CHP

Official Full Name

calcium binding protein P22

Synonyms

chp; chemotaxis-inhibiting protein CHIPS; Chemotaxis inhibiting protein; secreted protein that specifically inhibits the activation of neutrophils and monocytes by binding to the formylated peptide receptor and the C5a receptor; blocks neutrophil migration towards the infection site and hinders the establishment of the initial; calcium binding protein P22; calcium-binding protein p22; calcineurin B homolog; SLC9A1 binding protein; calcium-binding protein CHP; calcineurin homologous protein; SLC9A1BP; FLJ20350

Cat.No.	Product Name	Price
CSC-DC003114	Panoply™ Human CHP1 Knockdown Stable Cell Line	Inquiry
CSC-DC013287	Panoply™ Human RHOV Knockdown Stable Cell Line	Inquiry
CSC-SC003114	Panoply™ Human CHP1 Over-expressing Stable Cell Line	Inquiry
CSC-SC013287	Panoply™ Human RHOV Over-expressing Stable Cell Line	Inquiry

Cat.No.	Product Name	Price
AD03696Z	Human CHP adenoviral particles	Inquiry
AD13745Z	Human RHOV adenoviral particles	Inquiry
LV08987L	human CHP (NM_007236) lentivirus particles	Inquiry
LV23998L	human RHOV (NM_133639) lentivirus particles	Inquiry

Cat.No.	Product Name	Price
SHH263325	shRNA set against Human CHP (NM_007236.4)	Inquiry
SHH395440	shRNA set against Rat RHOV (NM_138542.2)	Inquiry
SHW007892	shRNA set against Danio rerio RHOV (NM_001012250)	Inquiry
SHG176167	shRNA set against Rat Chp(NM_024139.2)	Inquiry
SHG176185	shRNA set against Human CHP(NM_007236.4)	Inquiry
SHG176203	shRNA set against Rat Rhov(NM_138542.2)	Inquiry
SHH263329	shRNA set against Mouse CHP (NM_144807.3)	Inquiry
SHH263333	shRNA set against Rat CHP (NM_024139.2)	Inquiry
SHH395432	shRNA set against Human RHOV (NM_133639.3)	Inquiry
SHH395436	shRNA set against Mouse RHOV (NM_145530.2)	Inquiry
SHW000741	shRNA set against Chicken CHP1 (NM_001007930)	Inquiry
SHW015997	shRNA set against Danio rerio CHP1 (NM_199715)	Inquiry

Cat.No.	Product Name	Price
CDCH397190	Mouse Rhov ORF clone(NM_145530.2)	Inquiry
CDCR379346	Rat Chp ORF Clone(NM_024139.2)	Inquiry
CDFR012269	Rat Chp cDNA Clone(NM_024139.2)	Inquiry
CDFR014245	Rat Rhov cDNA Clone(NM_138542.2)	Inquiry
MiUTR1H-02129	CHP1 miRNA 3'UTR clone	Inquiry
MiUTR1R-00972	CHP miRNA 3'UTR clone	Inquiry
MiUTR1R-06952	RHOV miRNA 3'UTR clone	Inquiry
CDCB162216	Chicken CHP1 ORF Clone (NM_001007930)	Inquiry
CDCB169367	Danio rerio RHOV ORF Clone (NM_001012250)	Inquiry
CDCB177472	Danio rerio CHP1 ORF Clone (NM_199715)	Inquiry
CDCB184496	Rabbit RHOV ORF clone (XM_002717975.2)	Inquiry
CDCB191275	Rabbit CHP1 ORF clone (XM_008269578.1)	Inquiry
CDCL183559	Human CHP ORF clone(NM_007236.4)	Inquiry
CDCR381292	Rat Rhov ORF Clone(NM_138542.2)	Inquiry
CDCS413129	Human CHP ORF Clone (BC008373)	Inquiry
CDCS416736	Human RHOV ORF Clone (BC112945)	Inquiry

Detailed Information

Overview

Calcium binding protein P22 is a phosphoprotein that binds to sodium hydroxide exchanger (NHEs) and Ca²⁺. It can act as a transporter, regulator or activator to control the concentration of Ca²⁺ in the cytoplasm participate in various cell functions, decode Ca²⁺ signals, and regulate the concentration of Ca²⁺ in the cell.

