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S100G Human, Sheep Polyclonal Antibody

  • Regulatory status:RUO
  • Type:Polyclonal Antibody
  • Other names:S100 calcium-binding protein G, Vitamin D-dependent calcium-binding protein intestinal, CABP, Calbindin-D9k, CABP9K, CALB3, S100D
  • Species:Human
Cat. No. Size Price
1 pc / 2 - 5 pcs / 6+ pcs


RD184225100 0.1 mg $277 / $243 / On request
PubMed Product Details
Technical Data

Type

Polyclonal Antibody

Applications

Western blotting, ELISA, Immunohistochemistry

Antibodies Applications

Source of Antigen

E. coli

Hosts

Sheep

Preparation

The antibody was raised in sheep by immunization with the recombinant Human S100G.

Amino Acid Sequence

The immunization antigen (10.04 kDa) is a protein containing 87 AA of recombinant Human S100G. N-Terminal His-tag, 9 extra AA.

MKHHHHHHASTKKSPEELKRIFEKYAAKEGDPDQLSKDELKLLIQAEFPSLLKGPNTLDDLFQELDKNGDGEVSFEEFQVLVKKISQ

Species Reactivity

Human. Not yet tested in other species.

Purification Method

Immunoaffinity chromatography on a column with immobilized recombinant Human S100G.

Antibody Content

0.1 mg (determined by BCA method, BSA was used as a standard)

Formulation

The antibody is lyophilized in 0.05 M phosphate buffer, 0.1 M NaCl, pH 7.2.

Reconstitution

Add 0.2 ml of deionized water and let the lyophilized pellet dissolve completely. Slight turbidity may occur after reconstitution, which does not affect activity of the antibody. In this case clarify the solution by centrifugation.

Shipping

At ambient temperature. Upon receipt, store the product at the temperature recommended below.

Storage/Expiration

The lyophilized antibody remains stable and fully active until the expiry date when stored at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles and store frozen at -80°C. Reconstituted antibody can be stored at 4°C for a limited period of time; it does not show decline in activity after one week at 4°C.

Quality Control Test

Indirect ELISA – to determine titer of the antibody SDS PAGE – to determine purity of the antibody BCA - to determine quantity of the antibody

Note

This product is for research use only.

Summary

Research topic

Cardiovascular disease, Neural tissue markers, Oncology, Others

Summary

S100G (S100 calcium binding protein G, Calbindin 3 (CALB3), CaBP9K, CABP1) is a member of the S100 family of calcium-binding proteins. The gene encoding human S100G is located on the X-chromosome (Xq22) and consists of three exons and contains four Alu repeats. The S100G protein (molecular weight 9 kDa) is monomeric and contains two Ca2+ binding motifs, a classical C-terminal EF-hand with a canonical Ca2+ binding loop and an S100-specific N-terminal EF-hand with a modified Ca2+ binding loop called ‘‘pseudo EF-hand’’. S100G protein is present in many organs, cartilage, bone and certain teeth, such as the ameloblasts of incisors and molars. In addition, S100G mRNA is detected in the proximal small intestine, but not in human kidney, uterus or placenta (however, the protein is present in these tissues in other species). S100G is also present in mammalian intestinal epithelial cells (enterocytes). S100G mediates the transport of calcium across the enterocytes from the apical side, where entry is regulated by the calcium channel TRPV6, to the basolateral side, where calcium pumps such as PMCA1 utilize intracellular adenosine triphosphate to pump calcium into the blood. The transport of calcium across the enterocyte cytoplasm appears to be rate-limiting for calcium absorption in the intestine; the presence of calbindin increases the amount of calcium crossing the cell without raising the free concentration. Expression of S100G, like that of calbindin-D28k, is stimulated by the active vitamin D metabolite, calcitriol although the precise mechanisms are still controversial. In mice that lack the receptor for vitamin D, S100G is reduced, but not absent. The members of the S100 family are multifunctional signaling proteins that influence with many cellular events. S100G appear to be involved in neurotrophic and/or neuroprotective processes, but the mechanisms of action are not completely understood. S100G has protective neurotrophic effects during brain development, and alterations in level may serve as an early, quantitative indicator of fetal brain damage in some biological fluids (eg, cord blood). Calcium-regulatory molecule S100G is dynamically expressed and regulated in the uterine endometrium during pregnancy and suggesting that regulation of calcium ion concentration may be critical for the establishment and maintenance of pregnancy in pigs.

Summary References (9)

References to S100G

  • Choi Y, Seo H, Kim M, Ka H. Dynamic expression of calcium-regulatory molecules, TRPV6 and S100G, in the uterine endometrium during pregnancy in pigs. Biol Reprod. 2009 Dec;81 (6):1122-30
  • Donato R. RAGE: a single receptor for several ligands and different cellular responses: the case of certain S100 proteins. Curr Mol Med. 2007 Dec;7 (8):711-24
  • Griffiths EJ, Rutter GA. Mitochondrial calcium as a key regulator of mitochondrial ATP production in mammalian cells. Biochim Biophys Acta. 2009 Nov;1787 (11):1324-33
  • Leclerc E, Fritz G, Vetter SW, Heizmann CW. Binding of S100 proteins to RAGE: an update. Biochim Biophys Acta. 2009 Jun;1793 (6):993-1007
  • Marenholz I, Lovering RC, Heizmann CW. An update of the S100 nomenclature. Biochim Biophys Acta. 2006 Nov;1763 (11):1282-3
  • Rosenberg MJ, Wolff CR, El-Emawy A, Staples MC, Perrone-Bizzozero NI, Savage DD. Effects of moderate drinking during pregnancy on placental gene expression. Alcohol. 2010 Nov-Dec;44 (7-8):673-90
  • Schaub MC, Heizmann CW. Calcium, troponin, calmodulin, S100 proteins: from myocardial basics to new therapeutic strategies. Biochem Biophys Res Commun. 2008 Apr 25;369 (1):247-64
  • Shang X, Cheng H, Zhou R. Chromosomal mapping, differential origin and evolution of the S100 gene family. Genet Sel Evol. 2008 Jul-Aug;40 (4):449-64
  • Veresov VG, Konev SV. Bridging the gaps in 3D structure of the inositol 1,4,5-trisphosphate receptor-binding core. Biochem Biophys Res Commun. 2006 Mar 24;341 (4):1277-85
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