Recombinant Rat Calmodulin-1 (CALM1) Protein (His-SUMO&Myc)

Name: Recombinant Rat Calmodulin-1 (CALM1) Protein (His-SUMO&Myc)
Brand: Beta LifeScience
SKU: BLC-02832P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Rattus norvegicus (Rat) Calm1.

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Product Overview

Description	Recombinant Rat Calmodulin-1 (CALM1) Protein (His-SUMO&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P0DP29
Target Symbol	CALM1
Synonyms	Calm1; Calm; Cam; Cam1; CaMICalmodulin-1
Species	Rattus norvegicus (Rat)
Expression System	E.coli
Tag	N-6His-SUMO&C-Myc
Target Protein Sequence	ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK
Expression Range	2-149aa
Protein Length	Full Length of Mature Protein
Mol. Weight	34.2 kDa
Research Area	Signal Transduction
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis. Is a regulator of voltage-dependent L-type calcium channels. Mediates calcium-dependent inactivation of CACNA1C. Positively regulates calcium-activated potassium channel activity of KCNN2. Forms a potassium channel complex with KCNQ1 and regulates electrophysiological activity of the channel via calcium-binding. Acts as a sensor to modulate the endomplasmic reticulum contacts with other organelles mediated by VMP1:ATP2A2.
Subcellular Location	Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle pole. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.
Protein Families	Calmodulin family
Database References	KEGG: rno:24242 UniGene: PMID: 29279520 These results suggest a connection between Ca(2+)-signaling via excitation-contraction coupling and the regulation of STARS-mediated gene expression in muscles. PMID: 27132186 Hydrogen peroxide reduces calmodulin binding to RYR2 in rat cardiomyocytes. PMID: 26092277 Disruption of calmodulin binding to KCNQ2 also impairs enrichment of heteromeric KCNQ2/KCNQ3 channels at the axonal surface by blocking their trafficking from the endoplasmic reticulum to the axon. PMID: 25077630 Study reveals that apoCaM itself prominently regulates both voltage-gated Ca2+ and Na channels; ApoCaM binding to these channels enhances opening several-fold, matching the strongest forms of ion-channel regulation. PMID: 25417111 The molecular events underlying the association between CaM and Kv7.2 and their regulation by Ca(2+), was examined. PMID: 24489773 The study proposes that the structural basis of calcineurin activation by calmodulin is through displacement of the disordered fragment of the autoinhibitory domain which otherwise impedes active site access. PMID: 24018048 Recombinant small (SK2) calcium channel and calmodulin bind with three different stoichiometries that depend on the molar ratio of 2SKp/2CaM in solution. PMID: 24420768 CK2-mediated phosphorylation of calmodulin regulates the M-current, which is tonically regulated by CK2 and PP1 anchored to the KCNQ2 channel complex. PMID: 24627475 GRK5 nuclear translocation downstream of select Gq-activating hypertrophic ligands is a calmodulin-dependent process PMID: 23472081 Structural basis for the association of MAP6 protein with microtubules and its regulation by calmodulin. PMID: 23831686 Data indicate that the two distinct CaM/OLFp complexes existed simultaneously with stable structures. PMID: 22877078 structures of intact calmodulin (CaM)-free and CaM-bound endothelial nitric oxide synthase (eNOS) PMID: 23266515 Sustained Epac activation induces a strong positive inotropic effect relating to enhanced calcium signaling and increased expression of calmodulin. PMID: 22910094 Neurogranin targets calmodulin and lowers the threshold for the induction of long-term potentiation. PMID: 22848456 The crystal structure of a CaM.Orai1-calmodulin binding domain complex, is reported. PMID: 23109337 Cx32 is differentially phosphorylated and exists in a complex with SAP97 and CaM. PMID: 22718765 Calmodulin bound to the first IQ motif is responsible for calcium-dependent regulation of myosin 5a. PMID: 22437832 In PMCA-suppressed lines total CaM increased, and the calm I and calm II genes appeared to be responsible for this effect PMID: 21912933 Calmodulin facilitates endocytosis in an activity-dependent manner. PMID: 22184217 PKC and CaM protein expressions