Recombinant Human Lim Domain-Binding Protein 3 (LDB3) Protein (GST)

Name: Recombinant Human Lim Domain-Binding Protein 3 (LDB3) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-09123P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Lim Domain-Binding Protein 3 (LDB3) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	O75112
Target Symbol	LDB3
Synonyms	CMD1C; CYPHER; HGNC:15710; KIAA01613; KIAA0613; Ldb3; LDB3_HUMAN; LDB3Z1; LDB3Z4; LIM domain binding 3; LIM domain binding protein 3; LIM domain-binding protein 3; LVNC3; ORACLE; PDLIM6; PDZ and LIM domain 6; Protein cypher; Z band alternatively spliced PDZ motif; Z band alternatively spliced PDZ motif protein; Z-band alternatively spliced PDZ-motif protein; ZASP
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MSYSVTLTGPGPWGFRLQGGKDFNMPLTISRITPGSKAAQSQLSQGDLVVAIDGVNTDTMTHLEAQNKIKSASYNLSLTLQKSKRPIPISTTAPPVQTPLPVIPHQKVVVNSPANADYQERFNPSALKDSALSTHKPIEVKGLGGKATIIHAQYNTPISMYSQDAIMDAIAGQAQAQGSDFSGSLPIKDLAVDSASPVYQAVIKSQNKPEDEADEWARRSSNLQSRSFRILAQMTGTEFMQDPDEEALRRSRERFETERNSPRFAKLRNWHHGLSAQILNVKS
Expression Range	1-283aa
Protein Length	Full Length of Isoform 6
Mol. Weight	58.0kDa
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	May function as an adapter in striated muscle to couple protein kinase C-mediated signaling via its LIM domains to the cytoskeleton.
Subcellular Location	Cytoplasm, perinuclear region. Cell projection, pseudopodium. Cytoplasm, cytoskeleton. Cytoplasm, myofibril, sarcomere, Z line. Note=Localized to the cytoplasm around nuclei and pseudopodia of undifferentiated cells and detected throughout the myotubes of differentiated cells. Colocalizes with ACTN2 at the Z-lines.
Database References	HGNC: 15710 OMIM: 601493 KEGG: hsa:11155 UniGene: Hs.657271
Associated Diseases	Cardiomyopathy, dilated 1C, with or without left ventricular non-compaction (CMD1C); Left ventricular non-compaction 3 (LVNC3); Myopathy, myofibrillar, 4 (MFM4)
Tissue Specificity	Expressed primarily in skeletal muscle and to a lesser extent in heart. Also detected in brain and placenta.

Gene Functions References

Interaction is demonstrated between ZASP and two new binding partners both of which have roles in signalling, regulation of gene expression and muscle differentiation; the mechanosensing protein Ankrd2 and the tumour suppressor protein p53. PMID: 24647531
p.(D117N) variant in Cypher/ZASP is not a causative mutation for dilated cardiomyopathy and ventricular arrhythmias. PMID: 26419279
A novel heterozygous missense mutation (p.N155H) in a highly conserved PDZ-like motif of ZASP was identified. The results indicate that typical ZASP-MFM presenting with late-onset distal myopathy is commonly associated with mutations in PDZ-like motif of ZASP. PMID: 27546599
The molecular basis for high-affinity binding of ZASP to G-Actin has been described. PMID: 28349680
this is the first family with Arrhythmogenic right ventricular cardiomyopathy where a mutation in LDB3 is associated with Arrhythmogenic right ventricular cardiomyopathy PMID: 25041374
Study identified abnormal inclusion of LDB3 exon 11 specific to myotonic dystrophy type at the RNA and protein level; inclusion changed the affinity of LDB3 for PKC, indicating that exon 11 may contribute to the activation of PKC in DM1 PMID: 24878509
results show that MFM-associated ZASP mutations in the actin-binding domain have deleterious effects on the core structure of the Z-discs in skeletal muscle. PMID: 24668811
Z-band alternatively spliced PDZ motif protein (ZASP) is the major O-linked beta-N-acetylglucosamine-substituted protein in human heart myofibrils PMID: 23271734
This results of this indicted that One patient harbored the missense mutation c.1719G>A (p.V566M) in the ZASP gene. PMID: 22349865
ZASP1 can form protein complex with telethonin/T-Cap and Na(v)1.5. The left ventricular noncompaction-specific ZASP1 mutation can cause loss of function of Na(v)1.5, without significant alteration of the cytoskeletal protein complex. PMID: 22929165
TNNT3 and LDB3 showed abnormal splicing and appeared more pronounced in myotonic dystrophies type 2 relative to myotonic dystrophies type 1. PMID: 20066428
the D626N mutation of Cypher/ZASP increases the affinity of the LIM domain for protein kinase C, which may be related to pathogenesis of dilated cardiomyopathy PMID: 14660611
ZASP/Cypher internal fragments containing either ZM exon 4 or 6 co-localized with alpha-actinin in cultured myoblasts and nonmuscle cells. PMID: 16476425
Tafazzins are essential during fetal and early post-natal life. PMID: 17394203
ZASP/Cypher anchors PGM1 to Z-disc under conditions of stress. The impaired binding of PGM1 to ZASP/Cypher might be involved in the pathogenesis of dilated cardiomyopathy. PMID: 19377068

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.