Recombinant Mouse Induced Myeloid Leukemia Cell Differentiation Protein Mcl-1 Homolog (MCL1) Protein (His-SUMO)

Name: Recombinant Mouse Induced Myeloid Leukemia Cell Differentiation Protein Mcl-1 Homolog (MCL1) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-10236P
Availability: InStock

Greater than 90% 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 Mus musculus (Mouse) Mcl1.

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Product Overview

Description	Recombinant Mouse Induced Myeloid Leukemia Cell Differentiation Protein Mcl-1 Homolog (MCL1) Protein (His-SUMO) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P97287
Target Symbol	MCL1
Synonyms	Mcl1Induced myeloid leukemia cell differentiation protein Mcl-1 homolog; Bcl-2-related protein EAT/mcl1
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MFGLRRNAVIGLNLYCGGASLGAGGGSPAGARLVAEEAKARREGGGEAALLPGARVVARPPPVGAEDPDVTASAERRLHKSPGLLAVPPEEMAASAAAAIVSPEEELDGCEPEAIGKRPAVLPLLERVSEAAKSSGADGSLPSTPPPPEEEEDDLYRQSLEIISRYLREQATGSKDSKPLGEAGAAGRRALETLRRVGDGVQRNHETAFQGMLRKLDIKNEGDVKSFSRVMVHVFKDGVTNWGRIVTLISFGAFVAKHLKSVNQESFIEPLAETITDVLVRTKRDWLVKQRGWDGFVEFFHVQDLEGG
Expression Range	1-308aa
Protein Length	Partial
Mol. Weight	48.9kDa
Research Area	Others
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 the regulation of apoptosis versus cell survival, and in the maintenance of viability but not of proliferation. Mediates its effects by interactions with a number of other regulators of apoptosis. Isoform 2 has antiapoptotic activity.
Subcellular Location	Membrane; Single-pass membrane protein. Cytoplasm. Mitochondrion. Nucleus, nucleoplasm. Note=Cytoplasmic, associated with mitochondria.
Protein Families	Bcl-2 family
Database References	KEGG: mmu:17210 STRING: 10090.ENSMUSP00000044048 UniGene: PMID: 27913212 miR-29b suppressed cellular proliferation and promoted apoptosis of pulmonary artery smooth muscle cells, possibly through the inhibition of Mcl-1 and CCND2. PMID: 29662889 Authors treated Mcl-1(+/-) heterozygous mice, which have a ~50% reduction in MCL-1 protein in their cells, with a broad range of chemotherapeutic drugs. Monitoring of treated mice revealed that a wide range of chemotherapeutic drugs had no significant effect on the general well-being of Mcl-1(+/-) mice with no overt damage to a broad range of tissues. PMID: 28800129 analysis of how a hydrophobic staple induces an unanticipated structural rearrangement in Mcl-1 upon binding PMID: 29339518 Mcl-1 is a disease-specific target of Cdk5, which associates with Cdk5 under basal conditions, but is not regulated by it. PMID: 28751497 These findings elucidate a crucial molecular pathway of B cell selection in the earliest phases of activation by identifying a novel link between B cell receptor affinity and BAFF-R signaling towards Mcl-1. PMID: 27762293 Even though the Mcl-1 protein in Mcl1-flox-del homozygous animals is normal, the males were still infertile. PMID: 27906183 The findings support a model in which survival is determined by quantitative participation of multiple anti-apoptotic proteins, BCL2, Mcl1, and BCL2A1, rather than by a single anti-apoptotic protein. PMID: 28362427 This dynamic change in B cell survival mechanisms is unique to Epstein-Barr virus-infected cells and relies on regulation of MCL-1 mitochondrial localization and BFL-1 transcription by the viral EBNA3A protein. PMID: 28425914 Overexpression of Mcl-1 via the hemopoietic cell specific vavP-Mcl-1 transgene markedly exacerbates and accelerates the lpr phenotype. The progressive splenomegaly and lymphadenopathy displayed by lpr mice was far more severe in Mcl-1tg/lpr littermates PMID: 27813531 Endothelial cell -specific deletion of Mcl1 resulted in a dose-dependent increase in endothelial cell apoptosis in the angiogenic vasculature and a corresponding decline in vessel density. PMID: 26943318 Our findings indicate that MCL-1 expression is an important biomarker of TEC survival PMID: 28972012 These results identify MCL-1 as a critical prosurvival protein for preventing beta-cell death and clarify the mechanisms behind its downregulation by proinflammatory cytokines. PMID: 28667119 These data show that Mcl-1 is dispensable for the regulation of apoptosis during infection with different large DNA viruses.Bcl-XL, on the other hand, can be important to maintain survival of virus-infected cells PMID: 27537523 BCL-XL expression promotes survival of immature B cells, expression of BCL-2 is important for survival of mature B cells and long-lived plasma cells (PC), and expression of MCL-1 is important for survival throughout B-cell development. PMID: 27560714 miR-32/MCL-1 pathway members were identified as key early genetic events driving melanoma progression. PMID: 27846237 GSK3B-MCL1 signaling to regulate axonal autophagy might be important for the successful completion of Wallerian degeneration. PMID: 28053206 Specific downregulation of Mcl-1 significantly increases apoptosis of peritoneal macrophages and that the MAPK signaling pathway is the primary mediator of Mcl-1 