were downregulated in the hippocampus of neonatal rats exposed to lead. PMID: 19358756 Both the location and orientation of CaM binding on the RyR2 are very similar to the skeletal muscle RyR1 isoform. PMID: 22067155 PKC and CaM mRNA expression was downregulated in the hippocampus of baby rats with chronic lead exposure. PMID: 18761789 molecular mechanisms of the phosphorylation-dependent regulation of NHE1 PMID: 21931166 The present findings provide new insights on how MA interacts with CaM that may ultimately help in identification of the functional role of CaM-Gag interactions in the HIV replication cycle. PMID: 21799007 Ca(2+) influx regulates assembly of a fully active CaN-calmodulin complex selectively on the tail of dynIxb and the complex is recruited to sites of activity-dependent bulk endocytosis in nerve terminals PMID: 21730063 These results indicate that the aberrant formation of the activation link between CaMBD [(calmodulin)-binding domain] and CaMLD (CaM-like domain) of RyR is a key step in the development of hypertrophy in cultured cardiomyocytes. PMID: 21649588 Calcium/calmodulin interferes with the association of AKAP150 with TRPV1. PMID: 21569553 Data indicate that, in lactational rats, hippocampal neurogranin, CaMKII, calmodulin and calcineurin are involved in the brain impairment by developmental iodine deficiency and hypothyroidism. PMID: 20654708 The BD-N and BD-C2 binding domains are sufficient for CaM binding to the native channel and BD-C1 is unable to bind CaM independently. PMID: 20523736 translocation of CaM and CaMKII from the cytoplasm to the nucleus serves as messengers to transmit the pathogenic signal elicited in the surface membrane and in the RyR2 to the nuclear transcriptional sites to activate hypertrophy. PMID: 20433809 CaM acts as a mediator in the Ca2+-dependent modulation of KCNQ channels. PMID: 12032157 Calmodulin activity is critical for activation of volume-regulated anion channels in rat cerebral astrocytes. PMID: 15095369 the majority of CaM nuclear entry occurs by facilitated mechanisms in all cell types examined, in part by a Ca2+-independent and in part by a Ca2+-dependent translocation mechanism PMID: 15522886 the Ral-CaM complex defines a multifaceted regulatory mechanism for PLC-delta1 activation PMID: 15817490 binding of 14-3-3, calmodulin and calcium channel beta-subunits to Kir/Gem is mutually exclusive PMID: 15860732 These results explain how Calmodulin and iNOS coordinately function to form a stable complex that functions within the first 30 min following bacterial infection to upregulate the innate immune system involving macrophage activation. PMID: 16893173 Ca2+-dependent CaM cascade might contribute to NMDA induced activation of PI-3K/Akt pathway. PMID: 17492691 This study provides the first evidence that CaM and PKCdelta organize actin dynamics in the early endosomal compartment, thereby regulating the intracellular trafficking of EGFR. PMID: 17959830 analysis of conformational changes of calmodulin upon Ca2+ binding PMID: 18178620 The solution structures of complexes between calcium-saturated calmodulin (Ca (2+)/CaM) and a CaM-binding domain of the HIV-1 matrix protein p17 have been determined by small-angle X-ray scattering. PMID: 18553937 Diabetes-induced acceleration of I(to) current inactivation is due to a reduced effect of CaMKII on I(to) channels as a result of a diabetes-induced reduction in calmodulin protein expression. PMID: 19088444 In the intact SK channel complex, the N-lobe of calmodulin provides ligand-binding sites for channel gating, and that its ligand-binding properties are comparable to those of the N-lobe in isolated calmodulin. PMID: 19144926 The oxidation-induced loss of secondary structure, as measured by circular dichroism, correlated with the rate of degradation for wild-type and mutant calmodulin containing Leu substitutions in the C-terminus. PMID: 19231837 CaM bound to KCNQ2 acts as a Ca2+ sensor, conferring Ca2+ dependence to the trafficking of the channel to the plasma membrane and fully explaining the requirement of CaM binding for KCNQ2 function. PMID: 19494108

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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