Figure 1. Some P22 with their Locatins & Functions (http://www. apsubiology. org).

P22 and Calcium Ions

Calcium ions act as a second messenger to control a wide range of physiological effects. Disorders of intracellular calcium levels can lead to irreversible damage and even disease. Therefore, calcium homeostasis, is very important and requires very strict regulation. In cells, the role of Ca²⁺ is largely dependent on large amounts of P22, which has the ability to bind to this ion in specific regions. For example, the family of vertebrate ef-hand Ca²⁺ binding protein S100 (soluble in saturated ammonium sulfate) affects a variety of biological processes, including cell cycle progression, cell growth, cell viability, transcription and cell differentiation.

In addition, P22 controls the concentration of Ca²⁺ in the cytoplasm by acting as a Ca²⁺ transporter on the cell membrane or a Ca²⁺ modulation sensor participating in multiple cell functions. For example, calsyntenin is expressed on ER/golgi bodies and plasma membranes of almost all neurons regulating post-synaptic signaling and APP lysis. In presynaptic vesicles, synaptic binding protein is a highly conserved P22 that promotes the release of neurotransmitters by triggering extracellular secretions.

Structure

The P22 contains a highly conserved helix-ring-helix structure or EF chiral sequence. In general, EF chiral motifs come in pairs (EF chiral motifs) and facilitate the synergistic binding of two Ca²⁺ ions in each domain. However, P22s containing single or odd number of EF chiral motifs have also been found in bacteria and eukaryotes, and are thought to play a role through the dimerization mechanism.

Some of these Ca²⁺ binding proteins, such as CaM, the most common Ca²⁺ binding proteins, exist in the cytoplasm, organelles, or cell membranes of eukaryotic cells as Ca²⁺ receptors. Other proteins appear to act as storage devices for Ca²⁺ (such as calcium-flavine, calcium web). Structurally, calmodulin is an acidic protein composed of two spherical structural domains (each region has a pair of EF hands) connected by a flexible spiral region.

Role in Disease

Of the more than 200 ef-hand calcium-binding protein family members in the human body, the most studied are calretinin (CR), calbindin d-28k (CB) and parvalbumin (PV). CR is mainly expressed in granulocytes and their parallel fibers, while PV and CB are distributed in axons, somatic cells, dendrites and spinal cord of purkinje cells. Studies have shown that antibodies to CR, CB, and PV are appropriate tools for demonstrating transient features and developmental changes in human fetal brain tissue and for detecting specific changes in pathological specimens. In late pregnancy, CB and CR were expressed in a variety of nerve cells in the subplate. The subplate is a very wide area under the cortical plate, which is a "waiting room" where different cortical affections reside before entering the cortical plate. At the 7th and 8th months, the cortex mesenchymal between CB- and PV-ir was observed in the deeper part of the cortex plate. Fetal hydrocephalus results in severe changes of CB-ir and PV-ir neurons in the lower and cortical plates: contraction of ir neurons, loss of process markers, and, in most cases, total loss of immune markers. These changes, which cannot be detected in nissl stained slices, indicate significant impairment in neural function.

References:

Carafoli E, Santella L, Branca D, Brini M (2001) Generation, control, and processing of cellular calcium signals. Crit Rev Biochem Mol Biol. 36:107–260
Kinjo, Tashi G; Schnetkamp, Paul PM. Ca²⁺ Chemistry (May 2016), Storage and Transport in Biologic Systems: An Overview. Madame Curie Bioscience Database .
"CABP1 Gene". GeneCards.
Schwaller B1, Meyer M, Schiffmann S.'New' functions for 'old' proteins: the role of the calcium-binding proteins calbindin D-28k, calretinin and parvalbumin, in cerebellar physiology. Studies with knockout mice. Cerebellum. 2002 Dec; 1(4):241-58.
Ulfig N (2002). Calcium-binding proteins in the human developing brain. Adv Anat Embryol Cell Biol. 165: III-IX, 1-92.

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