expression. PMID: 26876933 MCL1 plays a pivotal role in Leydig-cell steroidogenesis, and might provide novel insights into metabolic regulation in this cell PMID: 26995740 Although loss of one Mcl-1 allele did not noticeably impair the survival of normal B lymphoid cells, it markedly diminished the survival of Proto-Oncogene Proteins c-myc overexpressing B cell progenitors. PMID: 26947081 MCL-1 loss in early B-lymphoid progenitors delayed MYC-driven lymphomagenesis. PMID: 26962682 High Mcl-1 levels enhanced mTOR phosphorylation and augmented the differentiation of terminal effector cells and effector memory CD8 T cells. PMID: 26855329 Data suggest Leishmania donovani exploits host anti-apoptotic protein MCL-1 to prevent apoptosis of host macrophages upon treatment with antiparasitic agents; thus, L. donovani protects its host, a factor in progression of visceral leishmaniasis. PMID: 26670606 Data demonstrate that soluble factors from MM cells are able to generate MDSC through Mcl-1 upregulation. PMID: 25871384 a mechanism of inverse coregulation between BECN1 and MCL1 significantly contributes to their opposing roles in tumorigenesis PMID: 25837021 There is a non-redundant pathway linking IL-15 to Mcl1 in the maintenance of NK cells and innate immune responses in vivo. PMID: 25119382 Authors recognize MCL-1 as the essential survival factor required for conservation of the postnatal PMF pool, growing follicle survival and effective oocyte mitochondrial function. PMID: 25950485 Tax interacted with and activated TRAF6, and triggered its mitochondrial localization, where it conjugated four carboxyl-terminal lysine residues of MCL-1 with lysine 63-linked polyubiquitin chains PMID: 25340740 deletion of Mir155 prevents Fas-induced hepatocyte apoptosis and liver injury through the up-regulation of Mcl1. PMID: 25794705 Inverse co-regulation of Beclin 1 and Mcl-1 represents a mechanism of functional counteraction in cancer. PMID: 25472497 miR-29a is involved in the pathogenesis of ulcerative colitis by regulating intestinal epithelial apoptosis via Mcl-1. PMID: 25674218 MCL1, but not that of BAK, forms stable heterodimeric complexes with cBID in a manner adjustable by membrane cardiolipin content and curvature degree. PMID: 25987560 MCL1 has lipid-dependent bimodal membrane activity. PMID: 25314294 These results demonstrate that antagonism between PUMA and MCL-1 constitutes the major axis of control of hematopoietic stem cell survival. PMID: 25847014 Cafestol overcomes ABT-737 resistance in Mcl-1-overexpressed renal carcinoma Caki cells through downregulation of Mcl-1 expression and upregulation of Bim expression. PMID: 25375379 These data demonstrate that Mcl-1 is essential for mammopoiesis and identify EGF as a critical trigger of Mcl-1 translation to ensure survival of milk-producing alveolar cells. PMID: 25730472 conditional gene deletion and loss of the granulocytic subset does not alter tumor growth or incidence in vivo PMID: 25500368 analysis of the role of BCL-XL or MCL-1 in the development and sustained growth of thymic lymphoma elicited by loss of p53 reveals that only MCL-1 is critical PMID: 25368374 Downregulation of Mcl-1 has anti-inflammatory pro-resolution effects and enhances bacterial clearance from the lung. PMID: 24280938 Pro-apoptotic Bim and anti-apoptotic Mcl-1. PMID: 24825007 Mcl-1 positively regulates cell viability and negatively regulates the bone-resorbing activity of osteoclasts both in vitro and in vivo. PMID: 24096094 Noxa is targeted to the mitochondrial membrane where it neutralises Mcl-1 via its C-terminal BH3-domain. PMID: 23733106 Data indicate that Mcl-1 deficient embryonic fibroblasts (MEFs) reliant only on Bcl-XL for survival, and Bax/Bak deficient MEFs support a mechanism-based induction of apoptosis. PMID: 23767404 mouse Mcl1 is a prosurvival Bcl2 relative that blunts stress-induced apoptosis, causes male sterility, and promotes tumorigenesis PMID: 24363325 Notch1 inhibits apoptosis of stimulated macrophages by directly controlling the mcl1 promoter. PMID: 23872918 Mcl-1 is critical for promoting effector T-cell responses, but does so by combating pro-apoptotic molecules beyond Bim. PMID: 23558951 Loss of parkin function through biallelic mutation of PARK2 may lead to death of dopaminergic neurons through unregulated SCF(Fbw7beta)-mediated ubiquitylation-dependent proteolysis of Mcl-1. PMID: 23858059 data support the metabolic control of Mcl-1 expression as a key event in the effects of caloric restriction in sensitizing lymphoma cells to apoptosis PMID: 23966420 Antiapoptotic Mcl-1 is critical for the survival and niche-filling capacity of Foxp3 regulatory T cells. PMID: 23852275 In the absence of p27(Kip1), Mcl1 failed to induce neural progenitor cell (NPC) cell cycle exit, demonstrating that p27(Kip1) is required for Mcl1-mediated NPC terminal mitosis. PMID: 23824576

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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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