Recombinant Mouse Disintegrin And Metalloproteinase Domain-Containing Protein 12 (ADAM12) Protein (His&Myc)

Name: Recombinant Mouse Disintegrin And Metalloproteinase Domain-Containing Protein 12 (ADAM12) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-08831P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: Enzymes, Featured enzyme molecules, Protease, Recombinant proteins

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Product Overview

Description	Recombinant Mouse Disintegrin And Metalloproteinase Domain-Containing Protein 12 (ADAM12) Protein (His&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q61824
Target Symbol	ADAM12
Synonyms	Adam12; MltnaDisintegrin and metalloproteinase domain-containing protein 12; ADAM 12; EC 3.4.24.-; Meltrin-alpha
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	ETLKMTKYVELVIVADNREFQRQGKDLEKVKQRLIEIANHVDKFYRPLNIRIVLVGVEVWNDIDKCSISQDPFTSLHEFLDWRKIKLLPRKSHDNAQLISGVYFQGTTIGMAPIMSMCTAEQSGGVVMDHSDSPLGAAVTLAHELGHNFGMNHDTLERGCSCRMAAEKGGCIMNPSTGFPFPMVFSSCSRKDLEASLEKGMGMCLFNLPEVKQAFGGRKCGNGYVEEGEECDCGEPEECTNRCCNATTCTLKPDAVCAHGQCCEDCQLKPPGTACRGSSNSCDLPEFCTGTAPHCPANVYLHDGHPCQGVDGYCYNGICQTHEQQCVTLWGPGAKPAPGICFERVNSAGDPYGNCGKDSKSAFAKCELRDAKCGKIQCQGGASRPVIGTNAVSIETNIPQQEGGRILCRGTHVYLGDDMPDPGLVLAGTKCAEGKICLNRRCQNISVFGVHKCAMQCHGRGVCNNRKNCHCEAHWAPPFCDKFGFGGSTDSGPIRQADNQG
Expression Range	206-706aa
Protein Length	Partial
Mol. Weight	61.4 kDa
Research Area	Cancer
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	Involved in skeletal muscle regeneration, specifically at the onset of cell fusion. Also involved in macrophage-derived giant cells (MGC) and osteoclast formation from mononuclear precursors.
Subcellular Location	Membrane; Single-pass type I membrane protein.
Database References	KEGG: mmu:11489 STRING: 10090.ENSMUSP00000065213 UniGene: Mm.439714
Tissue Specificity	Expressed during early developing mesenchymal cells that give rise to skeletal muscle, bones and visceral organs. Not expressed in adult normal muscle but expressed in regenerating muscle.

Gene Functions References

In conclusion, MiR29a regulates endothelial cell ADAM12 upregulation in ischemia and this is impaired in hyperglycemia. PMID: 28637396
It was concluded that TNF-alpha-induced changes in extracellular matix components increased expression of ADAM12 among other changes that were temporally related with the onset of myocyte function. PMID: 27487498
ADAM12 and ADAM17 are essential molecules for the impairment of barrier function of retinal vasculature under hypoxia. PMID: 26242473
Augmentation of ADAM12 expression in vivo improved outcomes in Balb/c mice, whereas knockdown of ADAM12 made outcomes worse in C57Bl/6 mice. In vitro, ADAM12 expression modulates endothelial cell proliferation, survival, and angiogenesis. PMID: 26163448
The effect of insulin-like growth factor-I on ADAM12 expression during the course of myogenesis is reported. PMID: 26975138
Nitric oxide synthase deficiency has differential effects on ADAM12 expression in growing mouse brain. PMID: 25892053
Inhibition of Erbb2 suppressed the increase in metalloproteinase ADAM12 expression in skin tumors. PMID: 24798404
TGF-beta stimulation of renal cells results in a significant up-regulation of Adams 10, 17, 12, and 19 PMID: 24103556
ADAM12 enhanced ephrin-A1 cleavage in response to transforming growth factor-betra1 in primary tumors. PMID: 23686306
The endogenous SnoN plays a role in regulating ADAM12 expression in response to TGFbeta1. PMID: 20457602
Adam12 is spatiotemporally expressed in decidualizing stromal cells in intact pregnant females and in pseudopregnant mice undergoing artificially induced decidualization. PMID: 19841944
properly folded mouse ADAM12, after passing a rate-limiting step of exit from the ER, is processed in the secretory pathway and reaches the cell surface, where it can mediate adhesion-mediated signaling PMID: 12000744
These observations suggest Meltrin alpha may be involved in regulating adipogenesis and myogenesis through a linked developmental pathway.We also report here the chromosomal locations of Meltrin alpha in the mouse PMID: 12482960
Adam12 overexpression in skeletal muscle results in compenstaion for dystrophin- deficiency by increasing alpha7 integrin, utrophin and associated glycoproteins. PMID: 12915458
Role of metalloproteinase disintegrin ADAM12 in determination of quiescent reserve cells during myogenic differentiation in vitro was studied. PMID: 12972593
involvement of meltrin alpha in the development of obesity and in adipogenic cell proliferation. PMID: 15637293
novel protein-protein interaction reported here involving the extracellular domain of ADAM12 may have important biological consequences during myoblast differentiation PMID: 15849365
observations suggest that a disintegrin and metalloproteinase (ADAM)-8,-9,-10,-12,-15,and -17 play an important role in mouse uterine tissue remodelling during the oestrous cycle PMID: 15907280
ADAM12 is a potential target for design of drugs that prevent carcinoma growth and is essential for tumor development and progression in the W10 mouse model for prostate cancer. PMID: 16607276
endogenous ADAM9 and/or ADAM12 present in wild type mouse embryonic fibroblasts contribute to Dll1 processing PMID: 17107962
Adam12 contributes to Tgfb signaling through interaction with the type II receptor. PMID: 17620406
ADAM12 seemed to inhibit the satellite cell response and delay myoblast differentiation. PMID: 17982130
Breast cancer-associated mutations interfere with the intracellular trafficking of ADAM12 and result in loss of the functional ADAM12 at the cell surface. PMID: 18241035
Agonist signaling of both hypertension and hypertrophy depends on posttranscriptional and transcriptional mechanisms that involve MMP-7, which is transcriptionally connected with ADAM-12 PMID: 19398663
Findings provide the first in vivo evidence that agonist-induced cardiac hypertrophy and fibrosis processes are signaled through TACE, which acts through novel pathways involving transcriptional regulation of ADAM-12 and MMP-2. PMID: 19581512

FAQs

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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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.