFVLGVFIKFRNTPIVKATNRELSYLLLFSLLCCFSSSLFFIGEPQDWTCRLRQPAFGISFVLCISCILVKTNRVLLVFEAKIPTSFHRKWWGLNLQFLLVFLCTFMQIVICVIWLYTAPPSSYRNQELEDEIIFITCHEGSLMALGFLIGYTCLLAAICFFFAFKSRKLPENFNEAKFITFSMLIFFIVWISFIPAYASTYGKFVSAVEVIAILAASFGLLACIFFNKIYIILFKPSRNTIEEVRCSTAAHAFKVAARATLRRSNVSRKRSSSLGGSTGSTPSSSISSKSNSEDPFPQPERQKQQQPLALTQQEQQQQPLTLPQQQRSQQQPRCKQKVIFGSGTVTFSLSFDEPQKNAMAHRNSTHQNSLEAQKSSDTLTRHEPLLPLQCGETDLDLTVQETGLQGPVGGDQRPEVEDPEELSPALVVSSSQSFVISGGGSTVTENVVNS

PTMs - P41180 As Substrate

Site PTM Type Enzyme
T186 Phosphorylation
T195 Phosphorylation
N261 N-Glycosylation
N287 N-Glycosylation
K336 Acetylation
S342 Phosphorylation
N446 N-Glycosylation
N468 N-Glycosylation
N488 N-Glycosylation
N541 N-Glycosylation
N594 N-Glycosylation
T888 Phosphorylation P05129 (PRKCG) , P17252 (PRKCA) , P05771 (PRKCB)
S892 Phosphorylation
S895 Phosphorylation
S899 Phosphorylation
S900 Phosphorylation
T906 Phosphorylation
S915 Phosphorylation

Research Backgrounds

Function:

G-protein-coupled receptor that senses changes in the extracellular concentration of calcium ions and plays a key role in maintaining calcium homeostasis. Senses fluctuations in the circulating calcium concentration and modulates the production of parathyroid hormone (PTH) in parathyroid glands (By similarity). The activity of this receptor is mediated by a G-protein that activates a phosphatidylinositol-calcium second messenger system. The G-protein-coupled receptor activity is activated by a co-agonist mechanism: aromatic amino acids, such as Trp or Phe, act concertedly with divalent cations, such as calcium or magnesium, to achieve full receptor activation.

PTMs:

N-glycosylated.

Ubiquitinated by RNF19A; which induces proteasomal degradation.

Subcellular Location:

Cell membrane>Multi-pass membrane protein.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

Expressed in the temporal lobe, frontal lobe, parietal lobe, hippocampus, and cerebellum. Also found in kidney, lung, liver, heart, skeletal muscle, placenta.

Subunit Structure:

Homodimer; disulfide-linked. Interacts with VCP and RNF19A. Interacts with ARRB1 (By similarity).

Family&Domains:

The extracellular regions of the homodimer interact in a side-by-side fashion while facing opposite directions (PubMed:27434672, PubMed:27386547). Each extracellular region consists of three domains, LB1 (ligand-binding 1), LB2 and CR (cysteine-rich) (PubMed:17360426). The two lobe-shaped domains LB1 and LB2 form a venus flytrap module (PubMed:27434672, PubMed:27386547). In the inactive configuration, the venus flytrap modules of both protomers are in the open conformation associated with the resting state (open-open) and the interdomain cleft is empty (PubMed:27434672). In addition, each protomer contains three anions, which reinforce the inactive conformation, and one calcium ion (PubMed:27434672). In the active configuration, both protomers of extracellular regions have the closed conformation associated with agonist-binding (closed-closed) (PubMed:27434672, PubMed:27386547). The ligand-binding cleft of each protomer is solely occupied by an aromatic amino-acid (PubMed:27434672, PubMed:27386547). Calcium is bound at four novel sites, including one at the homodimer interface (PubMed:27434672, PubMed:27386547). Agonist-binding induces large conformational changes within the extracellular region homodimer: first, the venus flytrap module of each protomer undergoes domain closure (PubMed:27434672, PubMed:27386547). Second, the LB2 regions of the two protomers approach each other, resulting in an expansion of the homodimer interactions involving LB2 domains (PubMed:27434672, PubMed:27386547). Third, the CR regions of the two subunits interact to form a large homodimer interface that is unique to the active state (PubMed:27434672, PubMed:27386547). The CR regions are brought into close contact by the motion involving LB2 since the two domains are rigidly associated within each subunit (PubMed:27434672, PubMed:27386547).

Belongs to the G-protein coupled receptor 3 family.

Research Fields

· Organismal Systems > Immune system > NOD-like receptor signaling pathway.   (View pathway)

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