MCL1 Research Reagents

Induced myeloid leukemia cell differentiation protein Mcl-1 is a protein in humans that is encoded by MCL1 gene. 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 1 inhibits apoptosis. Isoform 2 promotes apoptosis.

The following MCL1 reagents supplied by CUSABIO are manufactured under a strict quality control system. Multiple applications have been validated and solid technical support is offered.

MCL1 Antibodies

MCL1 Antibodies for Mus musculus (Mouse)

MCL1 Antibodies for Homo sapiens (Human)

MCL1 Antibodies for Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

MCL1 Proteins

MCL1 Proteins for Rhodobacter sphaeroides (strain ATCC 17029 / ATH 2.4.9)

MCL1 Proteins for Rhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3)

MCL1 Proteins for Rhodobacter capsulatus (Rhodopseudomonas capsulata)

MCL1 Proteins for Rhodobacter sphaeroides (strain KD131 / KCTC 12085)

MCL1 Proteins for Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)

MCL1 Proteins for Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)

MCL1 Proteins for Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

MCL1 Proteins for Mus musculus (Mouse)

MCL1 Proteins for Felis catus (Cat) (Felis silvestris catus)

MCL1 Proteins for Canis lupus familiaris (Dog) (Canis familiaris)

MCL1 Background

Myeloid cell leukemia 1, encoded by the MCL1 gene, is an anti-apoptotic member of the Bcl-2 family [1]. The MCL1 protein was originally identified as an immediate-early gene expressed during PMA-induced differentiation of ML-1 myeloid leukemia cells [2]. Like its Bcl-2 relatives, MCL1 is ubiquitously expressed but has its particular tissue distribution [3][4] along with its specific physiological roles. Sequence analysis revealed that MCL1 contained 3 putative BH domains and its large N-terminal region included potential regulatory motifs that could be predicted to modulate its pro-survival function. Lack of the transmembrane domain in the C-terminal region of MCL1 blocks its membrane insertion and localization [5]. MCL1 is capable of heterodimerizing with other Bcl-2 family members due to the high structural and functional homology between its resides 170-300 and both Bcl-2 and Bcl-Xl [6]. Three studies exhibited that MCL1 is structurally similar to its pro-survival relatives, with a surface surface-exposed hydrophobic groove for the binding of other BH3 domain-containing proteins [7-9]. Mcl-1 binds and sequesters the pro-apoptotic proteins such as Bak and Bax, thus inhibiting apoptosis. And MCL1 also associates with and obstructs a subset of the BH3-only pro-apoptotic Bcl-2 family members, which induce the polymerization of Bak and Bax. The degradation of MCL1 can attenuate the suppression of Bak and Bax polymerization. MCL1's interaction with a second subset of the BH3-only pro-apoptotic Bcl-2 family members, which induce dissociation of Bak and Bax from Mcl-1, can also achieve the aim. Numerous diverse cell-types are reliant on MCL1 for their survival and development. For instance, MCL1 deletion is peri-implantation lethal in mouse embryogenesis [10]. MCL1 has also been shown to be required for the development and maintenance of B and T-lymphocytes [11] and is also required for neural development [12].

[1] Craig RW, Jabs EW, et al. Human and mouse chromosomal mapping of the myeloid cell leukemia-1 gene: MCL1 maps to human chromosome 1q21, a region that is frequently altered in preneoplastic and neoplastic disease [J]. Genomics. 1995, 23 (2): 457–63.
[2] Kozopas KM, Yang T, et al. MCL1, a gene expressed in programmed myeloid cell differentiation, has sequence similarity to BCL2[J]. Proc Natl Acad Sci U S A. 1993, 90 (8): 3516–20.
[3] T. Yang, K.M. Kozopas, et al. The intracellular distribution and pattern of expression of Mcl-1 overlap with, but are not identical to, those of Bcl-2 [J]. J. Cell Biol., 128 (6) (1995), pp. 1173-1184.
[4] S. Krajewski, et al. Immunohistochemical analysis of Mcl-1 protein in human tissues. Differential regulation of Mcl-1 and Bcl-2 protein production suggests a unique role for Mcl-1 in control of programmed cell death in vivo [J]. Am. J. Pathol., 146 (6) (1995), pp. 1309-1319.
[5] C. Akgul, et al. In vivo localisation and stability of human Mcl-1 using green fluorescent protein (GFP) fusion proteins [J]. FEBS Lett., 478 (1–2) (2000), pp. 72-76.
[6] R.J. Lutz. Role of the BH3 (Bcl-2 homology 3) domain in the regulation of apoptosis and Bcl-2-related proteins [J]. Biochem. Soc. Trans., 28 (2) (2000), pp. 51-56.
[7] C.L. Day, et al. Solution structure of prosurvival Mcl-1 and characterization of its binding by proapoptotic BH3-only ligands [J]. J. Biol. Chem., 280 (6) (2005), pp. 4738-4744.
[8] L. Chen, et al. Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function [J]. Mol. Cell, 17 (3) (2005), pp. 393-403.
[9] C.L. Day, et al. Structure of the BH3 domains from the p53-inducible BH3-only proteins Noxa and Puma in complex with Mcl-1 [J]. J. Mol. Biol., 380 (5) (2008), pp. 958-971.
[10] J.L. Rinkenberger, et al. Mcl-1 deficiency results in peri-implantation embryonic lethality [J]. Genes Dev., 14 (1) (2000), pp. 23-27.
[11] J.T. Opferman, et al. Development and maintenance of B and T lymphocytes requires antiapoptotic MCL-1 [J]. Nature, 426 (6967) (2003), pp. 671-676.
[12] N. Arbour, et al. Mcl-1 is a key regulator of apoptosis during CNS development and after DNA damage [J]. J. Neurosci., 28 (24) (2008), pp. 6068-6078.


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